JPH11513883A - ヒト血管内皮増殖因子２ - Google Patents
ヒト血管内皮増殖因子２Info
- Publication number
- JPH11513883A JPH11513883A JP9501427A JP50142797A JPH11513883A JP H11513883 A JPH11513883 A JP H11513883A JP 9501427 A JP9501427 A JP 9501427A JP 50142797 A JP50142797 A JP 50142797A JP H11513883 A JPH11513883 A JP H11513883A
- Authority
- JP
- Japan
- Prior art keywords
- polypeptide
- polynucleotide
- vegf2
- dna
- cells
- 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- Withdrawn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
- 101000808011 Homo sapiens Vascular endothelial growth factor A Proteins 0.000 title description 5
- 102000058223 human VEGFA Human genes 0.000 title description 5
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 189
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 182
- 229920001184 polypeptide Polymers 0.000 claims abstract description 181
- 238000000034 method Methods 0.000 claims abstract description 76
- 108020004414 DNA Proteins 0.000 claims abstract description 61
- 239000005557 antagonist Substances 0.000 claims abstract description 20
- 230000035772 mutation Effects 0.000 claims abstract description 12
- 238000002405 diagnostic procedure Methods 0.000 claims abstract description 3
- 108091033319 polynucleotide Proteins 0.000 claims description 91
- 102000040430 polynucleotide Human genes 0.000 claims description 91
- 239000002157 polynucleotide Substances 0.000 claims description 90
- 239000013598 vector Substances 0.000 claims description 59
- 239000012634 fragment Substances 0.000 claims description 53
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 39
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 34
- 230000014509 gene expression Effects 0.000 claims description 33
- 239000002299 complementary DNA Substances 0.000 claims description 32
- 150000001413 amino acids Chemical class 0.000 claims description 29
- 150000001875 compounds Chemical class 0.000 claims description 29
- 150000007523 nucleic acids Chemical group 0.000 claims description 29
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 19
- 201000010099 disease Diseases 0.000 claims description 18
- 230000008569 process Effects 0.000 claims description 14
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 12
- 230000027455 binding Effects 0.000 claims description 12
- 238000001727 in vivo Methods 0.000 claims description 11
- 239000000556 agonist Substances 0.000 claims description 6
- 230000003993 interaction Effects 0.000 claims description 5
- 230000002401 inhibitory effect Effects 0.000 claims description 2
- 230000001131 transforming effect Effects 0.000 claims description 2
- VJBCNMFKFZIXHC-UHFFFAOYSA-N azanium;2-(4-methyl-5-oxo-4-propan-2-yl-1h-imidazol-2-yl)quinoline-3-carboxylate Chemical compound N.N1C(=O)C(C(C)C)(C)N=C1C1=NC2=CC=CC=C2C=C1C(O)=O VJBCNMFKFZIXHC-UHFFFAOYSA-N 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract description 130
- 102000004169 proteins and genes Human genes 0.000 abstract description 90
- 108091026890 Coding region Proteins 0.000 abstract description 19
- 230000002792 vascular Effects 0.000 abstract description 9
- 230000004936 stimulating effect Effects 0.000 abstract description 5
- 230000029663 wound healing Effects 0.000 abstract description 5
- 206010039073 rheumatoid arthritis Diseases 0.000 abstract description 4
- 206010012689 Diabetic retinopathy Diseases 0.000 abstract description 3
- 206010061218 Inflammation Diseases 0.000 abstract description 3
- 230000004054 inflammatory process Effects 0.000 abstract description 3
- 230000004614 tumor growth Effects 0.000 abstract description 3
- 201000004681 Psoriasis Diseases 0.000 abstract description 2
- 238000010188 recombinant method Methods 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 99
- 235000018102 proteins Nutrition 0.000 description 86
- 235000001014 amino acid Nutrition 0.000 description 28
- 239000000203 mixture Substances 0.000 description 28
- 210000001519 tissue Anatomy 0.000 description 24
- 239000002609 medium Substances 0.000 description 22
- 239000013612 plasmid Substances 0.000 description 22
- 108020003175 receptors Proteins 0.000 description 22
- 102000005962 receptors Human genes 0.000 description 22
- 239000013615 primer Substances 0.000 description 19
- 210000002889 endothelial cell Anatomy 0.000 description 18
- 241000700605 Viruses Species 0.000 description 17
- 238000005516 engineering process Methods 0.000 description 17
- 230000033115 angiogenesis Effects 0.000 description 15
- 238000003556 assay Methods 0.000 description 14
- 238000004519 manufacturing process Methods 0.000 description 14
- 108091008146 restriction endonucleases Proteins 0.000 description 14
- 239000002773 nucleotide Substances 0.000 description 13
- 125000003729 nucleotide group Chemical group 0.000 description 13
- 210000000349 chromosome Anatomy 0.000 description 12
- 230000000694 effects Effects 0.000 description 12
- 230000035755 proliferation Effects 0.000 description 12
- 239000000523 sample Substances 0.000 description 12
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 108091034117 Oligonucleotide Proteins 0.000 description 10
- 239000013604 expression vector Substances 0.000 description 10
- 108020004999 messenger RNA Proteins 0.000 description 10
- 241000701447 unidentified baculovirus Species 0.000 description 10
- 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 9
- 210000002950 fibroblast Anatomy 0.000 description 9
- 230000001177 retroviral effect Effects 0.000 description 9
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 8
- 206010028980 Neoplasm Diseases 0.000 description 8
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 8
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 8
- 208000027418 Wounds and injury Diseases 0.000 description 8
- 239000002253 acid Substances 0.000 description 8
- 125000000539 amino acid group Chemical group 0.000 description 8
- 238000004458 analytical method Methods 0.000 description 8
- 230000000295 complement effect Effects 0.000 description 8
- 230000000875 corresponding effect Effects 0.000 description 8
- 230000002068 genetic effect Effects 0.000 description 8
- 239000003550 marker Substances 0.000 description 8
- 239000003226 mitogen Substances 0.000 description 8
- 230000008439 repair process Effects 0.000 description 8
- 238000013518 transcription Methods 0.000 description 8
- 230000035897 transcription Effects 0.000 description 8
- 241000701161 unidentified adenovirus Species 0.000 description 8
- 210000003556 vascular endothelial cell Anatomy 0.000 description 8
- 241000701022 Cytomegalovirus Species 0.000 description 7
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 7
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 7
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 7
- 230000001580 bacterial effect Effects 0.000 description 7
- 210000003527 eukaryotic cell Anatomy 0.000 description 7
- 239000012091 fetal bovine serum Substances 0.000 description 7
- 238000009396 hybridization Methods 0.000 description 7
- 238000004806 packaging method and process Methods 0.000 description 7
- 239000002245 particle Substances 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 7
- 241000894006 Bacteria Species 0.000 description 6
- 206010006187 Breast cancer Diseases 0.000 description 6
- 208000026310 Breast neoplasm Diseases 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- 241000588724 Escherichia coli Species 0.000 description 6
- 102000009524 Vascular Endothelial Growth Factor A Human genes 0.000 description 6
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 6
- 238000004587 chromatography analysis Methods 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 239000003623 enhancer Substances 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 102000039446 nucleic acids Human genes 0.000 description 6
- 108020004707 nucleic acids Proteins 0.000 description 6
- 230000010076 replication Effects 0.000 description 6
- 239000007787 solid Substances 0.000 description 6
- 241000238631 Hexapoda Species 0.000 description 5
- 108091092195 Intron Proteins 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 5
- 206010052428 Wound Diseases 0.000 description 5
- 239000011543 agarose gel Substances 0.000 description 5
- 230000000692 anti-sense effect Effects 0.000 description 5
- 230000004071 biological effect Effects 0.000 description 5
- 238000004113 cell culture Methods 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 230000002759 chromosomal effect Effects 0.000 description 5
- 239000003814 drug Substances 0.000 description 5
- 230000006870 function Effects 0.000 description 5
- 230000012010 growth Effects 0.000 description 5
- 238000000338 in vitro Methods 0.000 description 5
- 210000004962 mammalian cell Anatomy 0.000 description 5
- 238000013507 mapping Methods 0.000 description 5
- 230000001105 regulatory effect Effects 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 238000013519 translation Methods 0.000 description 5
- 108020005544 Antisense RNA Proteins 0.000 description 4
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 4
- 108700024394 Exon Proteins 0.000 description 4
- 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 4
- 101710163270 Nuclease Proteins 0.000 description 4
- 101710182846 Polyhedrin Proteins 0.000 description 4
- 108010076504 Protein Sorting Signals Proteins 0.000 description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 4
- 102000006601 Thymidine Kinase Human genes 0.000 description 4
- 108020004440 Thymidine kinase Proteins 0.000 description 4
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 239000003184 complementary RNA Substances 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 229940079593 drug Drugs 0.000 description 4
- 239000012737 fresh medium Substances 0.000 description 4
- 230000035876 healing Effects 0.000 description 4
- 229960002897 heparin Drugs 0.000 description 4
- 229920000669 heparin Polymers 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 208000015181 infectious disease Diseases 0.000 description 4
- 208000014674 injury Diseases 0.000 description 4
- 238000003780 insertion Methods 0.000 description 4
- 230000037431 insertion Effects 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000008194 pharmaceutical composition Substances 0.000 description 4
- 239000013600 plasmid vector Substances 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
- 239000013589 supplement Substances 0.000 description 4
- 238000001356 surgical procedure Methods 0.000 description 4
- 229940104230 thymidine Drugs 0.000 description 4
- 238000001890 transfection Methods 0.000 description 4
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 229920001817 Agar Polymers 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 108010062580 Concanavalin A Proteins 0.000 description 3
- 102000012410 DNA Ligases Human genes 0.000 description 3
- 108010061982 DNA Ligases Proteins 0.000 description 3
- 238000001712 DNA sequencing Methods 0.000 description 3
- 238000012286 ELISA Assay Methods 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 206010018338 Glioma Diseases 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 101000595923 Homo sapiens Placenta growth factor Proteins 0.000 description 3
- 241001465754 Metazoa Species 0.000 description 3
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 3
- 102100035194 Placenta growth factor Human genes 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 3
- 230000009471 action Effects 0.000 description 3
- 239000008272 agar Substances 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 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 3
- 230000003321 amplification Effects 0.000 description 3
- 230000002491 angiogenic effect Effects 0.000 description 3
- 230000037396 body weight Effects 0.000 description 3
- 244000309466 calf Species 0.000 description 3
- 230000004663 cell proliferation Effects 0.000 description 3
- 239000004568 cement Substances 0.000 description 3
- 230000002596 correlated effect Effects 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
- 230000006378 damage Effects 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 230000029087 digestion Effects 0.000 description 3
- 239000000539 dimer Substances 0.000 description 3
- 238000010828 elution Methods 0.000 description 3
- 210000002257 embryonic structure Anatomy 0.000 description 3
- 238000001415 gene therapy Methods 0.000 description 3
- 239000000710 homodimer Substances 0.000 description 3
- 230000002163 immunogen Effects 0.000 description 3
- 239000007943 implant Substances 0.000 description 3
- 238000010348 incorporation Methods 0.000 description 3
- 208000032839 leukemia Diseases 0.000 description 3
- 229960004452 methionine Drugs 0.000 description 3
- 238000003199 nucleic acid amplification method Methods 0.000 description 3
- 239000002751 oligonucleotide probe Substances 0.000 description 3
- 230000008488 polyadenylation Effects 0.000 description 3
- 239000002244 precipitate Substances 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 150000003384 small molecules Chemical class 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000002904 solvent Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 230000000451 tissue damage Effects 0.000 description 3
- 231100000827 tissue damage Toxicity 0.000 description 3
- 230000017423 tissue regeneration Effects 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 241001430294 unidentified retrovirus Species 0.000 description 3
- 238000011144 upstream manufacturing Methods 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 2
- NKDFYOWSKOHCCO-YPVLXUMRSA-N 20-hydroxyecdysone Chemical compound C1[C@@H](O)[C@@H](O)C[C@]2(C)[C@@H](CC[C@@]3([C@@H]([C@@](C)(O)[C@H](O)CCC(C)(O)C)CC[C@]33O)C)C3=CC(=O)[C@@H]21 NKDFYOWSKOHCCO-YPVLXUMRSA-N 0.000 description 2
- 102100022900 Actin, cytoplasmic 1 Human genes 0.000 description 2
- 108010085238 Actins Proteins 0.000 description 2
- 201000001320 Atherosclerosis Diseases 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- 230000006820 DNA synthesis Effects 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 108090000386 Fibroblast Growth Factor 1 Proteins 0.000 description 2
- 102000003974 Fibroblast growth factor 2 Human genes 0.000 description 2
- 108090000379 Fibroblast growth factor 2 Proteins 0.000 description 2
- ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 2
- 101710154606 Hemagglutinin Proteins 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 101710141347 Major envelope glycoprotein Proteins 0.000 description 2
- 102000003792 Metallothionein Human genes 0.000 description 2
- 108090000157 Metallothionein Proteins 0.000 description 2
- 241000699660 Mus musculus Species 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241001460678 Napo <wasp> Species 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
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 229930182555 Penicillin Natural products 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
- 108091000080 Phosphotransferase Proteins 0.000 description 2
- 239000004793 Polystyrene Substances 0.000 description 2
- 101710176177 Protein A56 Proteins 0.000 description 2
- 108020005091 Replication Origin Proteins 0.000 description 2
- 102000006382 Ribonucleases Human genes 0.000 description 2
- 108010083644 Ribonucleases Proteins 0.000 description 2
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 2
- 206010039491 Sarcoma Diseases 0.000 description 2
- 241000187747 Streptomyces Species 0.000 description 2
- 101100226845 Strongylocentrotus purpuratus EGF2 gene Proteins 0.000 description 2
- 241000711517 Torovirus Species 0.000 description 2
- 102100039037 Vascular endothelial growth factor A Human genes 0.000 description 2
- 108020005202 Viral DNA Proteins 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 238000007792 addition Methods 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 210000004204 blood vessel Anatomy 0.000 description 2
- 210000000988 bone and bone Anatomy 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 239000003638 chemical reducing agent Substances 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000013611 chromosomal DNA Substances 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 239000013599 cloning vector Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 210000000805 cytoplasm Anatomy 0.000 description 2
- 230000004069 differentiation Effects 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000001502 gel electrophoresis Methods 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 210000002216 heart Anatomy 0.000 description 2
- 239000000185 hemagglutinin Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 210000003917 human chromosome Anatomy 0.000 description 2
- 210000004754 hybrid cell Anatomy 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 238000007901 in situ hybridization Methods 0.000 description 2
- 230000002458 infectious effect Effects 0.000 description 2
- 206010022000 influenza Diseases 0.000 description 2
- 230000000968 intestinal effect Effects 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 210000004940 nucleus Anatomy 0.000 description 2
- 229940049954 penicillin Drugs 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 102000020233 phosphotransferase Human genes 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 2
- 229920002223 polystyrene Polymers 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 238000012552 review Methods 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 239000002356 single layer Substances 0.000 description 2
- 210000004927 skin cell Anatomy 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 230000002459 sustained effect Effects 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000014621 translational initiation Effects 0.000 description 2
- 210000003606 umbilical vein Anatomy 0.000 description 2
- 230000008728 vascular permeability Effects 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 description 1
- GJCOSYZMQJWQCA-UHFFFAOYSA-N 9H-xanthene Chemical compound C1=CC=C2CC3=CC=CC=C3OC2=C1 GJCOSYZMQJWQCA-UHFFFAOYSA-N 0.000 description 1
- 102000013563 Acid Phosphatase Human genes 0.000 description 1
- 108010051457 Acid Phosphatase Proteins 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108700028369 Alleles Proteins 0.000 description 1
- 102100022987 Angiogenin Human genes 0.000 description 1
- 108020004491 Antisense DNA Proteins 0.000 description 1
- 240000003291 Armoracia rusticana Species 0.000 description 1
- 235000011330 Armoracia rusticana Nutrition 0.000 description 1
- 241001203868 Autographa californica Species 0.000 description 1
- 241000201370 Autographa californica nucleopolyhedrovirus Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- SGHZXLIDFTYFHQ-UHFFFAOYSA-L Brilliant Blue Chemical compound [Na+].[Na+].C=1C=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C(=CC=CC=2)S([O-])(=O)=O)C=CC=1N(CC)CC1=CC=CC(S([O-])(=O)=O)=C1 SGHZXLIDFTYFHQ-UHFFFAOYSA-L 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 108091062157 Cis-regulatory element Proteins 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 108091033380 Coding strand Proteins 0.000 description 1
- 241001274613 Corvus frugilegus Species 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 241000255581 Drosophila <fruit fly, genus> Species 0.000 description 1
- 241001131785 Escherichia coli HB101 Species 0.000 description 1
- 241000701959 Escherichia virus Lambda Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 102000003971 Fibroblast Growth Factor 1 Human genes 0.000 description 1
- 102100031706 Fibroblast growth factor 1 Human genes 0.000 description 1
- 241000700662 Fowlpox virus Species 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 208000002966 Giant Cell Tumor of Bone Diseases 0.000 description 1
- 241000713813 Gibbon ape leukemia virus Species 0.000 description 1
- 208000032612 Glial tumor Diseases 0.000 description 1
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 1
- 102100036263 Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial Human genes 0.000 description 1
- 208000009889 Herpes Simplex Diseases 0.000 description 1
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 1
- 108010033040 Histones Proteins 0.000 description 1
- 101000619542 Homo sapiens E3 ubiquitin-protein ligase parkin Proteins 0.000 description 1
- 101001001786 Homo sapiens Glutamyl-tRNA(Gln) amidotransferase subunit C, mitochondrial Proteins 0.000 description 1
- 101000999079 Homo sapiens Radiation-inducible immediate-early gene IEX-1 Proteins 0.000 description 1
- 101000879840 Homo sapiens Serglycin Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 1
- 241000725303 Human immunodeficiency virus Species 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000004310 Ion Channels Human genes 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- 208000034693 Laceration Diseases 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 101000808007 Mus musculus Vascular endothelial growth factor A Proteins 0.000 description 1
- 241000713883 Myeloproliferative sarcoma virus Species 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 108020004711 Nucleic Acid Probes Proteins 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108700026244 Open Reading Frames Proteins 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010033276 Peptide Fragments Proteins 0.000 description 1
- 102000007079 Peptide Fragments Human genes 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical group [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 102000016611 Proteoglycans Human genes 0.000 description 1
- 108010067787 Proteoglycans Proteins 0.000 description 1
- 241000125945 Protoparvovirus Species 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 108020005067 RNA Splice Sites Proteins 0.000 description 1
- 239000013614 RNA sample Substances 0.000 description 1
- 208000017442 Retinal disease Diseases 0.000 description 1
- 206010038923 Retinopathy Diseases 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 241000714474 Rous sarcoma virus Species 0.000 description 1
- 101100379247 Salmo trutta apoa1 gene Proteins 0.000 description 1
- 102100037344 Serglycin Human genes 0.000 description 1
- 206010040943 Skin Ulcer Diseases 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 241000713896 Spleen necrosis virus Species 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- 102000004357 Transferases Human genes 0.000 description 1
- 108090000992 Transferases Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 208000025865 Ulcer Diseases 0.000 description 1
- 208000024780 Urticaria Diseases 0.000 description 1
- 108091008605 VEGF receptors Proteins 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- 208000000558 Varicose Ulcer Diseases 0.000 description 1
- 102000009484 Vascular Endothelial Growth Factor Receptors Human genes 0.000 description 1
- 101000614028 Vespa velutina Phospholipase A1 verutoxin-1 Proteins 0.000 description 1
- IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 1
- 230000003187 abdominal effect Effects 0.000 description 1
- 239000006659 ace medium Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 230000006154 adenylylation Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 108010072788 angiogenin Proteins 0.000 description 1
- 238000002399 angioplasty Methods 0.000 description 1
- 210000004102 animal cell Anatomy 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 239000003816 antisense DNA Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 238000011888 autopsy Methods 0.000 description 1
- 238000000376 autoradiography Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 210000002798 bone marrow cell Anatomy 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 210000000424 bronchial epithelial cell Anatomy 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 208000035269 cancer or benign tumor Diseases 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 210000000748 cardiovascular system Anatomy 0.000 description 1
- 230000003197 catalytic effect Effects 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 108091092328 cellular RNA Proteins 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- 210000002987 choroid plexus Anatomy 0.000 description 1
- 208000037976 chronic inflammation Diseases 0.000 description 1
- 230000006020 chronic inflammation Effects 0.000 description 1
- 238000012875 competitive assay Methods 0.000 description 1
- 230000006957 competitive inhibition Effects 0.000 description 1
- 239000003636 conditioned culture medium Substances 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 208000029078 coronary artery disease Diseases 0.000 description 1
- 210000004351 coronary vessel Anatomy 0.000 description 1
- 238000002316 cosmetic surgery Methods 0.000 description 1
- 239000011243 crosslinked material Substances 0.000 description 1
- 239000000287 crude extract Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000003599 detergent Substances 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000000032 diagnostic agent Substances 0.000 description 1
- 229940039227 diagnostic agent Drugs 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- OZRNSSUDZOLUSN-LBPRGKRZSA-N dihydrofolic acid Chemical compound N=1C=2C(=O)NC(N)=NC=2NCC=1CNC1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 OZRNSSUDZOLUSN-LBPRGKRZSA-N 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- 231100000676 disease causative agent Toxicity 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 235000013399 edible fruits Nutrition 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000013020 embryo development Effects 0.000 description 1
- 210000001671 embryonic stem cell Anatomy 0.000 description 1
- 210000003038 endothelium Anatomy 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000001400 expression cloning Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 239000012847 fine chemical Substances 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 238000013467 fragmentation Methods 0.000 description 1
- 238000006062 fragmentation reaction Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- ZZUFCTLCJUWOSV-UHFFFAOYSA-N furosemide Chemical compound C1=C(Cl)C(S(=O)(=O)N)=CC(C(O)=O)=C1NCC1=CC=CO1 ZZUFCTLCJUWOSV-UHFFFAOYSA-N 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 208000005017 glioblastoma Diseases 0.000 description 1
- 102000018146 globin Human genes 0.000 description 1
- 108060003196 globin Proteins 0.000 description 1
- 230000002414 glycolytic effect Effects 0.000 description 1
- 239000006451 grace's insect medium Substances 0.000 description 1
- 239000011544 gradient gel Substances 0.000 description 1
- RQFCJASXJCIDSX-UUOKFMHZSA-N guanosine 5'-monophosphate Chemical compound C1=2NC(N)=NC(=O)C=2N=CN1[C@@H]1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H]1O RQFCJASXJCIDSX-UUOKFMHZSA-N 0.000 description 1
- 208000024348 heart neoplasm Diseases 0.000 description 1
- 210000003958 hematopoietic stem cell Anatomy 0.000 description 1
- 210000003494 hepatocyte Anatomy 0.000 description 1
- 239000000833 heterodimer Substances 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000014726 immortalization of host cell Effects 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000977 initiatory effect Effects 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 230000002601 intratumoral effect Effects 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 230000026045 iodination Effects 0.000 description 1
- 238000006192 iodination reaction Methods 0.000 description 1
- 230000007794 irritation Effects 0.000 description 1
- 208000028867 ischemia Diseases 0.000 description 1
- 238000002955 isolation Methods 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
- 210000002510 keratinocyte Anatomy 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 101150109249 lacI gene Proteins 0.000 description 1
- 101150066555 lacZ gene Proteins 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 210000003041 ligament Anatomy 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 238000001638 lipofection Methods 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 208000037841 lung tumor Diseases 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 230000031864 metaphase Effects 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 230000002297 mitogenic effect Effects 0.000 description 1
- 210000003098 myoblast Anatomy 0.000 description 1
- 230000002107 myocardial effect Effects 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 239000002853 nucleic acid probe Substances 0.000 description 1
- 238000011580 nude mouse model Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 229940046166 oligodeoxynucleotide Drugs 0.000 description 1
- 238000011275 oncology therapy Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 102000045222 parkin Human genes 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000003239 periodontal effect Effects 0.000 description 1
- 210000002379 periodontal ligament Anatomy 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 210000001428 peripheral nervous system Anatomy 0.000 description 1
- 102000013415 peroxidase activity proteins Human genes 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 125000000864 peroxy group Chemical group O(O*)* 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 150000003906 phosphoinositides Chemical class 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 230000001817 pituitary effect Effects 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 208000024361 placenta neoplasm Diseases 0.000 description 1
- -1 pol III Proteins 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 102000054765 polymorphisms of proteins Human genes 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 230000030788 protein refolding Effects 0.000 description 1
- 239000012264 purified product Substances 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 238000003127 radioimmunoassay Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 210000003296 saliva Anatomy 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 230000001568 sexual effect Effects 0.000 description 1
- 238000007390 skin biopsy Methods 0.000 description 1
- 231100000019 skin ulcer Toxicity 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 230000000392 somatic effect Effects 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 230000008093 supporting effect Effects 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 229920002994 synthetic fiber Polymers 0.000 description 1
- 230000002123 temporal effect Effects 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000008467 tissue growth Effects 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000011830 transgenic mouse model Methods 0.000 description 1
- 230000008733 trauma Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 231100000397 ulcer Toxicity 0.000 description 1
- 230000002485 urinary effect Effects 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 230000006459 vascular development Effects 0.000 description 1
- 208000019553 vascular disease Diseases 0.000 description 1
- 210000005166 vasculature Anatomy 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 229920001285 xanthan gum Polymers 0.000 description 1
- 210000005253 yeast cell Anatomy 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
- C07K14/52—Cytokines; Lymphokines; Interferons
-
- 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
- C07K14/475—Growth factors; Growth regulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/02—Stomatological preparations, e.g. drugs for caries, aphtae, periodontitis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/02—Drugs for dermatological disorders for treating wounds, ulcers, burns, scars, keloids, or the like
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/08—Drugs for skeletal disorders for bone diseases, e.g. rachitism, Paget's disease
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
- A61P35/04—Antineoplastic agents specific for metastasis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/08—Vasodilators for multiple indications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/14—Vasoprotectives; Antihaemorrhoidals; Drugs for varicose therapy; Capillary stabilisers
-
- 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/49—Platelet-derived growth factor [PDGF]
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2799/00—Uses of viruses
- C12N2799/02—Uses of viruses as vector
- C12N2799/021—Uses of viruses as vector for the expression of a heterologous nucleic acid
- C12N2799/026—Uses of viruses as vector for the expression of a heterologous nucleic acid where the vector is derived from a baculovirus
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cardiology (AREA)
- Heart & Thoracic Surgery (AREA)
- Gastroenterology & Hepatology (AREA)
- Biomedical Technology (AREA)
- Toxicology (AREA)
- Physical Education & Sports Medicine (AREA)
- Diabetes (AREA)
- Rheumatology (AREA)
- Dermatology (AREA)
- General Engineering & Computer Science (AREA)
- Vascular Medicine (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Pain & Pain Management (AREA)
- Oncology (AREA)
- Obesity (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/465,968 | 1995-06-06 | ||
| US08/465,968 US6608182B1 (en) | 1994-03-08 | 1995-06-06 | Human vascular endothelial growth factor 2 |
| PCT/US1996/009001 WO1996039515A1 (en) | 1995-06-06 | 1996-06-06 | Human vascular endothelial growth factor 2 |
Related Child Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP11147333A Division JP2000069982A (ja) | 1995-06-06 | 1999-05-26 | ヒト血管内皮増殖因子２ |
| JP2007106593A Division JP2007244388A (ja) | 1995-06-06 | 2007-04-13 | ヒト血管内皮増殖因子２ |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH11513883A true JPH11513883A (ja) | 1999-11-30 |
Family
ID=23849909
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP9501427A Withdrawn JPH11513883A (ja) | 1995-06-06 | 1996-06-06 | ヒト血管内皮増殖因子２ |
| JP11147333A Withdrawn JP2000069982A (ja) | 1995-06-06 | 1999-05-26 | ヒト血管内皮増殖因子２ |
| JP2007106593A Pending JP2007244388A (ja) | 1995-06-06 | 2007-04-13 | ヒト血管内皮増殖因子２ |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP11147333A Withdrawn JP2000069982A (ja) | 1995-06-06 | 1999-05-26 | ヒト血管内皮増殖因子２ |
| JP2007106593A Pending JP2007244388A (ja) | 1995-06-06 | 2007-04-13 | ヒト血管内皮増殖因子２ |
Country Status (10)
| Country | Link |
|---|---|
| US (3) | US6608182B1 (enExample) |
| EP (1) | EP0837934B1 (enExample) |
| JP (3) | JPH11513883A (enExample) |
| KR (1) | KR100511692B1 (enExample) |
| CN (2) | CN1552855A (enExample) |
| AT (1) | ATE347595T1 (enExample) |
| AU (1) | AU714484B2 (enExample) |
| CA (1) | CA2224093C (enExample) |
| DE (1) | DE69636752T2 (enExample) |
| WO (1) | WO1996039515A1 (enExample) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007244388A (ja) * | 1995-06-06 | 2007-09-27 | Human Genome Sciences Inc | ヒト血管内皮増殖因子２ |
Families Citing this family (72)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6824777B1 (en) | 1992-10-09 | 2004-11-30 | Licentia Ltd. | Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy |
| US5932540A (en) | 1994-03-08 | 1999-08-03 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| ATE309360T1 (de) | 1994-03-08 | 2005-11-15 | Human Genome Sciences Inc | Vaskularer endothelialer wachstumsfaktor 2 |
| US6734285B2 (en) | 1994-03-08 | 2004-05-11 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 proteins and compositions |
| US7186688B1 (en) | 1994-03-08 | 2007-03-06 | Human Genome Sciences, Inc. | Methods of stimulating angiogenesis in a patient by administering vascular endothelial growth factor 2 |
| US6040157A (en) * | 1994-03-08 | 2000-03-21 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US7153827B1 (en) | 1994-03-08 | 2006-12-26 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 and methods of use |
| US7109308B1 (en) * | 1994-03-08 | 2006-09-19 | Human Genome Sciences, Inc. | Antibodies to human vascular endothelial growth factor 2 |
| US7597886B2 (en) | 1994-11-07 | 2009-10-06 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US6130071A (en) * | 1997-02-05 | 2000-10-10 | Helsinki University Licensing, Ltd. | Vascular endothelial growth factor C (VEGF-C) ΔCys156 protein and gene, and uses thereof |
| US6245530B1 (en) | 1995-08-01 | 2001-06-12 | Ludwig Institute For Cancer Research | Receptor ligand |
| US6403088B1 (en) | 1995-08-01 | 2002-06-11 | Helsinki University Licensing, Ltd. | Antibodies reactive with VEGF-C, a ligand for the Flt4 receptor tyrosine kinase (VEGFR-3) |
| US6645933B1 (en) | 1995-08-01 | 2003-11-11 | Helsinki University Licensing Ltd. Oy | Receptor ligand VEGF-C |
| WO2002060950A2 (en) | 1994-11-14 | 2002-08-08 | Ludwig Institute For Cancer Research | Flt4(vegfr-3) as a target for tumor imaging and anti-tumor therapy |
| US6221839B1 (en) | 1994-11-14 | 2001-04-24 | Helsinki University Licensing Ltd. Oy | FIt4 ligand and methods of use |
| US6818220B1 (en) | 1994-11-14 | 2004-11-16 | Licentia Ltd. | Vascular endothelial growth factor C (VEGF-C) protein and gene mutants thereof, and uses thereof |
| WO1998033917A1 (en) * | 1994-11-14 | 1998-08-06 | The Ludwig Institute For Cancer Research | Vascular endothelial growth factor c (vegf-c) protein and gene, mutants thereof, and uses thereof |
| US7429646B1 (en) | 1995-06-05 | 2008-09-30 | Human Genome Sciences, Inc. | Antibodies to human tumor necrosis factor receptor-like 2 |
| US7727761B2 (en) | 1995-08-01 | 2010-06-01 | Vegenics Limited | Vascular endothelial growth factor C (VEGF-C) protein and gene, mutants thereof, and uses thereof |
| US6361946B1 (en) | 1997-02-05 | 2002-03-26 | Licentia Ltd | Vascular endothelial growth factor C (VEGF-C) protein and gene, mutants thereof, and uses thereof |
| AU755708B2 (en) * | 1995-08-01 | 2002-12-19 | Vegenics Limited | Receptor ligand VEGF-C |
| AU2003201371B2 (en) * | 1995-08-01 | 2007-03-01 | Helsinki University Licensing Ltd. Oy | Receptor Ligand VEGF-C |
| ATE242809T1 (de) * | 1995-09-08 | 2003-06-15 | Genentech Inc | Vegf-verwandtes protein |
| US6994989B1 (en) | 1995-11-08 | 2006-02-07 | Immunex Corp. | FLK-1 binding proteins |
| WO1997017442A1 (en) | 1995-11-08 | 1997-05-15 | Immunex Corporation | Flk-1 binding protein |
| WO1997033904A1 (en) | 1996-03-12 | 1997-09-18 | Human Genome Sciences, Inc. | Death domain containing receptors |
| US6713061B1 (en) | 1996-03-12 | 2004-03-30 | Human Genome Sciences, Inc. | Death domain containing receptors |
| US7357927B2 (en) | 1996-03-12 | 2008-04-15 | Human Genome Sciences, Inc. | Death domain containing receptors |
| US6635743B1 (en) | 1996-03-22 | 2003-10-21 | Human Genome Sciences, Inc. | Apoptosis inducing molecule II and methods of use |
| US7964190B2 (en) | 1996-03-22 | 2011-06-21 | Human Genome Sciences, Inc. | Methods and compositions for decreasing T-cell activity |
| US20060171907A1 (en) * | 1996-11-21 | 2006-08-03 | The Procter & Gamble Company | Oral care compositions providing enhanced whitening and stain prevention |
| US7125714B2 (en) | 1997-02-05 | 2006-10-24 | Licentia Ltd. | Progenitor cell materials and methods |
| AU6691098A (en) * | 1997-03-07 | 1998-09-22 | Wistar Institute Of Anatomy & Biology, The | Method and compositions for healing tissue defects and inducing hypervascularityin mammalian tissue |
| US6676937B1 (en) | 1998-03-09 | 2004-01-13 | Caritas St. Elizabeth's Medical Center Of Boston Inc. | Compositions and methods for modulating vascularization |
| EP1062319A4 (en) * | 1998-03-13 | 2003-04-23 | Human Genome Sciences Inc | VASCULAR ENDOTHELIAL GROWTH FACTOR 2 |
| CA2345276C (en) | 1998-10-09 | 2011-03-29 | Ludwig Institute For Cancer Research | Flt4 (vegfr-3) as a target for tumor imaging and anti-tumor therapy |
| US6958147B1 (en) | 1998-10-26 | 2005-10-25 | Licentia Ltd | Use of VEGF-C to prevent restenosis |
| US6783953B1 (en) | 1998-12-22 | 2004-08-31 | Janssen Pharmaceutica N.V. | Vascular endothelial growth factor-X |
| US7223724B1 (en) | 1999-02-08 | 2007-05-29 | Human Genome Sciences, Inc. | Use of vascular endothelial growth factor to treat photoreceptor cells |
| EP2357192A1 (en) | 1999-02-26 | 2011-08-17 | Human Genome Sciences, Inc. | Human endokine alpha and methods of use |
| WO2000058511A1 (en) | 1999-03-26 | 2000-10-05 | Ludwig Institute For Cancer Research | Screening and therapy for lymphatic disorders involving the flt4 receptor tyrosine kinase (vegfr-3) |
| US6764820B2 (en) * | 1999-03-26 | 2004-07-20 | Ludwig Institute For Cancer Research | Screening for lymphatic disorders involving the FLT4 receptor tyrosine kinase (VEGFR-3) |
| US6965010B2 (en) * | 2000-02-25 | 2005-11-15 | Licentia, Ltd. | Materials and methods involving hybrid vascular endothelial growth factor DNAs and proteins |
| US7291597B2 (en) * | 2000-04-06 | 2007-11-06 | Franco Wayne P | Growth factor therapy mobilization of stem cells into the peripheral blood |
| US7288521B2 (en) * | 2000-04-06 | 2007-10-30 | Franco Wayne P | Growth factor therapy mobilization of stem cells into the peripheral blood |
| JP2003530838A (ja) | 2000-04-12 | 2003-10-21 | ヒューマン ゲノム サイエンシズ インコーポレイテッド | アルブミン融合タンパク質 |
| CN1211126C (zh) | 2000-08-04 | 2005-07-20 | 人体基因组科学有限公司 | 血管内皮生长因子2 |
| US7067317B2 (en) | 2000-12-07 | 2006-06-27 | Sangamo Biosciences, Inc. | Regulation of angiogenesis with zinc finger proteins |
| EP1341914A2 (en) | 2000-12-07 | 2003-09-10 | Sangamo Biosciences Inc. | Regulation of angiogenesis with zinc finger proteins |
| US7611711B2 (en) * | 2001-01-17 | 2009-11-03 | Vegenics Limited | VEGFR-3 inhibitor materials and methods |
| WO2002083704A1 (en) | 2001-04-13 | 2002-10-24 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| AU2002252631A1 (en) * | 2001-04-13 | 2002-10-28 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US7402312B2 (en) | 2001-04-13 | 2008-07-22 | Human Genome Sciences, Inc. | Antibodies to vascular endothelial growth factor 2 (VEGF-2) |
| US20050232921A1 (en) * | 2001-04-13 | 2005-10-20 | Rosen Craig A | Vascular endothelial growth factor 2 |
| CN1555488A (zh) * | 2001-07-12 | 2004-12-15 | 路德维格癌症研究院 | 淋巴管内皮细胞物质及方法 |
| AU2002331669A1 (en) | 2001-08-23 | 2003-03-10 | The Wistar Institute Of Anatomy And Biology | An organotypic intestinal culture and methods of use thereof |
| US20040214766A1 (en) * | 2001-10-01 | 2004-10-28 | Kari Alitalo | VEGF-C or VEGF-D materials and methods for treatment of neuropathologies |
| US20030113324A1 (en) * | 2001-10-01 | 2003-06-19 | Kari Alitalo | Neuropilin/VEGF-C/VEGFR-3 materials and methods |
| ES2425738T3 (es) | 2001-12-21 | 2013-10-17 | Human Genome Sciences, Inc. | Proteínas de fusión de la albúmina |
| WO2003104428A2 (en) | 2002-01-21 | 2003-12-18 | Vaccinex, Inc. | Gene differentially expressed in breast and bladder cancer and encoded polypeptides |
| US20040120950A1 (en) * | 2002-12-20 | 2004-06-24 | Kari Alitalo | Modulation of VEGF-C/VEGFR-3 interactions in the treatment of rheumatoid arthritis |
| US20040248796A1 (en) * | 2003-02-04 | 2004-12-09 | Kari Alitalo | VEGF-B and PDGF modulation of stem cells |
| WO2005016963A2 (en) * | 2003-06-12 | 2005-02-24 | Ludwig Institute For Cancer Research | Heparin binding veger-3 ligands |
| EP1635860A2 (en) * | 2003-06-12 | 2006-03-22 | Ludwig Institute For Cancer Research | Use of vegf-c or vegf-d in reconstructive surgery |
| US7597884B2 (en) | 2004-08-09 | 2009-10-06 | Alios Biopharma, Inc. | Hyperglycosylated polypeptide variants and methods of use |
| US7358085B2 (en) | 2005-02-28 | 2008-04-15 | Sangamo Biosciences, Inc. | Anti-angiogenic methods and compositions |
| US20090035346A1 (en) * | 2005-06-21 | 2009-02-05 | Pervasis Therpeutics, Inc. | Methods and Compositions for Enhancing Vascular Access |
| KR101642846B1 (ko) | 2007-12-26 | 2016-07-26 | 백시넥스 인코포레이티드 | 항-ｃ35 항체 병용 치료 및 방법 |
| US20110172293A1 (en) | 2008-07-08 | 2011-07-14 | Fish Jason E | Methods and Compositions for Modulating Angiogenesis |
| SMT202000088T1 (it) | 2013-02-18 | 2020-03-13 | Vegenics Pty Ltd | Molecole leganti ligandi e relativi usi |
| CN108339154A (zh) * | 2017-01-25 | 2018-07-31 | 中国科学院遗传与发育生物学研究所 | 一种诱导颅脑损伤组织再生的功能生物材料及其应用 |
| CN111303271B (zh) * | 2020-02-19 | 2022-02-01 | 西安交通大学医学院第一附属医院 | 一种用于治疗肺纤维化的血小板源性生长因子重组疫苗及其应用 |
Family Cites Families (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0186084B1 (en) | 1984-12-24 | 1991-09-04 | Merck & Co. Inc. | Brain-derived growth factor |
| US5073492A (en) * | 1987-01-09 | 1991-12-17 | The Johns Hopkins University | Synergistic composition for endothelial cell growth |
| JPS6438100A (en) | 1987-07-31 | 1989-02-08 | Toray Industries | Vascular endothelial cell growth factor |
| JPH02117698A (ja) | 1988-10-27 | 1990-05-02 | Toray Ind Inc | 血管内皮細胞成長因子 |
| US5240848A (en) | 1988-11-21 | 1993-08-31 | Monsanto Company | Dna sequences encoding human vascular permeability factor having 189 amino acids |
| US5693622A (en) | 1989-03-21 | 1997-12-02 | Vical Incorporated | Expression of exogenous polynucleotide sequences cardiac muscle of a mammal |
| EP0399816B1 (en) | 1989-05-24 | 1995-12-20 | Merck & Co. Inc. | Purification and characterization of a glioma-derived growth factor |
| US5219739A (en) | 1989-07-27 | 1993-06-15 | Scios Nova Inc. | DNA sequences encoding bVEGF120 and hVEGF121 and methods for the production of bovine and human vascular endothelial cell growth factors, bVEGF120 and hVEGF121 |
| US5194596A (en) * | 1989-07-27 | 1993-03-16 | California Biotechnology Inc. | Production of vascular endothelial cell growth factor |
| CA2051796A1 (en) | 1990-09-21 | 1992-03-22 | Marvin L. Bayne | Vascular endothelial cell growth factor ii |
| WO1992014748A1 (en) | 1991-02-22 | 1992-09-03 | American Cyanamid Company | Identification of a novel human receptor tyrosine kinase gene |
| DE69229454T2 (de) | 1991-03-28 | 2000-01-05 | Merck & Co., Inc. | Untereinheit-C des vaskulären endothelialen Zellwachstumsfaktors |
| US5185438A (en) | 1991-04-02 | 1993-02-09 | The Trustees Of Princeton University | Nucleic acids encoding hencatoporetic stem cell receptor flk-2 |
| US5234908A (en) | 1991-04-12 | 1993-08-10 | Creative Biomolecules, Inc. | Method of treating gastrointestinal ulcers with platelet derived growth factor |
| US5661133B1 (en) | 1991-11-12 | 1999-06-01 | Univ Michigan | Collateral blood vessel formation in cardiac muscle by injecting a dna sequence encoding an angiogenic protein |
| US5861301A (en) | 1992-02-20 | 1999-01-19 | American Cayanamid Company | Recombinant kinase insert domain containing receptor and gene encoding same |
| US5326695A (en) * | 1992-05-15 | 1994-07-05 | Ludwig Institute For Cancer Research | Platelet derived growth factor agonists |
| US5776755A (en) * | 1992-10-09 | 1998-07-07 | Helsinki University Licensing, Ltd. | FLT4, a receptor tyrosine kinase |
| AU694097B2 (en) | 1992-11-18 | 1998-07-16 | Arch Development Corporation | Adenovirus-mediated gene transfer to cardiac and vascular smooth muscle |
| US5922572A (en) | 1994-01-25 | 1999-07-13 | Human Genome Sciences, Inc. | Polynucleotides encoding haemopoietic maturation factor |
| US5817485A (en) | 1994-03-08 | 1998-10-06 | Human Genome Sciences, Inc. | Nucleic acids and cells for recombinant production of fibroblast growth factor-10 |
| US5633147A (en) | 1994-03-08 | 1997-05-27 | Human Genome Sciences, Inc. | Transforming growth factor αH1 |
| ATE309360T1 (de) | 1994-03-08 | 2005-11-15 | Human Genome Sciences Inc | Vaskularer endothelialer wachstumsfaktor 2 |
| US5932540A (en) | 1994-03-08 | 1999-08-03 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US6608182B1 (en) | 1994-03-08 | 2003-08-19 | Human Genome Sciences, Inc. | Human vascular endothelial growth factor 2 |
| US6040157A (en) | 1994-03-08 | 2000-03-21 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| AU708903B2 (en) | 1994-08-23 | 1999-08-12 | Human Genome Sciences, Inc. | Human chemokine polypeptides |
| US5652225A (en) | 1994-10-04 | 1997-07-29 | St. Elizabeth's Medical Center Of Boston, Inc. | Methods and products for nucleic acid delivery |
| US6245530B1 (en) * | 1995-08-01 | 2001-06-12 | Ludwig Institute For Cancer Research | Receptor ligand |
| US6130071A (en) * | 1997-02-05 | 2000-10-10 | Helsinki University Licensing, Ltd. | Vascular endothelial growth factor C (VEGF-C) ΔCys156 protein and gene, and uses thereof |
| US6221839B1 (en) * | 1994-11-14 | 2001-04-24 | Helsinki University Licensing Ltd. Oy | FIt4 ligand and methods of use |
| WO1998033917A1 (en) | 1994-11-14 | 1998-08-06 | The Ludwig Institute For Cancer Research | Vascular endothelial growth factor c (vegf-c) protein and gene, mutants thereof, and uses thereof |
| US6403088B1 (en) * | 1995-08-01 | 2002-06-11 | Helsinki University Licensing, Ltd. | Antibodies reactive with VEGF-C, a ligand for the Flt4 receptor tyrosine kinase (VEGFR-3) |
| US6645933B1 (en) * | 1995-08-01 | 2003-11-11 | Helsinki University Licensing Ltd. Oy | Receptor ligand VEGF-C |
| US5792453A (en) | 1995-02-28 | 1998-08-11 | The Regents Of The University Of California | Gene transfer-mediated angiogenesis therapy |
| US5928939A (en) | 1995-03-01 | 1999-07-27 | Ludwig Institute For Cancer Research | Vascular endothelial growth factor-b and dna coding therefor |
| US5607918A (en) | 1995-03-01 | 1997-03-04 | Ludwig Institute For Cancer Research | Vascular endothelial growth factor-B and DNA coding therefor |
| ATE483733T1 (de) | 1995-06-14 | 2010-10-15 | Univ California | Hochaffine humane antikörper gegen tumorantigene |
| US6361946B1 (en) | 1997-02-05 | 2002-03-26 | Licentia Ltd | Vascular endothelial growth factor C (VEGF-C) protein and gene, mutants thereof, and uses thereof |
| WO1997008320A1 (en) | 1995-08-18 | 1997-03-06 | Morphosys Gesellschaft Für Proteinoptimierung Mbh | Protein/(poly)peptide libraries |
| ATE242809T1 (de) | 1995-09-08 | 2003-06-15 | Genentech Inc | Vegf-verwandtes protein |
| US6121246A (en) | 1995-10-20 | 2000-09-19 | St. Elizabeth's Medical Center Of Boston, Inc. | Method for treating ischemic tissue |
| WO1997017442A1 (en) | 1995-11-08 | 1997-05-15 | Immunex Corporation | Flk-1 binding protein |
| US5641750A (en) | 1995-11-29 | 1997-06-24 | Amgen Inc. | Methods for treating photoreceptors using glial cell line-derived neurotrophic factor (GDNF) protein product |
| JP2000517174A (ja) | 1996-08-13 | 2000-12-26 | ヒューマン・ジェノム・サイエンシズ・インコーポレイテッド | ケラチノサイト増殖因子―２（ｋｇｆ―２または線維芽細胞増殖因子―１２、ｆｇｆ―１２） |
| CA2263890C (en) | 1996-08-23 | 2013-05-14 | Ludwig Institute For Cancer Research | Recombinant vascular endothelial cell growth factor d (vegf-d) |
| WO1998024811A2 (en) | 1996-12-06 | 1998-06-11 | Zymogenetics, Inc. | Vascular endothelial growth factor |
| AU6691098A (en) | 1997-03-07 | 1998-09-22 | Wistar Institute Of Anatomy & Biology, The | Method and compositions for healing tissue defects and inducing hypervascularityin mammalian tissue |
| CN1260835A (zh) | 1997-04-25 | 2000-07-19 | 科莱特诺医疗公司 | 截短的vegf相关蛋白质 |
| AU745965B2 (en) | 1997-06-06 | 2002-04-11 | Asat Ag Applied Science & Technology | Anti-GPIIb/IIIa recombinant antibodies |
| AU8536998A (en) | 1997-06-10 | 1998-12-30 | Max-Planck-Gesellschaft Zur Forderung Der Wissenschaften E.V. | Regulatory sequences involved in hypoxia regulated gene expression and uses thereof |
| NZ501990A (en) | 1997-07-08 | 2002-09-27 | Viventia Biotech Inc | Compositions containing antigen-binding fragments that recognise the antigen recognised by a recombinant 4B5 antibody |
| WO1999008522A1 (en) | 1997-08-15 | 1999-02-25 | Ludwig Institute For Cancer Research | Stimulation, modulation and/or inhibition of endothelial proteolytic activity and/or angiogenic activity |
| GB9722131D0 (en) | 1997-10-20 | 1997-12-17 | Medical Res Council | Method |
| JP2001520875A (ja) | 1997-10-27 | 2001-11-06 | メルク エンド カムパニー インコーポレーテッド | 血管新生の刺激のための遺伝子治療 |
| EP1062319A4 (en) | 1998-03-13 | 2003-04-23 | Human Genome Sciences Inc | VASCULAR ENDOTHELIAL GROWTH FACTOR 2 |
| CA2361615A1 (en) | 1999-02-08 | 2000-08-10 | Human Genome Sciences, Inc. | The use of vascular endothelial growth factor 2 antagonist in the treatment of an injury to or disorder of an eye |
| DE10027695A1 (de) | 1999-05-27 | 2001-04-19 | Max Delbrueck Centrum | Vakzine gegen konformationsabhängige Antigene sowie gegen Antigene, die keine oder nicht ausschließlich Proteine oder Peptide sind |
| CA2376018A1 (en) | 1999-06-03 | 2000-12-14 | Human Genome Sciences, Inc. | Angiogenic proteins and uses thereof |
| MXPA02007449A (es) | 2000-02-03 | 2003-04-14 | Millennium Pharm Inc | Anticuerpos anti-ccr2 humanizados y metodos para el uso de los mismos. |
| TWI373343B (en) | 2000-02-10 | 2012-10-01 | Abbott Gmbh & Co Kg | Antibodies that bind human interleukin-18 and methods of making and using |
| CN1211126C (zh) | 2000-08-04 | 2005-07-20 | 人体基因组科学有限公司 | 血管内皮生长因子2 |
| WO2002083704A1 (en) | 2001-04-13 | 2002-10-24 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| AU2002252631A1 (en) | 2001-04-13 | 2002-10-28 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
| US20030170786A1 (en) | 2001-04-13 | 2003-09-11 | Rosen Craig A. | Vascular endothelial growth factor 2 |
| AU2002313770A1 (en) | 2002-04-12 | 2003-12-02 | Human Genome Sciences, Inc. | Vascular endothelial growth factor 2 |
-
1995
- 1995-06-06 US US08/465,968 patent/US6608182B1/en not_active Expired - Fee Related
-
1996
- 1996-06-06 CA CA002224093A patent/CA2224093C/en not_active Expired - Fee Related
- 1996-06-06 CN CNA2004100022261A patent/CN1552855A/zh active Pending
- 1996-06-06 WO PCT/US1996/009001 patent/WO1996039515A1/en not_active Ceased
- 1996-06-06 AU AU60467/96A patent/AU714484B2/en not_active Withdrawn - After Issue
- 1996-06-06 CN CN96194405A patent/CN1186518A/zh active Pending
- 1996-06-06 JP JP9501427A patent/JPH11513883A/ja not_active Withdrawn
- 1996-06-06 KR KR1019970709003A patent/KR100511692B1/ko not_active Expired - Fee Related
- 1996-06-06 EP EP96918130A patent/EP0837934B1/en not_active Revoked
- 1996-06-06 DE DE69636752T patent/DE69636752T2/de not_active Revoked
- 1996-06-06 AT AT96918130T patent/ATE347595T1/de not_active IP Right Cessation
-
1999
- 1999-05-26 JP JP11147333A patent/JP2000069982A/ja not_active Withdrawn
-
2002
- 2002-04-23 US US10/127,551 patent/US7115392B2/en not_active Expired - Fee Related
-
2007
- 2007-04-13 JP JP2007106593A patent/JP2007244388A/ja active Pending
-
2008
- 2008-10-24 US US12/258,109 patent/US20100143360A1/en not_active Abandoned
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2007244388A (ja) * | 1995-06-06 | 2007-09-27 | Human Genome Sciences Inc | ヒト血管内皮増殖因子２ |
Also Published As
| Publication number | Publication date |
|---|---|
| KR100511692B1 (ko) | 2005-12-27 |
| EP0837934B1 (en) | 2006-12-06 |
| US6608182B1 (en) | 2003-08-19 |
| AU714484B2 (en) | 2000-01-06 |
| DE69636752T2 (de) | 2007-10-11 |
| DE69636752D1 (de) | 2007-01-18 |
| US20100143360A1 (en) | 2010-06-10 |
| KR19990022522A (ko) | 1999-03-25 |
| CN1552855A (zh) | 2004-12-08 |
| ATE347595T1 (de) | 2006-12-15 |
| JP2000069982A (ja) | 2000-03-07 |
| AU6046796A (en) | 1996-12-24 |
| MX9709243A (es) | 1998-03-31 |
| CA2224093A1 (en) | 1996-12-12 |
| EP0837934A4 (en) | 2000-11-02 |
| JP2007244388A (ja) | 2007-09-27 |
| WO1996039515A1 (en) | 1996-12-12 |
| EP0837934A1 (en) | 1998-04-29 |
| US7115392B2 (en) | 2006-10-03 |
| CA2224093C (en) | 2003-03-25 |
| US20020120123A1 (en) | 2002-08-29 |
| CN1186518A (zh) | 1998-07-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JPH11513883A (ja) | ヒト血管内皮増殖因子２ | |
| JP2007244388A5 (enExample) | ||
| US7576189B2 (en) | Antibodies to human vascular endothelial growth factor 2 and methods of using the same | |
| JP2000508894A (ja) | 細胞外／上皮増殖因子ｈｃａｂａ５８ｘ | |
| JP2000513567A (ja) | 上皮分化因子 | |
| JPH11507504A (ja) | 線維芽細胞増殖因子１３ | |
| AU713364B2 (en) | Transforming growth factor alpha HII | |
| US20030022312A1 (en) | Human hepatoma-derived growth factor-2 | |
| JP2000508531A (ja) | 細胞外／上皮増殖因子様タンパク質 | |
| AU752206B2 (en) | Extracellular/epidermal growth factor like protein | |
| JP2001517064A (ja) | トランスフォーミング増殖因子アルファｈｉ | |
| AU716100B2 (en) | Human vascular endothelial growth factor 3 | |
| US20020119487A1 (en) | Human stem cell antigen 2 | |
| JP2000506371A (ja) | 成長因子ｈｔｔｅｒ３６ | |
| AU2005200574A1 (en) | Human Vascular Endothelial Factor 2 | |
| JPH11507506A (ja) | 内皮単球活性ポリペプチドｉｉｉ | |
| MXPA97009570A (en) | Growth factor 3 endothelial, vascular, hum | |
| JP2003047488A (ja) | ヒト肝ガン由来増殖因子−２ | |
| JP2003079371A (ja) | ヒト血管内皮増殖因子３ | |
| MXPA97009243A (en) | Human vascular endothelial growth factor | |
| CA2413012A1 (en) | Human vascular endothelial growth factor 2 | |
| JP2001507561A (ja) | 線維芽細胞増殖因子１４ | |
| JP2003245089A (ja) | 免疫細胞サイトカイン | |
| AU1951100A (en) | Human vascular endothelial growth factor 2 | |
| AU3818402A (en) | Transforming growth factor alpha HII |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20051122 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20060110 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20060323 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20060515 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20060707 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20070116 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20070413 |
|
| A911 | Transfer to examiner for re-examination before appeal (zenchi) |
Free format text: JAPANESE INTERMEDIATE CODE: A911 Effective date: 20070607 |
|
| A912 | Re-examination (zenchi) completed and case transferred to appeal board |
Free format text: JAPANESE INTERMEDIATE CODE: A912 Effective date: 20070705 |
|
| A761 | Written withdrawal of application |
Free format text: JAPANESE INTERMEDIATE CODE: A761 Effective date: 20100210 |