CA2395838A1 - Acides nucleiques, proteines et anticorps - Google Patents
Acides nucleiques, proteines et anticorps Download PDFInfo
- Publication number
- CA2395838A1 CA2395838A1 CA 2395838 CA2395838A CA2395838A1 CA 2395838 A1 CA2395838 A1 CA 2395838A1 CA 2395838 CA2395838 CA 2395838 CA 2395838 A CA2395838 A CA 2395838A CA 2395838 A1 CA2395838 A1 CA 2395838A1
- Authority
- CA
- Canada
- Prior art keywords
- seq
- polypeptide
- sequence
- polynucleotide
- column
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Withdrawn
Links
- 102000004169 proteins and genes Human genes 0.000 title claims description 135
- 150000007523 nucleic acids Chemical class 0.000 title claims description 124
- 102000039446 nucleic acids Human genes 0.000 title claims description 92
- 108020004707 nucleic acids Proteins 0.000 title claims description 92
- 108091005461 Nucleic proteins Proteins 0.000 title description 2
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 585
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 568
- 229920001184 polypeptide Polymers 0.000 claims description 562
- 102000040430 polynucleotide Human genes 0.000 claims description 374
- 108091033319 polynucleotide Proteins 0.000 claims description 374
- 239000002157 polynucleotide Substances 0.000 claims description 373
- 108090000623 proteins and genes Proteins 0.000 claims description 186
- 239000012634 fragment Substances 0.000 claims description 150
- 239000002299 complementary DNA Substances 0.000 claims description 143
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 126
- 238000000034 method Methods 0.000 claims description 122
- 125000003729 nucleotide group Chemical group 0.000 claims description 109
- 239000002773 nucleotide Substances 0.000 claims description 105
- 150000001413 amino acids Chemical class 0.000 claims description 47
- 239000013598 vector Substances 0.000 claims description 39
- 230000000694 effects Effects 0.000 claims description 34
- 230000027455 binding Effects 0.000 claims description 33
- 230000014509 gene expression Effects 0.000 claims description 31
- 238000012217 deletion Methods 0.000 claims description 28
- 230000037430 deletion Effects 0.000 claims description 28
- 230000004071 biological effect Effects 0.000 claims description 26
- 238000004519 manufacturing process Methods 0.000 claims description 17
- 239000000047 product Substances 0.000 claims description 11
- 230000035772 mutation Effects 0.000 claims description 5
- 238000004166 bioassay Methods 0.000 claims description 3
- 239000012472 biological sample Substances 0.000 claims description 3
- 238000012258 culturing Methods 0.000 claims description 3
- 230000001575 pathological effect Effects 0.000 claims 8
- 239000006228 supernatant Substances 0.000 claims 2
- 241000282414 Homo sapiens Species 0.000 description 234
- 210000004027 cell Anatomy 0.000 description 189
- 235000018102 proteins Nutrition 0.000 description 126
- 206010028980 Neoplasm Diseases 0.000 description 97
- 230000000295 complement effect Effects 0.000 description 76
- 235000001014 amino acid Nutrition 0.000 description 68
- 108091028043 Nucleic acid sequence Proteins 0.000 description 53
- 125000005647 linker group Chemical group 0.000 description 53
- 229940024606 amino acid Drugs 0.000 description 51
- 210000004556 brain Anatomy 0.000 description 49
- 201000011510 cancer Diseases 0.000 description 49
- 210000001519 tissue Anatomy 0.000 description 46
- 206010061535 Ovarian neoplasm Diseases 0.000 description 44
- 210000001072 colon Anatomy 0.000 description 39
- 206010033128 Ovarian cancer Diseases 0.000 description 37
- 230000001605 fetal effect Effects 0.000 description 37
- 238000009396 hybridization Methods 0.000 description 36
- 229920001223 polyethylene glycol Polymers 0.000 description 35
- 210000001744 T-lymphocyte Anatomy 0.000 description 34
- 239000002202 Polyethylene glycol Substances 0.000 description 33
- 230000000890 antigenic effect Effects 0.000 description 32
- 108020004414 DNA Proteins 0.000 description 29
- 210000001672 ovary Anatomy 0.000 description 29
- -1 . allelic variants Proteins 0.000 description 28
- 210000003719 b-lymphocyte Anatomy 0.000 description 28
- 238000006467 substitution reaction Methods 0.000 description 28
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 27
- DQLATGHUWYMOKM-UHFFFAOYSA-L cisplatin Chemical compound N[Pt](N)(Cl)Cl DQLATGHUWYMOKM-UHFFFAOYSA-L 0.000 description 27
- 108020001507 fusion proteins Proteins 0.000 description 27
- 102000037865 fusion proteins Human genes 0.000 description 27
- 210000004072 lung Anatomy 0.000 description 26
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 24
- 125000000539 amino acid group Chemical group 0.000 description 24
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 24
- 210000002307 prostate Anatomy 0.000 description 23
- 230000005714 functional activity Effects 0.000 description 22
- 108700026244 Open Reading Frames Proteins 0.000 description 20
- 230000004048 modification Effects 0.000 description 20
- 238000012986 modification Methods 0.000 description 20
- 210000000481 breast Anatomy 0.000 description 19
- 102000005962 receptors Human genes 0.000 description 19
- 108020003175 receptors Proteins 0.000 description 19
- 210000002216 heart Anatomy 0.000 description 18
- 230000002163 immunogen Effects 0.000 description 18
- 210000004185 liver Anatomy 0.000 description 18
- 239000000523 sample Substances 0.000 description 18
- 108060003951 Immunoglobulin Proteins 0.000 description 17
- 208000009956 adenocarcinoma Diseases 0.000 description 17
- 239000000427 antigen Substances 0.000 description 17
- 102000018358 immunoglobulin Human genes 0.000 description 17
- 239000003446 ligand Substances 0.000 description 17
- 108091007433 antigens Proteins 0.000 description 16
- 102000036639 antigens Human genes 0.000 description 16
- 210000004369 blood Anatomy 0.000 description 16
- 201000010099 disease Diseases 0.000 description 16
- 210000003734 kidney Anatomy 0.000 description 16
- 230000015572 biosynthetic process Effects 0.000 description 15
- 239000008280 blood Substances 0.000 description 15
- 210000004899 c-terminal region Anatomy 0.000 description 15
- 238000006243 chemical reaction Methods 0.000 description 15
- 239000000203 mixture Substances 0.000 description 15
- 201000009030 Carcinoma Diseases 0.000 description 14
- 108091026890 Coding region Proteins 0.000 description 14
- 241000699666 Mus <mouse, genus> Species 0.000 description 14
- 238000000746 purification Methods 0.000 description 14
- 210000000952 spleen Anatomy 0.000 description 14
- 239000002253 acid Substances 0.000 description 13
- 238000003556 assay Methods 0.000 description 13
- 230000002759 chromosomal effect Effects 0.000 description 13
- 238000005516 engineering process Methods 0.000 description 13
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 12
- 208000029742 colonic neoplasm Diseases 0.000 description 12
- 210000004408 hybridoma Anatomy 0.000 description 12
- 210000003205 muscle Anatomy 0.000 description 12
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 12
- 210000001550 testis Anatomy 0.000 description 12
- 102000004127 Cytokines Human genes 0.000 description 11
- 108090000695 Cytokines Proteins 0.000 description 11
- 210000000601 blood cell Anatomy 0.000 description 11
- 239000000463 material Substances 0.000 description 11
- 230000002611 ovarian Effects 0.000 description 11
- 238000003752 polymerase chain reaction Methods 0.000 description 11
- 230000008569 process Effects 0.000 description 11
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 10
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 238000005755 formation reaction Methods 0.000 description 10
- 210000002741 palatine tonsil Anatomy 0.000 description 10
- 210000002826 placenta Anatomy 0.000 description 10
- 241001465754 Metazoa Species 0.000 description 9
- 238000004590 computer program Methods 0.000 description 9
- 230000006870 function Effects 0.000 description 9
- 230000004927 fusion Effects 0.000 description 9
- 210000000496 pancreas Anatomy 0.000 description 9
- 238000002360 preparation method Methods 0.000 description 9
- 239000000126 substance Substances 0.000 description 9
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 8
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 8
- 238000007792 addition Methods 0.000 description 8
- 210000001185 bone marrow Anatomy 0.000 description 8
- 239000003814 drug Substances 0.000 description 8
- 210000004907 gland Anatomy 0.000 description 8
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 8
- 230000028993 immune response Effects 0.000 description 8
- 238000003018 immunoassay Methods 0.000 description 8
- 230000001817 pituitary effect Effects 0.000 description 8
- 230000000284 resting effect Effects 0.000 description 8
- 210000002536 stromal cell Anatomy 0.000 description 8
- 238000012360 testing method Methods 0.000 description 8
- 238000013519 translation Methods 0.000 description 8
- 241000588724 Escherichia coli Species 0.000 description 7
- 102000008100 Human Serum Albumin Human genes 0.000 description 7
- 108091006905 Human Serum Albumin Proteins 0.000 description 7
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 7
- 206010039491 Sarcoma Diseases 0.000 description 7
- 239000000556 agonist Substances 0.000 description 7
- 208000035475 disorder Diseases 0.000 description 7
- 229940079593 drug Drugs 0.000 description 7
- 230000003511 endothelial effect Effects 0.000 description 7
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 7
- 229910052760 oxygen Inorganic materials 0.000 description 7
- 239000013612 plasmid Substances 0.000 description 7
- 238000012545 processing Methods 0.000 description 7
- 210000002966 serum Anatomy 0.000 description 7
- 238000003786 synthesis reaction Methods 0.000 description 7
- 210000001541 thymus gland Anatomy 0.000 description 7
- 206010006187 Breast cancer Diseases 0.000 description 6
- 208000026310 Breast neoplasm Diseases 0.000 description 6
- 206010009944 Colon cancer Diseases 0.000 description 6
- 241000235648 Pichia Species 0.000 description 6
- 230000021736 acetylation Effects 0.000 description 6
- 238000006640 acetylation reaction Methods 0.000 description 6
- 230000004913 activation Effects 0.000 description 6
- 239000005557 antagonist Substances 0.000 description 6
- 230000000903 blocking effect Effects 0.000 description 6
- 210000000988 bone and bone Anatomy 0.000 description 6
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 6
- 239000003153 chemical reaction reagent Substances 0.000 description 6
- 125000004122 cyclic group Chemical group 0.000 description 6
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 6
- 235000018417 cysteine Nutrition 0.000 description 6
- 210000002458 fetal heart Anatomy 0.000 description 6
- 230000002068 genetic effect Effects 0.000 description 6
- 230000002209 hydrophobic effect Effects 0.000 description 6
- 210000002540 macrophage Anatomy 0.000 description 6
- 230000001404 mediated effect Effects 0.000 description 6
- 108020004999 messenger RNA Proteins 0.000 description 6
- 230000006320 pegylation Effects 0.000 description 6
- 230000000717 retained effect Effects 0.000 description 6
- 210000001525 retina Anatomy 0.000 description 6
- 210000003491 skin Anatomy 0.000 description 6
- 239000000243 solution Substances 0.000 description 6
- 210000002784 stomach Anatomy 0.000 description 6
- 210000003462 vein Anatomy 0.000 description 6
- 102000009027 Albumins Human genes 0.000 description 5
- 108010088751 Albumins Proteins 0.000 description 5
- 108010025188 Alcohol oxidase Proteins 0.000 description 5
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 5
- 102100031573 Hematopoietic progenitor cell antigen CD34 Human genes 0.000 description 5
- 101000777663 Homo sapiens Hematopoietic progenitor cell antigen CD34 Proteins 0.000 description 5
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 5
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 5
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 5
- 108091034117 Oligonucleotide Proteins 0.000 description 5
- 241000283973 Oryctolagus cuniculus Species 0.000 description 5
- 150000007513 acids Chemical class 0.000 description 5
- 239000002671 adjuvant Substances 0.000 description 5
- 230000004075 alteration Effects 0.000 description 5
- 229960000723 ampicillin Drugs 0.000 description 5
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 5
- 230000000692 anti-sense effect Effects 0.000 description 5
- 210000002449 bone cell Anatomy 0.000 description 5
- 238000007385 chemical modification Methods 0.000 description 5
- 238000003745 diagnosis Methods 0.000 description 5
- 230000002357 endometrial effect Effects 0.000 description 5
- 239000013604 expression vector Substances 0.000 description 5
- 210000002950 fibroblast Anatomy 0.000 description 5
- 229940088597 hormone Drugs 0.000 description 5
- 239000005556 hormone Substances 0.000 description 5
- 210000000987 immune system Anatomy 0.000 description 5
- 230000003053 immunization Effects 0.000 description 5
- 210000000936 intestine Anatomy 0.000 description 5
- 210000000265 leukocyte Anatomy 0.000 description 5
- 230000000670 limiting effect Effects 0.000 description 5
- 150000002632 lipids Chemical class 0.000 description 5
- 210000001161 mammalian embryo Anatomy 0.000 description 5
- 201000001441 melanoma Diseases 0.000 description 5
- 230000001394 metastastic effect Effects 0.000 description 5
- 206010061289 metastatic neoplasm Diseases 0.000 description 5
- 230000002969 morbid Effects 0.000 description 5
- 210000001577 neostriatum Anatomy 0.000 description 5
- 210000000440 neutrophil Anatomy 0.000 description 5
- 230000026731 phosphorylation Effects 0.000 description 5
- 238000006366 phosphorylation reaction Methods 0.000 description 5
- 230000001323 posttranslational effect Effects 0.000 description 5
- 238000010188 recombinant method Methods 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 238000012163 sequencing technique Methods 0.000 description 5
- 210000002460 smooth muscle Anatomy 0.000 description 5
- 241000894007 species Species 0.000 description 5
- 238000002560 therapeutic procedure Methods 0.000 description 5
- 230000009466 transformation Effects 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- 241000894006 Bacteria Species 0.000 description 4
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 4
- 102000014914 Carrier Proteins Human genes 0.000 description 4
- 108010078791 Carrier Proteins Proteins 0.000 description 4
- 108020004705 Codon Proteins 0.000 description 4
- 108020004635 Complementary DNA Proteins 0.000 description 4
- 206010012289 Dementia Diseases 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- 241000699670 Mus sp. Species 0.000 description 4
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 4
- 108091006006 PEGylated Proteins Proteins 0.000 description 4
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 4
- 206010035226 Plasma cell myeloma Diseases 0.000 description 4
- 101710086015 RNA ligase Proteins 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 240000008042 Zea mays Species 0.000 description 4
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 4
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 4
- 230000001919 adrenal effect Effects 0.000 description 4
- 230000009435 amidation Effects 0.000 description 4
- 238000007112 amidation reaction Methods 0.000 description 4
- 230000002788 anti-peptide Effects 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 210000001772 blood platelet Anatomy 0.000 description 4
- 229910052799 carbon Inorganic materials 0.000 description 4
- 210000000845 cartilage Anatomy 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 230000001413 cellular effect Effects 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 239000002738 chelating agent Substances 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 150000001875 compounds Chemical class 0.000 description 4
- 238000002591 computed tomography Methods 0.000 description 4
- 235000005822 corn Nutrition 0.000 description 4
- 238000012937 correction Methods 0.000 description 4
- 238000001212 derivatisation Methods 0.000 description 4
- 238000001514 detection method Methods 0.000 description 4
- 238000002405 diagnostic procedure Methods 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 210000003743 erythrocyte Anatomy 0.000 description 4
- 210000003527 eukaryotic cell Anatomy 0.000 description 4
- 230000003325 follicular Effects 0.000 description 4
- 230000022244 formylation Effects 0.000 description 4
- 238000006170 formylation reaction Methods 0.000 description 4
- 238000002873 global sequence alignment Methods 0.000 description 4
- 230000013595 glycosylation Effects 0.000 description 4
- 238000006206 glycosylation reaction Methods 0.000 description 4
- 230000035876 healing Effects 0.000 description 4
- 230000011132 hemopoiesis Effects 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 238000002649 immunization Methods 0.000 description 4
- 230000005847 immunogenicity Effects 0.000 description 4
- 229940072221 immunoglobulins Drugs 0.000 description 4
- 238000000338 in vitro Methods 0.000 description 4
- 238000001727 in vivo Methods 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 208000032839 leukemia Diseases 0.000 description 4
- 235000018977 lysine Nutrition 0.000 description 4
- 239000003550 marker Substances 0.000 description 4
- 201000000050 myeloid neoplasm Diseases 0.000 description 4
- 229910052757 nitrogen Inorganic materials 0.000 description 4
- 210000000056 organ Anatomy 0.000 description 4
- 230000003647 oxidation Effects 0.000 description 4
- 238000007254 oxidation reaction Methods 0.000 description 4
- 230000004853 protein function Effects 0.000 description 4
- 230000003248 secreting effect Effects 0.000 description 4
- 238000002864 sequence alignment Methods 0.000 description 4
- 230000004936 stimulating effect Effects 0.000 description 4
- 238000010189 synthetic method Methods 0.000 description 4
- 238000011282 treatment Methods 0.000 description 4
- 239000013638 trimer Substances 0.000 description 4
- 238000010798 ubiquitination Methods 0.000 description 4
- 230000034512 ubiquitination Effects 0.000 description 4
- 210000004291 uterus Anatomy 0.000 description 4
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 3
- 241000972773 Aulopiformes Species 0.000 description 3
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 3
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 3
- 102000053602 DNA Human genes 0.000 description 3
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 3
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 3
- 101001063991 Homo sapiens Leptin Proteins 0.000 description 3
- 102000003839 Human Proteins Human genes 0.000 description 3
- 108090000144 Human Proteins Proteins 0.000 description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 3
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 3
- 102000000589 Interleukin-1 Human genes 0.000 description 3
- 108010002352 Interleukin-1 Proteins 0.000 description 3
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 3
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 3
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 3
- 206010025323 Lymphomas Diseases 0.000 description 3
- 101000941356 Nostoc ellipsosporum Cyanovirin-N Proteins 0.000 description 3
- 208000001715 Osteoblastoma Diseases 0.000 description 3
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 3
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 108010076504 Protein Sorting Signals Proteins 0.000 description 3
- WDLRUFUQRNWCPK-UHFFFAOYSA-N Tetraxetan Chemical compound OC(=O)CN1CCN(CC(O)=O)CCN(CC(O)=O)CCN(CC(O)=O)CC1 WDLRUFUQRNWCPK-UHFFFAOYSA-N 0.000 description 3
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 3
- 206010052428 Wound Diseases 0.000 description 3
- 208000027418 Wounds and injury Diseases 0.000 description 3
- 210000001789 adipocyte Anatomy 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- QWCKQJZIFLGMSD-UHFFFAOYSA-N alpha-aminobutyric acid Chemical compound CCC(N)C(O)=O QWCKQJZIFLGMSD-UHFFFAOYSA-N 0.000 description 3
- 125000003277 amino group Chemical group 0.000 description 3
- 208000007502 anemia Diseases 0.000 description 3
- 235000003704 aspartic acid Nutrition 0.000 description 3
- 230000008901 benefit Effects 0.000 description 3
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 3
- 230000008827 biological function Effects 0.000 description 3
- 239000003114 blood coagulation factor Substances 0.000 description 3
- 210000000349 chromosome Anatomy 0.000 description 3
- 238000003776 cleavage reaction Methods 0.000 description 3
- 238000004132 cross linking Methods 0.000 description 3
- 230000009260 cross reactivity Effects 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 235000013922 glutamic acid Nutrition 0.000 description 3
- 239000004220 glutamic acid Substances 0.000 description 3
- 210000004013 groin Anatomy 0.000 description 3
- 239000003102 growth factor Substances 0.000 description 3
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 3
- 235000014304 histidine Nutrition 0.000 description 3
- 239000000710 homodimer Substances 0.000 description 3
- 102000049953 human LEP Human genes 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 230000001976 improved effect Effects 0.000 description 3
- 230000001965 increasing effect Effects 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 150000002500 ions Chemical class 0.000 description 3
- 210000000867 larynx Anatomy 0.000 description 3
- 210000001165 lymph node Anatomy 0.000 description 3
- 210000004698 lymphocyte Anatomy 0.000 description 3
- 230000003211 malignant effect Effects 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 230000002503 metabolic effect Effects 0.000 description 3
- 229930182817 methionine Natural products 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 238000002887 multiple sequence alignment Methods 0.000 description 3
- 210000003254 palate Anatomy 0.000 description 3
- 210000002381 plasma Anatomy 0.000 description 3
- 239000013600 plasmid vector Substances 0.000 description 3
- 230000006337 proteolytic cleavage Effects 0.000 description 3
- 230000006798 recombination Effects 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 230000001177 retroviral effect Effects 0.000 description 3
- 238000010839 reverse transcription Methods 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 235000019515 salmon Nutrition 0.000 description 3
- 230000007017 scission Effects 0.000 description 3
- 239000007787 solid Substances 0.000 description 3
- 210000004988 splenocyte Anatomy 0.000 description 3
- 210000000130 stem cell Anatomy 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- CXCHEKCRJQRVNG-UHFFFAOYSA-N 2,2,2-trifluoroethanesulfonyl chloride Chemical compound FC(F)(F)CS(Cl)(=O)=O CXCHEKCRJQRVNG-UHFFFAOYSA-N 0.000 description 2
- FUOOLUPWFVMBKG-UHFFFAOYSA-N 2-Aminoisobutyric acid Chemical compound CC(C)(N)C(O)=O FUOOLUPWFVMBKG-UHFFFAOYSA-N 0.000 description 2
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 2
- 230000005730 ADP ribosylation Effects 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 206010005949 Bone cancer Diseases 0.000 description 2
- 208000018084 Bone neoplasm Diseases 0.000 description 2
- 101100230428 Caenorhabditis elegans hil-5 gene Proteins 0.000 description 2
- 241000282461 Canis lupus Species 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 241000282326 Felis catus Species 0.000 description 2
- PXGOKWXKJXAPGV-UHFFFAOYSA-N Fluorine Chemical compound FF PXGOKWXKJXAPGV-UHFFFAOYSA-N 0.000 description 2
- 208000002966 Giant Cell Tumor of Bone Diseases 0.000 description 2
- 101710154606 Hemagglutinin Proteins 0.000 description 2
- 208000009292 Hemophilia A Diseases 0.000 description 2
- 241000238631 Hexapoda Species 0.000 description 2
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 2
- 208000029462 Immunodeficiency disease Diseases 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- 102000012214 Immunoproteins Human genes 0.000 description 2
- 108010036650 Immunoproteins Proteins 0.000 description 2
- 102000004877 Insulin Human genes 0.000 description 2
- 108090001061 Insulin Proteins 0.000 description 2
- 108010002386 Interleukin-3 Proteins 0.000 description 2
- 102000000646 Interleukin-3 Human genes 0.000 description 2
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 2
- 102100020880 Kit ligand Human genes 0.000 description 2
- 241000235058 Komagataella pastoris Species 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 108090001090 Lectins Proteins 0.000 description 2
- 102000004856 Lectins Human genes 0.000 description 2
- 241000408529 Libra Species 0.000 description 2
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 2
- 102000007651 Macrophage Colony-Stimulating Factor Human genes 0.000 description 2
- 108010046938 Macrophage Colony-Stimulating Factor Proteins 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 206010026749 Mania Diseases 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- RSPISYXLHRIGJD-UHFFFAOYSA-N OOOO Chemical compound OOOO RSPISYXLHRIGJD-UHFFFAOYSA-N 0.000 description 2
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 2
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- 241000282320 Panthera leo Species 0.000 description 2
- 108090000526 Papain Proteins 0.000 description 2
- 101710176177 Protein A56 Proteins 0.000 description 2
- 108010029485 Protein Isoforms Proteins 0.000 description 2
- 102000001708 Protein Isoforms Human genes 0.000 description 2
- 108010007127 Pulmonary Surfactant-Associated Protein D Proteins 0.000 description 2
- 102100027845 Pulmonary surfactant-associated protein D Human genes 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 2
- 208000034189 Sclerosis Diseases 0.000 description 2
- 102000007562 Serum Albumin Human genes 0.000 description 2
- 108010071390 Serum Albumin Proteins 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 108091081024 Start codon Proteins 0.000 description 2
- 208000037065 Subacute sclerosing leukoencephalitis Diseases 0.000 description 2
- 206010042297 Subacute sclerosing panencephalitis Diseases 0.000 description 2
- 108010092262 T-Cell Antigen Receptors Proteins 0.000 description 2
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 2
- 108090000190 Thrombin Proteins 0.000 description 2
- 108020004566 Transfer RNA Proteins 0.000 description 2
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 2
- 102100040247 Tumor necrosis factor Human genes 0.000 description 2
- YJQCOFNZVFGCAF-UHFFFAOYSA-N Tunicamycin II Natural products O1C(CC(O)C2C(C(O)C(O2)N2C(NC(=O)C=C2)=O)O)C(O)C(O)C(NC(=O)C=CCCCCCCCCC(C)C)C1OC1OC(CO)C(O)C(O)C1NC(C)=O YJQCOFNZVFGCAF-UHFFFAOYSA-N 0.000 description 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 2
- 230000010933 acylation Effects 0.000 description 2
- 238000005917 acylation reaction Methods 0.000 description 2
- 238000007818 agglutination assay Methods 0.000 description 2
- 230000002776 aggregation Effects 0.000 description 2
- 238000004220 aggregation Methods 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 238000005571 anion exchange chromatography Methods 0.000 description 2
- 150000001450 anions Chemical class 0.000 description 2
- 230000005875 antibody response Effects 0.000 description 2
- 230000010516 arginylation Effects 0.000 description 2
- 210000001367 artery Anatomy 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- UCMIRNVEIXFBKS-UHFFFAOYSA-N beta-alanine Chemical compound NCCC(O)=O UCMIRNVEIXFBKS-UHFFFAOYSA-N 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- HRURXKIZWNSHQB-UHFFFAOYSA-N bis(trifluoromethylsulfonyl)azanide;cobalt(2+) Chemical compound [Co+2].FC(F)(F)S(=O)(=O)[N-]S(=O)(=O)C(F)(F)F.FC(F)(F)S(=O)(=O)[N-]S(=O)(=O)C(F)(F)F HRURXKIZWNSHQB-UHFFFAOYSA-N 0.000 description 2
- 239000003130 blood coagulation factor inhibitor Substances 0.000 description 2
- 238000006664 bond formation reaction Methods 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 208000035269 cancer or benign tumor Diseases 0.000 description 2
- 150000001720 carbohydrates Chemical group 0.000 description 2
- 208000002458 carcinoid tumor Diseases 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000005277 cation exchange chromatography Methods 0.000 description 2
- 210000001638 cerebellum Anatomy 0.000 description 2
- 230000001684 chronic effect Effects 0.000 description 2
- 230000008878 coupling Effects 0.000 description 2
- 238000010168 coupling process Methods 0.000 description 2
- 238000005859 coupling reaction Methods 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- XVOYSCVBGLVSOL-UHFFFAOYSA-N cysteic acid Chemical compound OC(=O)C(N)CS(O)(=O)=O XVOYSCVBGLVSOL-UHFFFAOYSA-N 0.000 description 2
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 2
- 230000017858 demethylation Effects 0.000 description 2
- 238000010520 demethylation reaction Methods 0.000 description 2
- 210000004443 dendritic cell Anatomy 0.000 description 2
- 229960002086 dextran Drugs 0.000 description 2
- 206010012601 diabetes mellitus Diseases 0.000 description 2
- 230000004069 differentiation Effects 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 210000004696 endometrium Anatomy 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 230000002708 enhancing effect Effects 0.000 description 2
- 230000001037 epileptic effect Effects 0.000 description 2
- 210000000981 epithelium Anatomy 0.000 description 2
- 238000012869 ethanol precipitation Methods 0.000 description 2
- 230000001747 exhibiting effect Effects 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 210000004700 fetal blood Anatomy 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 2
- 210000001652 frontal lobe Anatomy 0.000 description 2
- BTCSSZJGUNDROE-UHFFFAOYSA-N gamma-aminobutyric acid Chemical compound NCCCC(O)=O BTCSSZJGUNDROE-UHFFFAOYSA-N 0.000 description 2
- 230000006251 gamma-carboxylation Effects 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 125000003827 glycol group Chemical group 0.000 description 2
- 210000003714 granulocyte Anatomy 0.000 description 2
- 150000003278 haem Chemical group 0.000 description 2
- 230000003394 haemopoietic effect Effects 0.000 description 2
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 2
- 239000000833 heterodimer Substances 0.000 description 2
- 125000000487 histidyl group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C([H])=N1 0.000 description 2
- 238000002744 homologous recombination Methods 0.000 description 2
- 230000006801 homologous recombination Effects 0.000 description 2
- 210000005260 human cell Anatomy 0.000 description 2
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 2
- 230000033444 hydroxylation Effects 0.000 description 2
- 238000005805 hydroxylation reaction Methods 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 238000007901 in situ hybridization Methods 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 229940125396 insulin Drugs 0.000 description 2
- 230000026045 iodination Effects 0.000 description 2
- 238000006192 iodination reaction Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- 238000005304 joining Methods 0.000 description 2
- 210000002510 keratinocyte Anatomy 0.000 description 2
- 210000003246 kidney medulla Anatomy 0.000 description 2
- 239000002523 lectin Substances 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 238000004020 luminiscence type Methods 0.000 description 2
- 210000002751 lymph Anatomy 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 238000013507 mapping Methods 0.000 description 2
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 2
- 230000011987 methylation Effects 0.000 description 2
- 238000007069 methylation reaction Methods 0.000 description 2
- 210000001616 monocyte Anatomy 0.000 description 2
- DNIAPMSPPWPWGF-UHFFFAOYSA-N monopropylene glycol Natural products CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 2
- 210000000066 myeloid cell Anatomy 0.000 description 2
- 230000007498 myristoylation Effects 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 210000002569 neuron Anatomy 0.000 description 2
- 230000003472 neutralizing effect Effects 0.000 description 2
- 238000010606 normalization Methods 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229940055729 papain Drugs 0.000 description 2
- 235000019834 papain Nutrition 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 239000000813 peptide hormone Substances 0.000 description 2
- 238000002823 phage display Methods 0.000 description 2
- 210000003800 pharynx Anatomy 0.000 description 2
- 125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 2
- 229940080469 phosphocellulose Drugs 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 230000013823 prenylation Effects 0.000 description 2
- 210000005267 prostate cell Anatomy 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 229940043131 pyroglutamate Drugs 0.000 description 2
- 230000006340 racemization Effects 0.000 description 2
- 238000002708 random mutagenesis Methods 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000010076 replication Effects 0.000 description 2
- 238000007363 ring formation reaction Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- FSYKKLYZXJSNPZ-UHFFFAOYSA-N sarcosine Chemical compound C[NH2+]CC([O-])=O FSYKKLYZXJSNPZ-UHFFFAOYSA-N 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 230000011664 signaling Effects 0.000 description 2
- 210000002027 skeletal muscle Anatomy 0.000 description 2
- 229910000162 sodium phosphate Inorganic materials 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 230000019635 sulfation Effects 0.000 description 2
- 238000005670 sulfation reaction Methods 0.000 description 2
- 210000001258 synovial membrane Anatomy 0.000 description 2
- 201000004595 synovitis Diseases 0.000 description 2
- 210000000538 tail Anatomy 0.000 description 2
- 208000001608 teratocarcinoma Diseases 0.000 description 2
- 229960004072 thrombin Drugs 0.000 description 2
- 210000001685 thyroid gland Anatomy 0.000 description 2
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 2
- ZHSGGJXRNHWHRS-VIDYELAYSA-N tunicamycin Chemical compound O([C@H]1[C@@H]([C@H]([C@@H](O)[C@@H](CC(O)[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C(NC(=O)C=C2)=O)O)O1)O)NC(=O)/C=C/CC(C)C)[C@H]1O[C@H](CO)[C@@H](O)[C@H](O)[C@H]1NC(C)=O ZHSGGJXRNHWHRS-VIDYELAYSA-N 0.000 description 2
- MEYZYGMYMLNUHJ-UHFFFAOYSA-N tunicamycin Natural products CC(C)CCCCCCCCCC=CC(=O)NC1C(O)C(O)C(CC(O)C2OC(C(O)C2O)N3C=CC(=O)NC3=O)OC1OC4OC(CO)C(O)C(O)C4NC(=O)C MEYZYGMYMLNUHJ-UHFFFAOYSA-N 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 230000029663 wound healing Effects 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- BVAUMRCGVHUWOZ-ZETCQYMHSA-N (2s)-2-(cyclohexylazaniumyl)propanoate Chemical compound OC(=O)[C@H](C)NC1CCCCC1 BVAUMRCGVHUWOZ-ZETCQYMHSA-N 0.000 description 1
- MRTPISKDZDHEQI-YFKPBYRVSA-N (2s)-2-(tert-butylamino)propanoic acid Chemical compound OC(=O)[C@H](C)NC(C)(C)C MRTPISKDZDHEQI-YFKPBYRVSA-N 0.000 description 1
- NPDBDJFLKKQMCM-SCSAIBSYSA-N (2s)-2-amino-3,3-dimethylbutanoic acid Chemical compound CC(C)(C)[C@H](N)C(O)=O NPDBDJFLKKQMCM-SCSAIBSYSA-N 0.000 description 1
- ASWBNKHCZGQVJV-UHFFFAOYSA-N (3-hexadecanoyloxy-2-hydroxypropyl) 2-(trimethylazaniumyl)ethyl phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OCC(O)COP([O-])(=O)OCC[N+](C)(C)C ASWBNKHCZGQVJV-UHFFFAOYSA-N 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- VOXZDWNPVJITMN-ZBRFXRBCSA-N 17β-estradiol Chemical compound OC1=CC=C2[C@H]3CC[C@](C)([C@H](CC4)O)[C@@H]4[C@@H]3CCC2=C1 VOXZDWNPVJITMN-ZBRFXRBCSA-N 0.000 description 1
- OGNSCSPNOLGXSM-UHFFFAOYSA-N 2,4-diaminobutyric acid Chemical compound NCCC(N)C(O)=O OGNSCSPNOLGXSM-UHFFFAOYSA-N 0.000 description 1
- UFBJCMHMOXMLKC-UHFFFAOYSA-N 2,4-dinitrophenol Chemical compound OC1=CC=C([N+]([O-])=O)C=C1[N+]([O-])=O UFBJCMHMOXMLKC-UHFFFAOYSA-N 0.000 description 1
- QRYXYRQPMWQIDM-UHFFFAOYSA-N 3-benzoyl-3-(2,5-dioxopyrrol-1-yl)-1-hydroxypyrrolidine-2,5-dione Chemical compound O=C1N(O)C(=O)CC1(C(=O)C=1C=CC=CC=1)N1C(=O)C=CC1=O QRYXYRQPMWQIDM-UHFFFAOYSA-N 0.000 description 1
- ZLOIGESWDJYCTF-XVFCMESISA-N 4-thiouridine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=S)C=C1 ZLOIGESWDJYCTF-XVFCMESISA-N 0.000 description 1
- SLXKOJJOQWFEFD-UHFFFAOYSA-N 6-aminohexanoic acid Chemical compound NCCCCCC(O)=O SLXKOJJOQWFEFD-UHFFFAOYSA-N 0.000 description 1
- CJIJXIFQYOPWTF-UHFFFAOYSA-N 7-hydroxycoumarin Natural products O1C(=O)C=CC2=CC(O)=CC=C21 CJIJXIFQYOPWTF-UHFFFAOYSA-N 0.000 description 1
- ZCYVEMRRCGMTRW-UHFFFAOYSA-N 7553-56-2 Chemical compound [I] ZCYVEMRRCGMTRW-UHFFFAOYSA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- 208000010507 Adenocarcinoma of Lung Diseases 0.000 description 1
- 206010052747 Adenocarcinoma pancreas Diseases 0.000 description 1
- 108010000239 Aequorin Proteins 0.000 description 1
- 241000234282 Allium Species 0.000 description 1
- 108010064733 Angiotensins Proteins 0.000 description 1
- 102000015427 Angiotensins Human genes 0.000 description 1
- 108090000935 Antithrombin III Proteins 0.000 description 1
- 102000004411 Antithrombin III Human genes 0.000 description 1
- 206010003445 Ascites Diseases 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 206010061728 Bone lesion Diseases 0.000 description 1
- 101800004538 Bradykinin Proteins 0.000 description 1
- 102400000967 Bradykinin Human genes 0.000 description 1
- 102100032367 C-C motif chemokine 5 Human genes 0.000 description 1
- 101150013553 CD40 gene Proteins 0.000 description 1
- 102000055006 Calcitonin Human genes 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical compound [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 1
- 241000282836 Camelus dromedarius Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 108010075016 Ceruloplasmin Proteins 0.000 description 1
- 102100023321 Ceruloplasmin Human genes 0.000 description 1
- 108010055166 Chemokine CCL5 Proteins 0.000 description 1
- 102000019034 Chemokines Human genes 0.000 description 1
- 108010012236 Chemokines Proteins 0.000 description 1
- 208000005243 Chondrosarcoma Diseases 0.000 description 1
- 208000010833 Chronic myeloid leukaemia Diseases 0.000 description 1
- 108090000317 Chymotrypsin Proteins 0.000 description 1
- 102100026735 Coagulation factor VIII Human genes 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- 102000007644 Colony-Stimulating Factors Human genes 0.000 description 1
- 108010071942 Colony-Stimulating Factors Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 241000186216 Corynebacterium Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 229930105110 Cyclosporin A Natural products 0.000 description 1
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 1
- 108010036949 Cyclosporine Proteins 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 102000052510 DNA-Binding Proteins Human genes 0.000 description 1
- 108700020911 DNA-Binding Proteins Proteins 0.000 description 1
- XPDXVDYUQZHFPV-UHFFFAOYSA-N Dansyl Chloride Chemical compound C1=CC=C2C(N(C)C)=CC=CC2=C1S(Cl)(=O)=O XPDXVDYUQZHFPV-UHFFFAOYSA-N 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 101150030061 Eloc gene Proteins 0.000 description 1
- 102100023688 Eotaxin Human genes 0.000 description 1
- 101710139422 Eotaxin Proteins 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- DNXHEGUUPJUMQT-CBZIJGRNSA-N Estrone Chemical compound OC1=CC=C2[C@H]3CC[C@](C)(C(CC4)=O)[C@@H]4[C@@H]3CCC2=C1 DNXHEGUUPJUMQT-CBZIJGRNSA-N 0.000 description 1
- QTANTQQOYSUMLC-UHFFFAOYSA-O Ethidium cation Chemical compound C12=CC(N)=CC=C2C2=CC=C(N)C=C2[N+](CC)=C1C1=CC=CC=C1 QTANTQQOYSUMLC-UHFFFAOYSA-O 0.000 description 1
- 108700024394 Exon Proteins 0.000 description 1
- 201000003542 Factor VIII deficiency Diseases 0.000 description 1
- 108010071289 Factor XIII Proteins 0.000 description 1
- 108091006020 Fc-tagged proteins Proteins 0.000 description 1
- 102000009123 Fibrin Human genes 0.000 description 1
- 108010073385 Fibrin Proteins 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 102100028071 Fibroblast growth factor 7 Human genes 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 description 1
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 108010051815 Glutamyl endopeptidase Proteins 0.000 description 1
- SXRSQZLOMIGNAQ-UHFFFAOYSA-N Glutaraldehyde Chemical compound O=CCCCC=O SXRSQZLOMIGNAQ-UHFFFAOYSA-N 0.000 description 1
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 241000989913 Gunnera petaloidea Species 0.000 description 1
- QXZGBUJJYSLZLT-UHFFFAOYSA-N H-Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg-OH Natural products NC(N)=NCCCC(N)C(=O)N1CCCC1C(=O)N1C(C(=O)NCC(=O)NC(CC=2C=CC=CC=2)C(=O)NC(CO)C(=O)N2C(CCC2)C(=O)NC(CC=2C=CC=CC=2)C(=O)NC(CCCN=C(N)N)C(O)=O)CCC1 QXZGBUJJYSLZLT-UHFFFAOYSA-N 0.000 description 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
- 102000012428 Hematopoietic Cell Growth Factors Human genes 0.000 description 1
- 108010022580 Hematopoietic Cell Growth Factors Proteins 0.000 description 1
- 208000031220 Hemophilia Diseases 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 230000010556 Heparin Binding Activity Effects 0.000 description 1
- 108090000481 Heparin Cofactor II Proteins 0.000 description 1
- 102100030500 Heparin cofactor 2 Human genes 0.000 description 1
- 240000001304 Hippeastrum striatum Species 0.000 description 1
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 1
- 101000582631 Homo sapiens Menin Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- PMMYEEVYMWASQN-DMTCNVIQSA-N Hydroxyproline Chemical compound O[C@H]1CN[C@H](C(O)=O)C1 PMMYEEVYMWASQN-DMTCNVIQSA-N 0.000 description 1
- 206010020772 Hypertension Diseases 0.000 description 1
- 208000013016 Hypoglycemia Diseases 0.000 description 1
- 208000001953 Hypotension Diseases 0.000 description 1
- 206010021143 Hypoxia Diseases 0.000 description 1
- 102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 description 1
- 101710177940 IgG receptor FcRn large subunit p51 Proteins 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 241000976924 Inca Species 0.000 description 1
- 229930010555 Inosine Natural products 0.000 description 1
- UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102000004388 Interleukin-4 Human genes 0.000 description 1
- 108090000978 Interleukin-4 Proteins 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- SNDPXSYFESPGGJ-BYPYZUCNSA-N L-2-aminopentanoic acid Chemical compound CCC[C@H](N)C(O)=O SNDPXSYFESPGGJ-BYPYZUCNSA-N 0.000 description 1
- AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ZGUNAGUHMKGQNY-ZETCQYMHSA-N L-alpha-phenylglycine zwitterion Chemical compound OC(=O)[C@@H](N)C1=CC=CC=C1 ZGUNAGUHMKGQNY-ZETCQYMHSA-N 0.000 description 1
- RHGKLRLOHDJJDR-BYPYZUCNSA-N L-citrulline Chemical compound NC(=O)NCCC[C@H]([NH3+])C([O-])=O RHGKLRLOHDJJDR-BYPYZUCNSA-N 0.000 description 1
- XIGSAGMEBXLVJJ-YFKPBYRVSA-N L-homocitrulline Chemical compound NC(=O)NCCCC[C@H]([NH3+])C([O-])=O XIGSAGMEBXLVJJ-YFKPBYRVSA-N 0.000 description 1
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 1
- SNDPXSYFESPGGJ-UHFFFAOYSA-N L-norVal-OH Natural products CCCC(N)C(O)=O SNDPXSYFESPGGJ-UHFFFAOYSA-N 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- 208000031671 Large B-Cell Diffuse Lymphoma Diseases 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 102100035304 Lymphotactin Human genes 0.000 description 1
- 101100348047 Mus musculus Ncam2 gene Proteins 0.000 description 1
- 206010073137 Myxoid liposarcoma Diseases 0.000 description 1
- RHGKLRLOHDJJDR-UHFFFAOYSA-N Ndelta-carbamoyl-DL-ornithine Natural products OC(=O)C(N)CCCNC(N)=O RHGKLRLOHDJJDR-UHFFFAOYSA-N 0.000 description 1
- 244000061176 Nicotiana tabacum Species 0.000 description 1
- 235000002637 Nicotiana tabacum Nutrition 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- MMPOTNFPDMJTRR-UHFFFAOYSA-N OOOOOOOOOOO Chemical compound OOOOOOOOOOO MMPOTNFPDMJTRR-UHFFFAOYSA-N 0.000 description 1
- 208000008589 Obesity Diseases 0.000 description 1
- 201000010133 Oligodendroglioma Diseases 0.000 description 1
- AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 description 1
- UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 description 1
- 208000001132 Osteoporosis Diseases 0.000 description 1
- 102000008108 Osteoprotegerin Human genes 0.000 description 1
- 108010035042 Osteoprotegerin Proteins 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 208000030852 Parasitic disease Diseases 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 241000237988 Patellidae Species 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 244000046052 Phaseolus vulgaris Species 0.000 description 1
- 235000010627 Phaseolus vulgaris Nutrition 0.000 description 1
- 208000007913 Pituitary Neoplasms Diseases 0.000 description 1
- 108010039918 Polylysine Proteins 0.000 description 1
- 239000004372 Polyvinyl alcohol Substances 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- 102000017975 Protein C Human genes 0.000 description 1
- 229940096437 Protein S Drugs 0.000 description 1
- 108010066124 Protein S Proteins 0.000 description 1
- 102000029301 Protein S Human genes 0.000 description 1
- 101100084022 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) lapA gene Proteins 0.000 description 1
- 208000010378 Pulmonary Embolism Diseases 0.000 description 1
- 102000009609 Pyrophosphatases Human genes 0.000 description 1
- 108010009413 Pyrophosphatases Proteins 0.000 description 1
- 108091034057 RNA (poly(A)) Proteins 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 1
- 230000018199 S phase Effects 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 101800001700 Saposin-D Proteins 0.000 description 1
- 108010077895 Sarcosine Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108050007496 Shikimate kinase 2 Proteins 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000256248 Spodoptera Species 0.000 description 1
- 108010039445 Stem Cell Factor Proteins 0.000 description 1
- 208000006011 Stroke Diseases 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- RAHZWNYVWXNFOC-UHFFFAOYSA-N Sulphur dioxide Chemical group O=S=O RAHZWNYVWXNFOC-UHFFFAOYSA-N 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 108020005038 Terminator Codon Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 241000011102 Thera Species 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 102000036693 Thrombopoietin Human genes 0.000 description 1
- 108010041111 Thrombopoietin Proteins 0.000 description 1
- 208000007536 Thrombosis Diseases 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- YZCKVEUIGOORGS-NJFSPNSNSA-N Tritium Chemical compound [3H] YZCKVEUIGOORGS-NJFSPNSNSA-N 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 1
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 229910052770 Uranium Inorganic materials 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Chemical compound CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 1
- 208000024248 Vascular System injury Diseases 0.000 description 1
- 208000035868 Vascular inflammations Diseases 0.000 description 1
- 208000012339 Vascular injury Diseases 0.000 description 1
- GXBMIBRIOWHPDT-UHFFFAOYSA-N Vasopressin Natural products N1C(=O)C(CC=2C=C(O)C=CC=2)NC(=O)C(N)CSSCC(C(=O)N2C(CCC2)C(=O)NC(CCCN=C(N)N)C(=O)NCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(CCC(N)=O)NC(=O)C1CC1=CC=CC=C1 GXBMIBRIOWHPDT-UHFFFAOYSA-N 0.000 description 1
- 108010004977 Vasopressins Proteins 0.000 description 1
- 102000002852 Vasopressins Human genes 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- FHNFHKCVQCLJFQ-NJFSPNSNSA-N Xenon-133 Chemical compound [133Xe] FHNFHKCVQCLJFQ-NJFSPNSNSA-N 0.000 description 1
- 210000001015 abdomen Anatomy 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 206010001323 adrenal adenoma Diseases 0.000 description 1
- 239000007801 affinity label Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 238000012867 alanine scanning Methods 0.000 description 1
- 125000001931 aliphatic group Chemical group 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 150000001408 amides Chemical group 0.000 description 1
- 229960002684 aminocaproic acid Drugs 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 210000004727 amygdala Anatomy 0.000 description 1
- 230000033115 angiogenesis Effects 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 229960005348 antithrombin iii Drugs 0.000 description 1
- 210000000709 aorta Anatomy 0.000 description 1
- KBZOIRJILGZLEJ-LGYYRGKSSA-N argipressin Chemical compound C([C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CSSC[C@@H](C(N[C@@H](CC=2C=CC(O)=CC=2)C(=O)N1)=O)N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCN=C(N)N)C(=O)NCC(N)=O)C1=CC=CC=C1 KBZOIRJILGZLEJ-LGYYRGKSSA-N 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 210000004082 barrier epithelial cell Anatomy 0.000 description 1
- 210000003651 basophil Anatomy 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000000975 bioactive effect Effects 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 230000000157 blood function Effects 0.000 description 1
- 230000036772 blood pressure Effects 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- QXZGBUJJYSLZLT-FDISYFBBSA-N bradykinin Chemical compound NC(=N)NCCC[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(=O)NCC(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CO)C(=O)N2[C@@H](CCC2)C(=O)N[C@@H](CC=2C=CC=CC=2)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)CCC1 QXZGBUJJYSLZLT-FDISYFBBSA-N 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 230000023852 carbohydrate metabolic process Effects 0.000 description 1
- 235000021256 carbohydrate metabolism Nutrition 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 125000002915 carbonyl group Chemical group [*:2]C([*:1])=O 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 210000000748 cardiovascular system Anatomy 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 239000002458 cell surface marker Substances 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 210000003588 centroblast Anatomy 0.000 description 1
- 235000013339 cereals Nutrition 0.000 description 1
- 230000002490 cerebral effect Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000001311 chemical methods and process Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 238000003200 chromosome mapping Methods 0.000 description 1
- 208000024207 chronic leukemia Diseases 0.000 description 1
- 229960002376 chymotrypsin Drugs 0.000 description 1
- 229960001265 ciclosporin Drugs 0.000 description 1
- 229960002173 citrulline Drugs 0.000 description 1
- 235000013477 citrulline Nutrition 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 201000010897 colon adenocarcinoma Diseases 0.000 description 1
- 229940047120 colony stimulating factors Drugs 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 230000009137 competitive binding Effects 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 230000024203 complement activation Effects 0.000 description 1
- 230000001268 conjugating effect Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 208000029078 coronary artery disease Diseases 0.000 description 1
- IDLFZVILOHSSID-OVLDLUHVSA-N corticotropin Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=C(O)C=C1 IDLFZVILOHSSID-OVLDLUHVSA-N 0.000 description 1
- 229960000258 corticotropin Drugs 0.000 description 1
- 208000030381 cutaneous melanoma Diseases 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- YPHMISFOHDHNIV-FSZOTQKASA-N cycloheximide Chemical compound C1[C@@H](C)C[C@H](C)C(=O)[C@@H]1[C@H](O)CC1CC(=O)NC(=O)C1 YPHMISFOHDHNIV-FSZOTQKASA-N 0.000 description 1
- 208000012106 cystic neoplasm Diseases 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- 108020001096 dihydrofolate reductase Proteins 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- PMMYEEVYMWASQN-UHFFFAOYSA-N dl-hydroxyproline Natural products OC1C[NH2+]C(C([O-])=O)C1 PMMYEEVYMWASQN-UHFFFAOYSA-N 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 238000007876 drug discovery Methods 0.000 description 1
- 210000001951 dura mater Anatomy 0.000 description 1
- 230000004064 dysfunction Effects 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000003979 eosinophil Anatomy 0.000 description 1
- 230000004890 epithelial barrier function Effects 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 210000003238 esophagus Anatomy 0.000 description 1
- 229960005309 estradiol Drugs 0.000 description 1
- 229930182833 estradiol Natural products 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000029142 excretion Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 229940012444 factor xiii Drugs 0.000 description 1
- 210000003754 fetus Anatomy 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 239000011737 fluorine Substances 0.000 description 1
- 229910052731 fluorine Inorganic materials 0.000 description 1
- 229940028334 follicle stimulating hormone Drugs 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 210000005153 frontal cortex Anatomy 0.000 description 1
- 239000000446 fuel Substances 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 229960003692 gamma aminobutyric acid Drugs 0.000 description 1
- 238000005227 gel permeation chromatography Methods 0.000 description 1
- 238000012817 gel-diffusion technique Methods 0.000 description 1
- 210000004602 germ cell Anatomy 0.000 description 1
- 210000004195 gingiva Anatomy 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- 150000002334 glycols Chemical class 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 230000035931 haemagglutination Effects 0.000 description 1
- 239000000185 hemagglutinin Substances 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 208000031169 hemorrhagic disease Diseases 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 238000012188 high-throughput screening assay Methods 0.000 description 1
- 210000003630 histaminocyte Anatomy 0.000 description 1
- 230000013632 homeostatic process Effects 0.000 description 1
- 102000047681 human MEN1 Human genes 0.000 description 1
- 210000003917 human chromosome Anatomy 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- 229960002591 hydroxyproline Drugs 0.000 description 1
- 230000002218 hypoglycaemic effect Effects 0.000 description 1
- 210000003016 hypothalamus Anatomy 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000036737 immune function Effects 0.000 description 1
- 208000026278 immune system disease Diseases 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 238000000760 immunoelectrophoresis Methods 0.000 description 1
- 238000010166 immunofluorescence Methods 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 238000003017 in situ immunoassay Methods 0.000 description 1
- 229910052738 indium Inorganic materials 0.000 description 1
- APFVFJFRJDLVQX-UHFFFAOYSA-N indium atom Chemical compound [In] APFVFJFRJDLVQX-UHFFFAOYSA-N 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 208000000509 infertility Diseases 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 231100000535 infertility Toxicity 0.000 description 1
- 230000004054 inflammatory process Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 229960003786 inosine Drugs 0.000 description 1
- 230000035990 intercellular signaling Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 229940076264 interleukin-3 Drugs 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 239000011630 iodine Substances 0.000 description 1
- 229910052740 iodine Inorganic materials 0.000 description 1
- 229910052742 iron Inorganic materials 0.000 description 1
- 201000002529 islet cell tumor Diseases 0.000 description 1
- 125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 1
- 230000000155 isotopic effect Effects 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 1
- 210000000231 kidney cortex Anatomy 0.000 description 1
- 206010023841 laryngeal neoplasm Diseases 0.000 description 1
- 210000002414 leg Anatomy 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 208000019423 liver disease Diseases 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 201000005249 lung adenocarcinoma Diseases 0.000 description 1
- 201000005296 lung carcinoma Diseases 0.000 description 1
- 208000020816 lung neoplasm Diseases 0.000 description 1
- 208000037841 lung tumor Diseases 0.000 description 1
- 108010019677 lymphotactin Proteins 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 210000003593 megakaryocyte Anatomy 0.000 description 1
- 210000002752 melanocyte Anatomy 0.000 description 1
- 210000004379 membrane Anatomy 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 210000001806 memory b lymphocyte Anatomy 0.000 description 1
- 210000000716 merkel cell Anatomy 0.000 description 1
- 208000030159 metabolic disease Diseases 0.000 description 1
- 230000031864 metaphase Effects 0.000 description 1
- SXTAYKAGBXMACB-UHFFFAOYSA-N methionine S-imide-S-oxide Natural products CS(=N)(=O)CCC(N)C(O)=O SXTAYKAGBXMACB-UHFFFAOYSA-N 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 208000016055 micropapillary serous carcinoma Diseases 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- ZTLGJPIZUOVDMT-UHFFFAOYSA-N n,n-dichlorotriazin-4-amine Chemical compound ClN(Cl)C1=CC=NN=N1 ZTLGJPIZUOVDMT-UHFFFAOYSA-N 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000036963 noncompetitive effect Effects 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- 125000003835 nucleoside group Chemical group 0.000 description 1
- 210000004940 nucleus Anatomy 0.000 description 1
- 235000020824 obesity Nutrition 0.000 description 1
- XXUPLYBCNPLTIW-UHFFFAOYSA-N octadec-7-ynoic acid Chemical compound CCCCCCCCCCC#CCCCCCC(O)=O XXUPLYBCNPLTIW-UHFFFAOYSA-N 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 210000002747 omentum Anatomy 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 229960003104 ornithine Drugs 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 201000008482 osteoarthritis Diseases 0.000 description 1
- 210000000963 osteoblast Anatomy 0.000 description 1
- 201000008968 osteosarcoma Diseases 0.000 description 1
- 108010071584 oxidized low density lipoprotein Proteins 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 208000022102 pancreatic neuroendocrine neoplasm Diseases 0.000 description 1
- 208000004019 papillary adenocarcinoma Diseases 0.000 description 1
- 201000005163 papillary serous adenocarcinoma Diseases 0.000 description 1
- 208000024641 papillary serous cystadenocarcinoma Diseases 0.000 description 1
- 230000000849 parathyroid Effects 0.000 description 1
- 229960001319 parathyroid hormone Drugs 0.000 description 1
- 239000000199 parathyroid hormone Substances 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 210000005259 peripheral blood Anatomy 0.000 description 1
- 239000011886 peripheral blood Substances 0.000 description 1
- 230000002688 persistence Effects 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 238000002135 phase contrast microscopy Methods 0.000 description 1
- NMHMNPHRMNGLLB-UHFFFAOYSA-N phloretic acid Chemical compound OC(=O)CCC1=CC=C(O)C=C1 NMHMNPHRMNGLLB-UHFFFAOYSA-N 0.000 description 1
- 101150009573 phoA gene Proteins 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 230000003169 placental effect Effects 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 229920000447 polyanionic polymer Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 108010039177 polyphenylalanine Proteins 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 235000019419 proteases Nutrition 0.000 description 1
- 238000013197 protein A assay Methods 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
- 239000012857 radioactive material Substances 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009257 reactivity Effects 0.000 description 1
- 239000000018 receptor agonist Substances 0.000 description 1
- 229940044601 receptor agonist Drugs 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000006722 reduction reaction Methods 0.000 description 1
- 238000005932 reductive alkylation reaction Methods 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 230000001850 reproductive effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 210000003079 salivary gland Anatomy 0.000 description 1
- 229940043230 sarcosine Drugs 0.000 description 1
- 238000002416 scanning tunnelling spectroscopy Methods 0.000 description 1
- 201000000980 schizophrenia Diseases 0.000 description 1
- 208000004548 serous cystadenocarcinoma Diseases 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 201000003708 skin melanoma Diseases 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 238000001228 spectrum Methods 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 208000023516 stroke disease Diseases 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 230000008685 targeting Effects 0.000 description 1
- 229910052713 technetium Inorganic materials 0.000 description 1
- GKLVYJBZJHMRIY-UHFFFAOYSA-N technetium atom Chemical compound [Tc] GKLVYJBZJHMRIY-UHFFFAOYSA-N 0.000 description 1
- 208000011317 telomere syndrome Diseases 0.000 description 1
- 230000002123 temporal effect Effects 0.000 description 1
- 229960000814 tetanus toxoid Drugs 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- 229910052716 thallium Inorganic materials 0.000 description 1
- BKVIYDNLLOSFOA-UHFFFAOYSA-N thallium Chemical compound [Tl] BKVIYDNLLOSFOA-UHFFFAOYSA-N 0.000 description 1
- 229940126585 therapeutic drug Drugs 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 108700012359 toxins Proteins 0.000 description 1
- FGMPLJWBKKVCDB-UHFFFAOYSA-N trans-L-hydroxy-proline Natural products ON1CCCC1C(O)=O FGMPLJWBKKVCDB-UHFFFAOYSA-N 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- HRXKRNGNAMMEHJ-UHFFFAOYSA-K trisodium citrate Chemical compound [Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O HRXKRNGNAMMEHJ-UHFFFAOYSA-K 0.000 description 1
- 229940038773 trisodium citrate Drugs 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 229910052722 tritium Inorganic materials 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 229960001322 trypsin Drugs 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- ORHBXUUXSCNDEV-UHFFFAOYSA-N umbelliferone Chemical compound C1=CC(=O)OC2=CC(O)=CC=C21 ORHBXUUXSCNDEV-UHFFFAOYSA-N 0.000 description 1
- HFTAFOQKODTIJY-UHFFFAOYSA-N umbelliferone Natural products Cc1cc2C=CC(=O)Oc2cc1OCC=CC(C)(C)O HFTAFOQKODTIJY-UHFFFAOYSA-N 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 230000024883 vasodilation Effects 0.000 description 1
- 229960003726 vasopressin Drugs 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 230000001755 vocal effect Effects 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 229920003169 water-soluble polymer Polymers 0.000 description 1
- 229950004094 xenon (133xe) Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/46—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- C07K14/47—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Toxicology (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Abstract
Publié sans précis
Applications Claiming Priority (236)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US17906500P | 2000-01-31 | 2000-01-31 | |
| US60/179,065 | 2000-01-31 | ||
| US18062800P | 2000-02-04 | 2000-02-04 | |
| US60/180,628 | 2000-02-04 | ||
| US18466400P | 2000-02-24 | 2000-02-24 | |
| US60/184,664 | 2000-02-24 | ||
| US18635000P | 2000-03-02 | 2000-03-02 | |
| US60/186,350 | 2000-03-02 | ||
| US18987400P | 2000-03-16 | 2000-03-16 | |
| US60/189,874 | 2000-03-16 | ||
| US19007600P | 2000-03-17 | 2000-03-17 | |
| US60/190,076 | 2000-03-17 | ||
| US19812300P | 2000-04-18 | 2000-04-18 | |
| US60/198,123 | 2000-04-18 | ||
| US20551500P | 2000-05-19 | 2000-05-19 | |
| US60/205,515 | 2000-05-19 | ||
| US20946700P | 2000-06-07 | 2000-06-07 | |
| US60/209,467 | 2000-06-07 | ||
| US21488600P | 2000-06-28 | 2000-06-28 | |
| US60/214,886 | 2000-06-28 | ||
| US21513500P | 2000-06-30 | 2000-06-30 | |
| US60/215,135 | 2000-06-30 | ||
| US21664700P | 2000-07-07 | 2000-07-07 | |
| US21688000P | 2000-07-07 | 2000-07-07 | |
| US60/216,647 | 2000-07-07 | ||
| US60/216,880 | 2000-07-07 | ||
| US21749600P | 2000-07-11 | 2000-07-11 | |
| US21748700P | 2000-07-11 | 2000-07-11 | |
| US60/217,496 | 2000-07-11 | ||
| US60/217,487 | 2000-07-11 | ||
| US21829000P | 2000-07-14 | 2000-07-14 | |
| US60/218,290 | 2000-07-14 | ||
| US22096300P | 2000-07-26 | 2000-07-26 | |
| US22096400P | 2000-07-26 | 2000-07-26 | |
| US60/220,963 | 2000-07-26 | ||
| US60/220,964 | 2000-07-26 | ||
| US22526600P | 2000-08-14 | 2000-08-14 | |
| US22544700P | 2000-08-14 | 2000-08-14 | |
| US22451900P | 2000-08-14 | 2000-08-14 | |
| US22521400P | 2000-08-14 | 2000-08-14 | |
| US22521300P | 2000-08-14 | 2000-08-14 | |
| US22451800P | 2000-08-14 | 2000-08-14 | |
| US22575900P | 2000-08-14 | 2000-08-14 | |
| US22575800P | 2000-08-14 | 2000-08-14 | |
| US22527000P | 2000-08-14 | 2000-08-14 | |
| US22575700P | 2000-08-14 | 2000-08-14 | |
| US22526800P | 2000-08-14 | 2000-08-14 | |
| US22526700P | 2000-08-14 | 2000-08-14 | |
| US60/224,519 | 2000-08-14 | ||
| US60/225,270 | 2000-08-14 | ||
| US60/225,268 | 2000-08-14 | ||
| US60/225,757 | 2000-08-14 | ||
| US60/225,447 | 2000-08-14 | ||
| US60/225,267 | 2000-08-14 | ||
| US60/225,213 | 2000-08-14 | ||
| US60/224,518 | 2000-08-14 | ||
| US60/225,759 | 2000-08-14 | ||
| US60/225,214 | 2000-08-14 | ||
| US60/225,266 | 2000-08-14 | ||
| US60/225,758 | 2000-08-14 | ||
| US22627900P | 2000-08-18 | 2000-08-18 | |
| US60/226,279 | 2000-08-18 | ||
| US22668100P | 2000-08-22 | 2000-08-22 | |
| US22686800P | 2000-08-22 | 2000-08-22 | |
| US22718200P | 2000-08-22 | 2000-08-22 | |
| US60/226,868 | 2000-08-22 | ||
| US60/227,182 | 2000-08-22 | ||
| US60/226,681 | 2000-08-22 | ||
| US22700900P | 2000-08-23 | 2000-08-23 | |
| US60/227,009 | 2000-08-23 | ||
| US22892400P | 2000-08-30 | 2000-08-30 | |
| US60/228,924 | 2000-08-30 | ||
| US22934300P | 2000-09-01 | 2000-09-01 | |
| US22928700P | 2000-09-01 | 2000-09-01 | |
| US22934400P | 2000-09-01 | 2000-09-01 | |
| US22934500P | 2000-09-01 | 2000-09-01 | |
| US60/229,287 | 2000-09-01 | ||
| US60/229,344 | 2000-09-01 | ||
| US60/229,345 | 2000-09-01 | ||
| US60/229,343 | 2000-09-01 | ||
| US22950900P | 2000-09-05 | 2000-09-05 | |
| US22951300P | 2000-09-05 | 2000-09-05 | |
| US60/229,513 | 2000-09-05 | ||
| US60/229,509 | 2000-09-05 | ||
| US23043800P | 2000-09-06 | 2000-09-06 | |
| US23043700P | 2000-09-06 | 2000-09-06 | |
| US60/230,437 | 2000-09-06 | ||
| US60/230,438 | 2000-09-06 | ||
| US23124400P | 2000-09-08 | 2000-09-08 | |
| US23141400P | 2000-09-08 | 2000-09-08 | |
| US23208000P | 2000-09-08 | 2000-09-08 | |
| US23208100P | 2000-09-08 | 2000-09-08 | |
| US23124300P | 2000-09-08 | 2000-09-08 | |
| US23141300P | 2000-09-08 | 2000-09-08 | |
| US23124200P | 2000-09-08 | 2000-09-08 | |
| US60/231,414 | 2000-09-08 | ||
| US60/231,242 | 2000-09-08 | ||
| US60/231,243 | 2000-09-08 | ||
| US60/231,244 | 2000-09-08 | ||
| US60/231,413 | 2000-09-08 | ||
| US60/232,081 | 2000-09-08 | ||
| US60/232,080 | 2000-09-08 | ||
| US23196800P | 2000-09-12 | 2000-09-12 | |
| US60/231,968 | 2000-09-12 | ||
| US23306300P | 2000-09-14 | 2000-09-14 | |
| US23239700P | 2000-09-14 | 2000-09-14 | |
| US23240100P | 2000-09-14 | 2000-09-14 | |
| US23239800P | 2000-09-14 | 2000-09-14 | |
| US23306500P | 2000-09-14 | 2000-09-14 | |
| US23239900P | 2000-09-14 | 2000-09-14 | |
| US23306400P | 2000-09-14 | 2000-09-14 | |
| US23240000P | 2000-09-14 | 2000-09-14 | |
| US60/232,401 | 2000-09-14 | ||
| US60/232,400 | 2000-09-14 | ||
| US60/232,398 | 2000-09-14 | ||
| US60/232,399 | 2000-09-14 | ||
| US60/233,064 | 2000-09-14 | ||
| US60/233,063 | 2000-09-14 | ||
| US60/232,397 | 2000-09-14 | ||
| US60/233,065 | 2000-09-14 | ||
| US23427400P | 2000-09-21 | 2000-09-21 | |
| US23422300P | 2000-09-21 | 2000-09-21 | |
| US60/234,274 | 2000-09-21 | ||
| US60/234,223 | 2000-09-21 | ||
| US23499700P | 2000-09-25 | 2000-09-25 | |
| US23499800P | 2000-09-25 | 2000-09-25 | |
| US60/234,998 | 2000-09-25 | ||
| US60/234,997 | 2000-09-25 | ||
| US23548400P | 2000-09-26 | 2000-09-26 | |
| US60/235,484 | 2000-09-26 | ||
| US23583400P | 2000-09-27 | 2000-09-27 | |
| US23583600P | 2000-09-27 | 2000-09-27 | |
| US60/235,836 | 2000-09-27 | ||
| US60/235,834 | 2000-09-27 | ||
| US23636800P | 2000-09-29 | 2000-09-29 | |
| US23636900P | 2000-09-29 | 2000-09-29 | |
| US23636700P | 2000-09-29 | 2000-09-29 | |
| US23637000P | 2000-09-29 | 2000-09-29 | |
| US23632700P | 2000-09-29 | 2000-09-29 | |
| US60/236,370 | 2000-09-29 | ||
| US60/236,327 | 2000-09-29 | ||
| US60/236,367 | 2000-09-29 | ||
| US60/236,368 | 2000-09-29 | ||
| US60/236,369 | 2000-09-29 | ||
| US23704000P | 2000-10-02 | 2000-10-02 | |
| US23680200P | 2000-10-02 | 2000-10-02 | |
| US23703900P | 2000-10-02 | 2000-10-02 | |
| US23703800P | 2000-10-02 | 2000-10-02 | |
| US23703700P | 2000-10-02 | 2000-10-02 | |
| US60/237,039 | 2000-10-02 | ||
| US60/237,038 | 2000-10-02 | ||
| US60/236,802 | 2000-10-02 | ||
| US60/237,037 | 2000-10-02 | ||
| US60/237,040 | 2000-10-02 | ||
| US23993500P | 2000-10-13 | 2000-10-13 | |
| US23993700P | 2000-10-13 | 2000-10-13 | |
| US60/239,935 | 2000-10-13 | ||
| US60/239,937 | 2000-10-13 | ||
| US24096000P | 2000-10-20 | 2000-10-20 | |
| US24178700P | 2000-10-20 | 2000-10-20 | |
| US24122100P | 2000-10-20 | 2000-10-20 | |
| US24178600P | 2000-10-20 | 2000-10-20 | |
| US24180800P | 2000-10-20 | 2000-10-20 | |
| US24178500P | 2000-10-20 | 2000-10-20 | |
| US24182600P | 2000-10-20 | 2000-10-20 | |
| US24180900P | 2000-10-20 | 2000-10-20 | |
| US60/241,221 | 2000-10-20 | ||
| US60/241,809 | 2000-10-20 | ||
| US60/241,787 | 2000-10-20 | ||
| US60/241,808 | 2000-10-20 | ||
| US60/241,785 | 2000-10-20 | ||
| US60/241,786 | 2000-10-20 | ||
| US60/241,826 | 2000-10-20 | ||
| US60/240,960 | 2000-10-20 | ||
| US24461700P | 2000-11-01 | 2000-11-01 | |
| US60/244,617 | 2000-11-01 | ||
| US60/246,299 | 2000-11-06 | ||
| US24647500P | 2000-11-08 | 2000-11-08 | |
| US24652800P | 2000-11-08 | 2000-11-08 | |
| US24661000P | 2000-11-08 | 2000-11-08 | |
| US24661100P | 2000-11-08 | 2000-11-08 | |
| US24647700P | 2000-11-08 | 2000-11-08 | |
| US24661300P | 2000-11-08 | 2000-11-08 | |
| US24652500P | 2000-11-08 | 2000-11-08 | |
| US24652700P | 2000-11-08 | 2000-11-08 | |
| US24647400P | 2000-11-08 | 2000-11-08 | |
| US24653200P | 2000-11-08 | 2000-11-08 | |
| US24660900P | 2000-11-08 | 2000-11-08 | |
| US60/246,478 | 2000-11-08 | ||
| US60/246,526 | 2000-11-08 | ||
| US60/246,613 | 2000-11-08 | ||
| US60/246,609 | 2000-11-08 | ||
| US60/246,611 | 2000-11-08 | ||
| US60/246,527 | 2000-11-08 | ||
| US60/246,610 | 2000-11-08 | ||
| US60/246,528 | 2000-11-08 | ||
| US60/246,523 | 2000-11-08 | ||
| US60/246,524 | 2000-11-08 | ||
| US60/246,532 | 2000-11-08 | ||
| US60/246,475 | 2000-11-08 | ||
| US60/246,476 | 2000-11-08 | ||
| US60/246,474 | 2000-11-08 | ||
| US60/246,477 | 2000-11-08 | ||
| US60/246,525 | 2000-11-08 | ||
| US60/249,217 | 2000-11-17 | ||
| US60/249,244 | 2000-11-17 | ||
| US60/249,265 | 2000-11-17 | ||
| US60/249,209 | 2000-11-17 | ||
| US60/249,218 | 2000-11-17 | ||
| US60/249,210 | 2000-11-17 | ||
| US60/249,212 | 2000-11-17 | ||
| US60/249,299 | 2000-11-17 | ||
| US60/249,208 | 2000-11-17 | ||
| US60/249,245 | 2000-11-17 | ||
| US60/249,214 | 2000-11-17 | ||
| US60/249,264 | 2000-11-17 | ||
| US60/249,297 | 2000-11-17 | ||
| US60/249,300 | 2000-11-17 | ||
| US60/249,207 | 2000-11-17 | ||
| US60/249,213 | 2000-11-17 | ||
| US60/249,216 | 2000-11-17 | ||
| US60/249,215 | 2000-11-17 | ||
| US60/249,211 | 2000-11-17 | ||
| US60/250,160 | 2000-12-01 | ||
| US60/250,391 | 2000-12-01 | ||
| US60/251,030 | 2000-12-05 | ||
| US60/256,719 | 2000-12-05 | ||
| US60/251,988 | 2000-12-05 | ||
| US60/251,479 | 2000-12-06 | ||
| US60/251,856 | 2000-12-08 | ||
| US60/251,868 | 2000-12-08 | ||
| US60/251,869 | 2000-12-08 | ||
| US60/251,989 | 2000-12-08 | ||
| US60/251,990 | 2000-12-08 | ||
| US60/254,097 | 2000-12-11 | ||
| US60/259,678 | 2001-01-05 |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2395838A1 true CA2395838A1 (fr) | 2001-08-02 |
Family
ID=27587118
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA 2395838 Withdrawn CA2395838A1 (fr) | 2000-01-31 | 2001-01-17 | Acides nucleiques, proteines et anticorps |
Country Status (2)
| Country | Link |
|---|---|
| CA (1) | CA2395838A1 (fr) |
| WO (2) | WO2001055168A1 (fr) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1230349B1 (fr) | 1999-11-18 | 2007-06-13 | Dendreon Corporation | Acides nucleiques codant pour des endotheliases, endotheliases et leurs utilisations |
| US7700341B2 (en) | 2000-02-03 | 2010-04-20 | Dendreon Corporation | Nucleic acid molecules encoding transmembrane serine proteases, the encoded proteins and methods based thereon |
| AU2001281967A1 (en) * | 2000-07-18 | 2002-01-30 | Bayer Aktiengesellschaft | Regulation of human desc1-like serine protease |
| AU2001283062A1 (en) | 2000-08-02 | 2002-02-13 | The Johns Hopkins University | Endothelial cell expression patterns |
| WO2002072786A2 (fr) | 2001-03-13 | 2002-09-19 | Corvas International, Inc. | Molecules d'acides nucleiques codant pour une serine protease transmembranaire 7, polypeptides codes et procedes associes |
| JP2004535166A (ja) | 2001-03-22 | 2004-11-25 | デンドレオン・サンディエゴ・リミテッド・ライアビリティ・カンパニー | セリンプロテアーゼcvsp14をコードする核酸分子、コードされるポリペプチドおよびそれに基づく方法 |
| US7105333B2 (en) | 2001-03-27 | 2006-09-12 | Deadreon Corporation | Nucleic acid molecules encoding a transmembrane serine protease 9, the encoded polypeptides and methods based thereon |
| US7033790B2 (en) | 2001-04-03 | 2006-04-25 | Curagen Corporation | Proteins and nucleic acids encoding same |
| KR20040080940A (ko) | 2001-05-14 | 2004-09-20 | 덴드레온 코포레이션 | 트랜스막 세린 프로테아제 10을 암호화하는 핵산 분자,암호화된 폴리펩티드 및 이에 근거한 방법 |
| US20040234990A1 (en) * | 2001-07-31 | 2004-11-25 | Hiroto Komano | Method of screening alzheimer's disease-associated gene |
| JPWO2003062429A1 (ja) * | 2002-01-23 | 2005-05-26 | 山之内製薬株式会社 | 新規セリンプロテアーゼ |
-
2001
- 2001-01-17 WO PCT/US2001/001331 patent/WO2001055168A1/fr not_active Ceased
- 2001-01-17 WO PCT/US2001/001320 patent/WO2001055441A2/fr not_active Ceased
- 2001-01-17 CA CA 2395838 patent/CA2395838A1/fr not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| WO2001055168A1 (fr) | 2001-08-02 |
| WO2001055441A2 (fr) | 2001-08-02 |
| WO2001055441A8 (fr) | 2001-09-07 |
| WO2001055168A8 (fr) | 2001-09-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2395398A1 (fr) | Acides nucleiques, proteines, et anticorps | |
| EP1404702A2 (fr) | Proteines secretees humaines | |
| US20070055056A1 (en) | 251 human secreted proteins | |
| CA2389722A1 (fr) | 15 proteines secretees humaines | |
| EP1460900A2 (fr) | Proteines humaines secretees | |
| CA2395838A1 (fr) | Acides nucleiques, proteines et anticorps | |
| CA2390438A1 (fr) | Nouvelles proteines 19 secretees par l'homme | |
| US20030036646A1 (en) | Uncoupling protein polynucleotides, polypeptides, and antibodies | |
| CA2385884A1 (fr) | 26 proteines secretees humaines | |
| US20070172830A1 (en) | Antibodies to hhpen62 polypeptide | |
| CA2389305A1 (fr) | 28 proteines secretees humaines | |
| CA2390421A1 (fr) | 24 proteines humaines secretees | |
| US20070026454A1 (en) | Human secreted proteins | |
| CA2395815A1 (fr) | Acides nucleiques, proteines et anticorps | |
| CA2397502A1 (fr) | Polynucleotides de serine/threonine-phosphatases, polypeptides et anticorps | |
| WO2001023402A1 (fr) | 43 proteines secretees humaines | |
| CA2384584A1 (fr) | 38 proteines secretees humaines | |
| US20070015162A1 (en) | 99 human secreted proteins | |
| WO2001034627A1 (fr) | 28 proteines humaines secretees | |
| CA2446610A1 (fr) | 20 proteines humaines secretees | |
| US20070032414A1 (en) | Human secreted proteins | |
| US20050239059A1 (en) | 67 human secreted proteins | |
| CA2393941A1 (fr) | Acides nucleiques, proteines et anticorps | |
| WO2001034767A2 (fr) | 22 proteines humaines secretees | |
| CA2387754A1 (fr) | 10 proteines humaines secretees |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| AZWI | Withdrawn application |