JP2008536479A - ジスルフィド架橋を有するタンパク質の発現法 - Google Patents
ジスルフィド架橋を有するタンパク質の発現法 Download PDFInfo
- Publication number
- JP2008536479A JP2008536479A JP2007556197A JP2007556197A JP2008536479A JP 2008536479 A JP2008536479 A JP 2008536479A JP 2007556197 A JP2007556197 A JP 2007556197A JP 2007556197 A JP2007556197 A JP 2007556197A JP 2008536479 A JP2008536479 A JP 2008536479A
- Authority
- JP
- Japan
- Prior art keywords
- disintegrin
- protein
- domain
- sequence
- thioredoxin
- 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.)
- Pending
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 242
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 230
- 238000000034 method Methods 0.000 title claims abstract description 115
- 230000014509 gene expression Effects 0.000 title claims abstract description 72
- 101800001224 Disintegrin Proteins 0.000 claims abstract description 158
- 108060008226 thioredoxin Proteins 0.000 claims abstract description 121
- 102000002933 Thioredoxin Human genes 0.000 claims abstract description 117
- 229940094937 thioredoxin Drugs 0.000 claims abstract description 113
- 230000015572 biosynthetic process Effects 0.000 claims abstract description 33
- 102000006010 Protein Disulfide-Isomerase Human genes 0.000 claims abstract description 24
- 108020003519 protein disulfide isomerase Proteins 0.000 claims abstract description 24
- 230000004071 biological effect Effects 0.000 claims abstract description 20
- 108010079911 Thioredoxin-disulfide reductase Proteins 0.000 claims abstract description 17
- 108010063907 Glutathione Reductase Proteins 0.000 claims abstract description 11
- 102100036442 Glutathione reductase, mitochondrial Human genes 0.000 claims abstract description 11
- 210000004027 cell Anatomy 0.000 claims description 113
- 102000006495 integrins Human genes 0.000 claims description 55
- 108010044426 integrins Proteins 0.000 claims description 55
- 241000588724 Escherichia coli Species 0.000 claims description 52
- 210000000805 cytoplasm Anatomy 0.000 claims description 48
- 102000037865 fusion proteins Human genes 0.000 claims description 46
- 108020001507 fusion proteins Proteins 0.000 claims description 46
- 210000004899 c-terminal region Anatomy 0.000 claims description 43
- 238000003776 cleavage reaction Methods 0.000 claims description 35
- 230000007017 scission Effects 0.000 claims description 35
- 101150057627 trxB gene Proteins 0.000 claims description 21
- 150000001413 amino acids Chemical group 0.000 claims description 19
- 239000002243 precursor Substances 0.000 claims description 19
- 102000013090 Thioredoxin-Disulfide Reductase Human genes 0.000 claims description 15
- 241000894006 Bacteria Species 0.000 claims description 14
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 13
- 101150043276 Lon gene Proteins 0.000 claims description 12
- 101150093139 ompT gene Proteins 0.000 claims description 12
- 230000002401 inhibitory effect Effects 0.000 claims description 11
- 239000013604 expression vector Substances 0.000 claims description 10
- 239000012634 fragment Substances 0.000 claims description 10
- 239000003446 ligand Substances 0.000 claims description 10
- 239000000178 monomer Substances 0.000 claims description 10
- 239000003998 snake venom Substances 0.000 claims description 10
- 208000010110 spontaneous platelet aggregation Diseases 0.000 claims description 10
- 230000033115 angiogenesis Effects 0.000 claims description 9
- 238000001727 in vivo Methods 0.000 claims description 8
- 102000005962 receptors Human genes 0.000 claims description 8
- 108020003175 receptors Proteins 0.000 claims description 8
- 108010012236 Chemokines Proteins 0.000 claims description 6
- 102000019034 Chemokines Human genes 0.000 claims description 6
- 230000034005 thiol-disulfide exchange Effects 0.000 claims description 6
- 206010027476 Metastases Diseases 0.000 claims description 5
- 230000009401 metastasis Effects 0.000 claims description 5
- 239000003053 toxin Substances 0.000 claims description 5
- 231100000765 toxin Toxicity 0.000 claims description 5
- 108700012359 toxins Proteins 0.000 claims description 5
- 102100023700 C-C motif chemokine 16 Human genes 0.000 claims description 4
- 101000978375 Homo sapiens C-C motif chemokine 16 Proteins 0.000 claims description 4
- 108060003951 Immunoglobulin Proteins 0.000 claims description 4
- 241000239226 Scorpiones Species 0.000 claims description 4
- 230000008859 change Effects 0.000 claims description 4
- 102000018358 immunoglobulin Human genes 0.000 claims description 4
- 230000017854 proteolysis Effects 0.000 claims description 4
- 239000000126 substance Substances 0.000 claims description 4
- 102000004127 Cytokines Human genes 0.000 claims description 3
- 108090000695 Cytokines Proteins 0.000 claims description 3
- 108010090109 Fibrolase Proteins 0.000 claims description 3
- 101000832769 Homo sapiens Disintegrin and metalloproteinase domain-containing protein 9 Proteins 0.000 claims description 3
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 claims description 3
- 101000808011 Homo sapiens Vascular endothelial growth factor A Proteins 0.000 claims description 3
- 108010050904 Interferons Proteins 0.000 claims description 3
- 102000014150 Interferons Human genes 0.000 claims description 3
- 108010001014 Plasminogen Activators Proteins 0.000 claims description 3
- 102000001938 Plasminogen Activators Human genes 0.000 claims description 3
- 239000003102 growth factor Substances 0.000 claims description 3
- 102000055277 human IL2 Human genes 0.000 claims description 3
- 102000058223 human VEGFA Human genes 0.000 claims description 3
- 229940047124 interferons Drugs 0.000 claims description 3
- 229940127126 plasminogen activator Drugs 0.000 claims description 3
- 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 2
- 101710164760 Chlorotoxin Proteins 0.000 claims description 2
- 101000599940 Homo sapiens Interferon gamma Proteins 0.000 claims description 2
- 101500025624 Homo sapiens Transforming growth factor beta-2 Proteins 0.000 claims description 2
- 102000009524 Vascular Endothelial Growth Factor A Human genes 0.000 claims description 2
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 claims description 2
- 230000021164 cell adhesion Effects 0.000 claims description 2
- 230000004663 cell proliferation Effects 0.000 claims description 2
- QPAKKWCQMHUHNI-GQIQPHNSSA-N chlorotoxin Chemical compound C([C@H]1C(=O)NCC(=O)N2CCC[C@H]2C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H]2CSSC[C@H]3C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H]4CSSC[C@@H](C(N[C@@H](CCSC)C(=O)N5CCC[C@H]5C(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](CCCNC(N)=N)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)CNC(=O)CNC(=O)[C@H](CSSC[C@H](NC(=O)[C@H](CC(C)C)NC2=O)C(=O)N[C@@H](CCCNC(N)=N)C(N)=O)NC4=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N3)=O)NC(=O)[C@@H](N)CCSC)C1=CC=C(O)C=C1 QPAKKWCQMHUHNI-GQIQPHNSSA-N 0.000 claims description 2
- 229960005534 chlorotoxin Drugs 0.000 claims description 2
- 102000043557 human IFNG Human genes 0.000 claims description 2
- 229940072221 immunoglobulins Drugs 0.000 claims description 2
- 210000004185 liver Anatomy 0.000 claims description 2
- 201000003874 Common Variable Immunodeficiency Diseases 0.000 claims 1
- 101000801481 Homo sapiens Tissue-type plasminogen activator Proteins 0.000 claims 1
- 102000011931 Nucleoproteins Human genes 0.000 claims 1
- 108010061100 Nucleoproteins Proteins 0.000 claims 1
- 229920002704 polyhistidine Polymers 0.000 claims 1
- 230000001131 transforming effect Effects 0.000 claims 1
- KNJNGVKTAFTUFL-OCMUWRIYSA-N ω-conotoxin Chemical compound N([C@@H](CO)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H]1C(N[C@@H](CSSC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H]1C(N[C@@H](CCCN=C(N)N)C(=O)N[C@H](CO)C(=O)NCC(=O)N[C@H](CCCCN)C(=O)N[C@H](CSSC1)C(N)=O)=O)=O)C(=O)[C@@H]1CSSC[C@@H](N)C(=O)N[C@H](CCCCN)C(=O)NCC(=O)N[C@H](CCCCN)C(=O)NCC(=O)N[C@H](C)C(=O)N[C@@H](CCCCN)C(=O)N1 KNJNGVKTAFTUFL-OCMUWRIYSA-N 0.000 claims 1
- 108091058550 ω-conotoxin Proteins 0.000 claims 1
- 108700021041 Disintegrin Proteins 0.000 abstract description 40
- 239000013598 vector Substances 0.000 abstract description 40
- 230000004927 fusion Effects 0.000 abstract description 15
- 230000001086 cytosolic effect Effects 0.000 abstract description 10
- 108091005804 Peptidases Proteins 0.000 abstract description 7
- 239000004365 Protease Substances 0.000 abstract description 7
- 230000007812 deficiency Effects 0.000 abstract 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 198
- 108010063294 contortrostatin Proteins 0.000 description 146
- 108010057810 vicrostatin Proteins 0.000 description 72
- 108020004705 Codon Proteins 0.000 description 42
- 239000013615 primer Substances 0.000 description 38
- 210000001322 periplasm Anatomy 0.000 description 35
- 230000000694 effects Effects 0.000 description 33
- 102000004190 Enzymes Human genes 0.000 description 27
- 108090000790 Enzymes Proteins 0.000 description 27
- 102000004316 Oxidoreductases Human genes 0.000 description 27
- 108090000854 Oxidoreductases Proteins 0.000 description 27
- 229940088598 enzyme Drugs 0.000 description 27
- 108091008146 restriction endonucleases Proteins 0.000 description 27
- 102000004195 Isomerases Human genes 0.000 description 24
- 108090000769 Isomerases Proteins 0.000 description 24
- 108010006035 Metalloproteases Proteins 0.000 description 24
- 102000005741 Metalloproteases Human genes 0.000 description 24
- 230000037361 pathway Effects 0.000 description 24
- 230000002441 reversible effect Effects 0.000 description 21
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 20
- 230000002829 reductive effect Effects 0.000 description 19
- 230000001580 bacterial effect Effects 0.000 description 18
- 230000006870 function Effects 0.000 description 18
- 238000010367 cloning Methods 0.000 description 17
- 101150077538 gor gene Proteins 0.000 description 17
- 230000012010 growth Effects 0.000 description 17
- 108700010070 Codon Usage Proteins 0.000 description 16
- 206010028980 Neoplasm Diseases 0.000 description 16
- 238000006664 bond formation reaction Methods 0.000 description 16
- IYMAXBFPHPZYIK-BQBZGAKWSA-N Arg-Gly-Asp Chemical compound NC(N)=NCCC[C@H](N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(O)=O IYMAXBFPHPZYIK-BQBZGAKWSA-N 0.000 description 15
- 239000002502 liposome Substances 0.000 description 15
- 239000012528 membrane Substances 0.000 description 15
- 239000002773 nucleotide Substances 0.000 description 15
- 125000003729 nucleotide group Chemical group 0.000 description 15
- 235000018417 cysteine Nutrition 0.000 description 14
- 210000004379 membrane Anatomy 0.000 description 14
- 239000000203 mixture Substances 0.000 description 14
- 239000013612 plasmid Substances 0.000 description 14
- 108010076504 Protein Sorting Signals Proteins 0.000 description 13
- 230000003993 interaction Effects 0.000 description 13
- 230000035772 mutation Effects 0.000 description 13
- 238000007254 oxidation reaction Methods 0.000 description 13
- 238000000746 purification Methods 0.000 description 13
- 108050005205 Glutaredoxin Proteins 0.000 description 12
- 102000017278 Glutaredoxin Human genes 0.000 description 12
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 12
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 12
- 108010076818 TEV protease Proteins 0.000 description 12
- 235000001014 amino acid Nutrition 0.000 description 12
- 238000000338 in vitro Methods 0.000 description 12
- 230000005764 inhibitory process Effects 0.000 description 12
- 230000003647 oxidation Effects 0.000 description 12
- 239000000047 product Substances 0.000 description 12
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 11
- 230000001419 dependent effect Effects 0.000 description 11
- 239000000710 homodimer Substances 0.000 description 11
- 238000006317 isomerization reaction Methods 0.000 description 11
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 11
- 239000003155 DNA primer Substances 0.000 description 10
- 125000000151 cysteine group Chemical class N[C@@H](CS)C(=O)* 0.000 description 10
- 238000004519 manufacturing process Methods 0.000 description 10
- 230000001590 oxidative effect Effects 0.000 description 10
- 206010006187 Breast cancer Diseases 0.000 description 9
- 208000026310 Breast neoplasm Diseases 0.000 description 9
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
- 108091028043 Nucleic acid sequence Proteins 0.000 description 9
- 102000035175 foldases Human genes 0.000 description 9
- 108091005749 foldases Proteins 0.000 description 9
- 230000009467 reduction Effects 0.000 description 9
- 238000011144 upstream manufacturing Methods 0.000 description 9
- 102100024616 Platelet endothelial cell adhesion molecule Human genes 0.000 description 8
- 101150044072 cn gene Proteins 0.000 description 8
- 239000000539 dimer Substances 0.000 description 8
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 8
- 230000006698 induction Effects 0.000 description 8
- 108020004999 messenger RNA Proteins 0.000 description 8
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 102100023038 WD and tetratricopeptide repeats protein 1 Human genes 0.000 description 7
- 238000004949 mass spectrometry Methods 0.000 description 7
- 230000004048 modification Effects 0.000 description 7
- 238000012986 modification Methods 0.000 description 7
- 230000008569 process Effects 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 230000032258 transport Effects 0.000 description 7
- AZQWKYJCGOJGHM-UHFFFAOYSA-N 1,4-benzoquinone Chemical compound O=C1C=CC(=O)C=C1 AZQWKYJCGOJGHM-UHFFFAOYSA-N 0.000 description 6
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 6
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 6
- 102000016359 Fibronectins Human genes 0.000 description 6
- 108010067306 Fibronectins Proteins 0.000 description 6
- 101000881168 Homo sapiens SPARC Proteins 0.000 description 6
- 102000035195 Peptidases Human genes 0.000 description 6
- 101000621511 Potato virus M (strain German) RNA silencing suppressor Proteins 0.000 description 6
- 101100235786 Rattus norvegicus Lonp1 gene Proteins 0.000 description 6
- 102100037599 SPARC Human genes 0.000 description 6
- 108020004566 Transfer RNA Proteins 0.000 description 6
- 108010031318 Vitronectin Proteins 0.000 description 6
- 102100035140 Vitronectin Human genes 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- 210000004204 blood vessel Anatomy 0.000 description 6
- 230000003197 catalytic effect Effects 0.000 description 6
- 150000002632 lipids Chemical class 0.000 description 6
- 102000004196 processed proteins & peptides Human genes 0.000 description 6
- 230000012846 protein folding Effects 0.000 description 6
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 6
- UKGGPJNBONZZCM-WDSKDSINSA-N Asp-Pro Chemical compound OC(=O)C[C@H](N)C(=O)N1CCC[C@H]1C(O)=O UKGGPJNBONZZCM-WDSKDSINSA-N 0.000 description 5
- 108020004414 DNA Proteins 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 5
- 102100036407 Thioredoxin Human genes 0.000 description 5
- 208000007536 Thrombosis Diseases 0.000 description 5
- 108010093581 aspartyl-proline Proteins 0.000 description 5
- 239000003054 catalyst Substances 0.000 description 5
- 239000013078 crystal Substances 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 238000002825 functional assay Methods 0.000 description 5
- 238000001840 matrix-assisted laser desorption--ionisation time-of-flight mass spectrometry Methods 0.000 description 5
- 229920001184 polypeptide Polymers 0.000 description 5
- 230000002265 prevention Effects 0.000 description 5
- 239000000725 suspension Substances 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 238000013518 transcription Methods 0.000 description 5
- 230000035897 transcription Effects 0.000 description 5
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 4
- 241000271045 Agkistrodon contortrix contortrix Species 0.000 description 4
- 108010047852 Integrin alphaVbeta3 Proteins 0.000 description 4
- 101710137500 T7 RNA polymerase Proteins 0.000 description 4
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 4
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 4
- 239000003242 anti bacterial agent Substances 0.000 description 4
- 229940088710 antibiotic agent Drugs 0.000 description 4
- 210000002469 basement membrane Anatomy 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 229960003669 carbenicillin Drugs 0.000 description 4
- FPPNZSSZRUTDAP-UWFZAAFLSA-N carbenicillin Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)C(C(O)=O)C1=CC=CC=C1 FPPNZSSZRUTDAP-UWFZAAFLSA-N 0.000 description 4
- 229960005091 chloramphenicol Drugs 0.000 description 4
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 4
- 238000004132 cross linking Methods 0.000 description 4
- 238000000132 electrospray ionisation Methods 0.000 description 4
- 239000003527 fibrinolytic agent Substances 0.000 description 4
- 235000019253 formic acid Nutrition 0.000 description 4
- 229960003180 glutathione Drugs 0.000 description 4
- 230000002209 hydrophobic effect Effects 0.000 description 4
- 230000008595 infiltration Effects 0.000 description 4
- 238000001764 infiltration Methods 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 239000011159 matrix material Substances 0.000 description 4
- 229910021645 metal ion Inorganic materials 0.000 description 4
- 238000003032 molecular docking Methods 0.000 description 4
- 238000005457 optimization Methods 0.000 description 4
- 238000004007 reversed phase HPLC Methods 0.000 description 4
- 230000002459 sustained effect Effects 0.000 description 4
- 150000003573 thiols Chemical class 0.000 description 4
- XLBBKEHLEPNMMF-SSUNCQRMSA-N 129038-42-2 Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CS)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(N)=O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)[C@@H](C)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CS)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CS)NC(=O)[C@H](CS)NC(=O)[C@H]1N(CCC1)C(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CS)NC(=O)[C@@H](N)CCC(O)=O)C1=CC=CC=C1 XLBBKEHLEPNMMF-SSUNCQRMSA-N 0.000 description 3
- 108010077805 Bacterial Proteins Proteins 0.000 description 3
- 108091026890 Coding region Proteins 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 241000206602 Eukaryota Species 0.000 description 3
- 108010024636 Glutathione Proteins 0.000 description 3
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 3
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 3
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 3
- 102000003992 Peroxidases Human genes 0.000 description 3
- 108010022425 Platelet Glycoprotein GPIIb-IIIa Complex Proteins 0.000 description 3
- 101000781681 Protobothrops flavoviridis Disintegrin triflavin Proteins 0.000 description 3
- 239000004098 Tetracycline Substances 0.000 description 3
- 239000000654 additive Substances 0.000 description 3
- 230000002776 aggregation Effects 0.000 description 3
- 238000004220 aggregation Methods 0.000 description 3
- 108010072041 arginyl-glycyl-aspartic acid Proteins 0.000 description 3
- 230000000975 bioactive effect Effects 0.000 description 3
- 230000005540 biological transmission Effects 0.000 description 3
- 201000011510 cancer Diseases 0.000 description 3
- 230000004712 cancer cell adhesion Effects 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 125000002228 disulfide group Chemical group 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 108010025752 echistatin Proteins 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 210000004907 gland Anatomy 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 238000012744 immunostaining Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 230000009545 invasion Effects 0.000 description 3
- 229930027917 kanamycin Natural products 0.000 description 3
- 229960000318 kanamycin Drugs 0.000 description 3
- 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 3
- 229930182823 kanamycin A Natural products 0.000 description 3
- 230000000813 microbial effect Effects 0.000 description 3
- 230000004899 motility Effects 0.000 description 3
- 108040007629 peroxidase activity proteins Proteins 0.000 description 3
- 230000002797 proteolythic effect Effects 0.000 description 3
- 230000035806 respiratory chain Effects 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 238000012163 sequencing technique Methods 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- 229960002180 tetracycline Drugs 0.000 description 3
- 229930101283 tetracycline Natural products 0.000 description 3
- 235000019364 tetracycline Nutrition 0.000 description 3
- 150000003522 tetracyclines Chemical class 0.000 description 3
- 229960000103 thrombolytic agent Drugs 0.000 description 3
- 230000014616 translation Effects 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 2
- HSTOKWSFWGCZMH-UHFFFAOYSA-N 3,3'-diaminobenzidine Chemical compound C1=C(N)C(N)=CC=C1C1=CC=C(N)C(N)=C1 HSTOKWSFWGCZMH-UHFFFAOYSA-N 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108010058207 Anistreplase Proteins 0.000 description 2
- 101000583080 Bunodosoma granuliferum Delta-actitoxin-Bgr2a Proteins 0.000 description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 101800000620 Disintegrin-like Proteins 0.000 description 2
- 108091006149 Electron carriers Proteins 0.000 description 2
- 241001646716 Escherichia coli K-12 Species 0.000 description 2
- 102000008946 Fibrinogen Human genes 0.000 description 2
- 108010049003 Fibrinogen Proteins 0.000 description 2
- 108010012088 Fibrinogen Receptors Proteins 0.000 description 2
- 102100037813 Focal adhesion kinase 1 Human genes 0.000 description 2
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 2
- WZUVPPKBWHMQCE-UHFFFAOYSA-N Haematoxylin Chemical compound C12=CC(O)=C(O)C=C2CC2(O)C1C1=CC=C(O)C(O)=C1OC2 WZUVPPKBWHMQCE-UHFFFAOYSA-N 0.000 description 2
- 102000002265 Human Growth Hormone Human genes 0.000 description 2
- 108010000521 Human Growth Hormone Proteins 0.000 description 2
- 239000000854 Human Growth Hormone Substances 0.000 description 2
- 102100022337 Integrin alpha-V Human genes 0.000 description 2
- 108010054278 Lac Repressors Proteins 0.000 description 2
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 2
- 108700005092 MHC Class II Genes Proteins 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 108010006519 Molecular Chaperones Proteins 0.000 description 2
- ACFIXJIJDZMPPO-NNYOXOHSSA-N NADPH Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](OP(O)(O)=O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 ACFIXJIJDZMPPO-NNYOXOHSSA-N 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 208000001132 Osteoporosis Diseases 0.000 description 2
- 238000012408 PCR amplification Methods 0.000 description 2
- 102000007456 Peroxiredoxin Human genes 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- 108010009583 Transforming Growth Factors Proteins 0.000 description 2
- 102000009618 Transforming Growth Factors Human genes 0.000 description 2
- 108010048673 Vitronectin Receptors Proteins 0.000 description 2
- 238000009825 accumulation Methods 0.000 description 2
- 238000001042 affinity chromatography Methods 0.000 description 2
- 230000001772 anti-angiogenic effect Effects 0.000 description 2
- 230000000118 anti-neoplastic effect Effects 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 102000006635 beta-lactamase Human genes 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 238000003570 cell viability assay Methods 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
- 238000004440 column chromatography Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 230000007711 cytoplasmic localization Effects 0.000 description 2
- 210000000172 cytosol Anatomy 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 150000002019 disulfides Chemical class 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 2
- 210000002889 endothelial cell Anatomy 0.000 description 2
- 230000002255 enzymatic effect Effects 0.000 description 2
- 231100000776 exotoxin Toxicity 0.000 description 2
- 239000002095 exotoxin Substances 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 230000002349 favourable effect Effects 0.000 description 2
- 229940012952 fibrinogen Drugs 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 238000010353 genetic engineering Methods 0.000 description 2
- 239000011521 glass Substances 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 101150109249 lacI gene Proteins 0.000 description 2
- 239000008101 lactose Substances 0.000 description 2
- HBMCYCKNGADUQP-CFIKXUEXSA-N leconotide Chemical compound NC(=N)NCCC[C@@H](C(=O)N[C@@H](C=S)C(N)=O)NC(=O)CNC(=O)[C@H](C(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](C=S)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](C=S)NC(=O)[C@H](CS)NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CS)CCSC)CC1=CC=C(O)C=C1 HBMCYCKNGADUQP-CFIKXUEXSA-N 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 239000012188 paraffin wax Substances 0.000 description 2
- 108030002458 peroxiredoxin Proteins 0.000 description 2
- 239000008194 pharmaceutical composition Substances 0.000 description 2
- 210000004623 platelet-rich plasma Anatomy 0.000 description 2
- 239000011148 porous material Substances 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000012545 processing Methods 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 238000009790 rate-determining step (RDS) Methods 0.000 description 2
- 238000003259 recombinant expression Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 238000000527 sonication Methods 0.000 description 2
- 238000010186 staining Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 101150118060 trxA gene Proteins 0.000 description 2
- 230000004614 tumor growth Effects 0.000 description 2
- 229960005356 urokinase Drugs 0.000 description 2
- 229960005486 vaccine Drugs 0.000 description 2
- 239000002435 venom Substances 0.000 description 2
- 231100000611 venom Toxicity 0.000 description 2
- 210000001048 venom Anatomy 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 230000003442 weekly effect Effects 0.000 description 2
- 238000012447 xenograft mouse model Methods 0.000 description 2
- 108091058552 ω-conotoxin CVID Proteins 0.000 description 2
- HYPYXGZDOYTYDR-HAJWAVTHSA-N 2-methyl-3-[(2e,6e,10e,14e)-3,7,11,15,19-pentamethylicosa-2,6,10,14,18-pentaenyl]naphthalene-1,4-dione Chemical compound C1=CC=C2C(=O)C(C/C=C(C)/CC/C=C(C)/CC/C=C(C)/CC/C=C(C)/CCC=C(C)C)=C(C)C(=O)C2=C1 HYPYXGZDOYTYDR-HAJWAVTHSA-N 0.000 description 1
- 108091022885 ADAM Proteins 0.000 description 1
- 102000029791 ADAM Human genes 0.000 description 1
- 206010002329 Aneurysm Diseases 0.000 description 1
- 206010002383 Angina Pectoris Diseases 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 206010003210 Arteriosclerosis Diseases 0.000 description 1
- 201000001320 Atherosclerosis Diseases 0.000 description 1
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 1
- 238000000035 BCA protein assay Methods 0.000 description 1
- 108020004256 Beta-lactamase Proteins 0.000 description 1
- 239000002028 Biomass Substances 0.000 description 1
- 208000006386 Bone Resorption Diseases 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 102000016289 Cell Adhesion Molecules Human genes 0.000 description 1
- 108010067225 Cell Adhesion Molecules Proteins 0.000 description 1
- 238000007808 Cell invasion assay Methods 0.000 description 1
- ACTIUHUUMQJHFO-UHFFFAOYSA-N Coenzym Q10 Natural products COC1=C(OC)C(=O)C(CC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)C)=C(C)C1=O ACTIUHUUMQJHFO-UHFFFAOYSA-N 0.000 description 1
- 102000005927 Cysteine Proteases Human genes 0.000 description 1
- 108010005843 Cysteine Proteases Proteins 0.000 description 1
- 108050008072 Cytochrome c oxidase subunit IV Proteins 0.000 description 1
- 102000000634 Cytochrome c oxidase subunit IV Human genes 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 108010016626 Dipeptides Proteins 0.000 description 1
- 101710140023 Disintegrin schistatin Proteins 0.000 description 1
- 230000010777 Disulfide Reduction Effects 0.000 description 1
- 108700033069 EC 1.97.-.- Proteins 0.000 description 1
- 238000002965 ELISA Methods 0.000 description 1
- 208000005189 Embolism Diseases 0.000 description 1
- 101710159936 Exactin Proteins 0.000 description 1
- BDAGIHXWWSANSR-UHFFFAOYSA-M Formate Chemical compound [O-]C=O BDAGIHXWWSANSR-UHFFFAOYSA-M 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
- 108010053070 Glutathione Disulfide Proteins 0.000 description 1
- 208000012766 Growth delay Diseases 0.000 description 1
- 102100031573 Hematopoietic progenitor cell antigen CD34 Human genes 0.000 description 1
- 101000777663 Homo sapiens Hematopoietic progenitor cell antigen CD34 Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 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
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- 102100025306 Integrin alpha-IIb Human genes 0.000 description 1
- 101710149643 Integrin alpha-IIb Proteins 0.000 description 1
- 108010042918 Integrin alpha5beta1 Proteins 0.000 description 1
- 102000012355 Integrin beta1 Human genes 0.000 description 1
- 108010022222 Integrin beta1 Proteins 0.000 description 1
- 102000008607 Integrin beta3 Human genes 0.000 description 1
- 108010020950 Integrin beta3 Proteins 0.000 description 1
- 208000032382 Ischaemic stroke Diseases 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 101100278567 Lelliottia amnigena dsbL gene Proteins 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 102000015930 Lon proteases Human genes 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 108700005089 MHC Class I Genes Proteins 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 102000005431 Molecular Chaperones Human genes 0.000 description 1
- 241000699666 Mus <mouse, genus> Species 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- 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 1
- 108010090127 Periplasmic Proteins Proteins 0.000 description 1
- 102000013566 Plasminogen Human genes 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 206010050661 Platelet aggregation inhibition Diseases 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 108010023294 Protease La Proteins 0.000 description 1
- 108030003943 Protein-disulfide reductases Proteins 0.000 description 1
- 208000010378 Pulmonary Embolism Diseases 0.000 description 1
- 229940122277 RNA polymerase inhibitor Drugs 0.000 description 1
- 206010039491 Sarcoma Diseases 0.000 description 1
- 208000006011 Stroke Diseases 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 108091008874 T cell receptors Proteins 0.000 description 1
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 1
- 101710167005 Thiol:disulfide interchange protein DsbD Proteins 0.000 description 1
- 102100032506 Thioredoxin reductase 3 Human genes 0.000 description 1
- 108091036066 Three prime untranslated region Proteins 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
- 208000001435 Thromboembolism Diseases 0.000 description 1
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
- 102100033571 Tissue-type plasminogen activator Human genes 0.000 description 1
- 235000012545 Vaccinium macrocarpon Nutrition 0.000 description 1
- 244000291414 Vaccinium oxycoccus Species 0.000 description 1
- 235000002118 Vaccinium oxycoccus Nutrition 0.000 description 1
- 101710099833 Venom protein Proteins 0.000 description 1
- 108010067390 Viral Proteins Proteins 0.000 description 1
- 238000005903 acid hydrolysis reaction Methods 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000012190 activator Substances 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 210000000577 adipose tissue Anatomy 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 101150024831 ahpC gene Proteins 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 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 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000004037 angiogenesis inhibitor Substances 0.000 description 1
- 230000006481 angiogenic pathway Effects 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000002001 anti-metastasis Effects 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 239000002246 antineoplastic agent Substances 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 208000011775 arteriosclerosis disease Diseases 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 230000004888 barrier function Effects 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000024279 bone resorption Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000012830 cancer therapeutic Substances 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 239000000969 carrier Substances 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 238000003352 cell adhesion assay Methods 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000006369 cell cycle progression Effects 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000012292 cell migration Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000004186 co-expression Effects 0.000 description 1
- 235000017471 coenzyme Q10 Nutrition 0.000 description 1
- ACTIUHUUMQJHFO-UPTCCGCDSA-N coenzyme Q10 Chemical compound COC1=C(OC)C(=O)C(C\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CC\C=C(/C)CCC=C(C)C)=C(C)C1=O ACTIUHUUMQJHFO-UPTCCGCDSA-N 0.000 description 1
- 230000001010 compromised effect Effects 0.000 description 1
- 235000004634 cranberry Nutrition 0.000 description 1
- 239000000179 crotalid venom Substances 0.000 description 1
- 108010045325 cyclic arginine-glycine-aspartic acid peptide Proteins 0.000 description 1
- 150000001944 cysteine derivatives Chemical class 0.000 description 1
- 210000004292 cytoskeleton Anatomy 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- 229910001873 dinitrogen Inorganic materials 0.000 description 1
- 229910001882 dioxygen Inorganic materials 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037765 diseases and disorders Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 150000004662 dithiols Chemical class 0.000 description 1
- 239000003937 drug carrier Substances 0.000 description 1
- 101150009558 dsbA gene Proteins 0.000 description 1
- 101150015101 dsbC gene Proteins 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000002330 electrospray ionisation mass spectrometry Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 101150012763 endA gene Proteins 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 210000001723 extracellular space Anatomy 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 239000003205 fragrance Substances 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 102000054767 gene variant Human genes 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 1
- 239000003966 growth inhibitor Substances 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 230000001744 histochemical effect Effects 0.000 description 1
- 230000005571 horizontal transmission Effects 0.000 description 1
- 230000036571 hydration Effects 0.000 description 1
- 238000006703 hydration reaction Methods 0.000 description 1
- 238000003384 imaging method Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 208000011379 keloid formation Diseases 0.000 description 1
- 108010060845 lactose permease Proteins 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000003589 local anesthetic agent Substances 0.000 description 1
- 229960005015 local anesthetics Drugs 0.000 description 1
- 239000000314 lubricant Substances 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 108010082117 matrigel Proteins 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000010534 mechanism of action Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 108010020410 methionine sulfoxide reductase Proteins 0.000 description 1
- 210000004088 microvessel Anatomy 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 108091005763 multidomain proteins Proteins 0.000 description 1
- 208000010125 myocardial infarction Diseases 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 238000011580 nude mouse model Methods 0.000 description 1
- 108010003052 omptin outer membrane protease Proteins 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 210000002997 osteoclast Anatomy 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 108010019188 periplasmic protein disulfide oxidoreductase Proteins 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 239000004417 polycarbonate Substances 0.000 description 1
- 229920000515 polycarbonate Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 230000001323 posttranslational effect Effects 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000002028 premature Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 230000007026 protein scission Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000007398 protein translocation Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 101150079601 recA gene Proteins 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 239000006176 redox buffer Substances 0.000 description 1
- NPCOQXAVBJJZBQ-UHFFFAOYSA-N reduced coenzyme Q9 Natural products COC1=C(O)C(C)=C(CC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)CCC=C(C)C)C(O)=C1OC NPCOQXAVBJJZBQ-UHFFFAOYSA-N 0.000 description 1
- 230000009331 reductive pathway Effects 0.000 description 1
- 230000001172 regenerating effect Effects 0.000 description 1
- 230000000754 repressing effect Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000027756 respiratory electron transport chain Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 230000011664 signaling Effects 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 229960000268 spectinomycin Drugs 0.000 description 1
- UNFWWIHTNXNPBV-WXKVUWSESA-N spectinomycin Chemical compound O([C@@H]1[C@@H](NC)[C@@H](O)[C@H]([C@@H]([C@H]1O1)O)NC)[C@]2(O)[C@H]1O[C@H](C)CC2=O UNFWWIHTNXNPBV-WXKVUWSESA-N 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 210000004895 subcellular structure Anatomy 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000001502 supplementing effect Effects 0.000 description 1
- 230000008093 supporting effect Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 108010074309 thioredoxin glutathione reductase Proteins 0.000 description 1
- IPIGTJPBWJEROO-UHFFFAOYSA-B thorium(4+);tetraphosphate Chemical compound [Th+4].[Th+4].[Th+4].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O IPIGTJPBWJEROO-UHFFFAOYSA-B 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 102000035160 transmembrane proteins Human genes 0.000 description 1
- 108091005703 transmembrane proteins Proteins 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 230000005747 tumor angiogenesis Effects 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
- 229940035936 ubiquinone Drugs 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 108020005087 unfolded proteins Proteins 0.000 description 1
- 210000003556 vascular endothelial cell Anatomy 0.000 description 1
- 230000008728 vascular permeability Effects 0.000 description 1
- 210000005166 vasculature Anatomy 0.000 description 1
- 235000019143 vitamin K2 Nutrition 0.000 description 1
- 239000011728 vitamin K2 Substances 0.000 description 1
- 229940041603 vitamin k 3 Drugs 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
- 230000037314 wound repair Effects 0.000 description 1
- AFVLVVWMAFSXCK-UHFFFAOYSA-N α-cyano-4-hydroxycinnamic acid Chemical compound OC(=O)C(C#N)=CC1=CC=C(O)C=C1 AFVLVVWMAFSXCK-UHFFFAOYSA-N 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
-
- 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
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
- C07K14/24—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria from Enterobacteriaceae (F), e.g. Citrobacter, Serratia, Proteus, Providencia, Morganella, Yersinia
- C07K14/245—Escherichia (G)
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6402—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals
- C12N9/6418—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from non-mammals from snakes
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/90—Isomerases (5.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/20—Fusion polypeptide containing a tag with affinity for a non-protein ligand
- C07K2319/21—Fusion polypeptide containing a tag with affinity for a non-protein ligand containing a His-tag
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/50—Fusion polypeptide containing protease site
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/90—Fusion polypeptide containing a motif for post-translational modification
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biomedical Technology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Gastroenterology & Hepatology (AREA)
- Biophysics (AREA)
- Marine Sciences & Fisheries (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Immunology (AREA)
- Epidemiology (AREA)
- Oncology (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US65252905P | 2005-02-11 | 2005-02-11 | |
| PCT/US2006/004413 WO2007086879A2 (en) | 2005-02-11 | 2006-02-09 | Method of expressing proteins with disulfide bridges |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2008536479A true JP2008536479A (ja) | 2008-09-11 |
| JP2008536479A5 JP2008536479A5 (cg-RX-API-DMAC10.html) | 2011-03-24 |
Family
ID=38309637
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2007556197A Pending JP2008536479A (ja) | 2005-02-11 | 2006-02-09 | ジスルフィド架橋を有するタンパク質の発現法 |
Country Status (7)
| Country | Link |
|---|---|
| US (4) | US7754850B2 (cg-RX-API-DMAC10.html) |
| EP (2) | EP2634252B1 (cg-RX-API-DMAC10.html) |
| JP (1) | JP2008536479A (cg-RX-API-DMAC10.html) |
| CN (1) | CN101535492A (cg-RX-API-DMAC10.html) |
| AU (1) | AU2006336468B2 (cg-RX-API-DMAC10.html) |
| CA (1) | CA2597647A1 (cg-RX-API-DMAC10.html) |
| WO (1) | WO2007086879A2 (cg-RX-API-DMAC10.html) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2019526253A (ja) * | 2016-08-25 | 2019-09-19 | ネクスゼン バイオテクノロジーズ インコーポレイテッドＮｅｘｇｅｎ Ｂｉｏｔｅｃｈｎｏｌｏｇｉｅｓ， Ｉｎｃ． | 皮膚細胞の増殖効果が増大したサソリ毒融合タンパク質及びそれを有効成分として含有するシワ改善、皮膚弾力の増大及びアンチエイジング化粧料組成物 |
Families Citing this family (22)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP2634252B1 (en) | 2005-02-11 | 2018-12-19 | University of Southern California | Method of expressing proteins with disulfide bridges |
| US8008256B2 (en) | 2006-05-01 | 2011-08-30 | University Of Southern California | Combination therapy for treatment of cancer |
| US7943728B2 (en) * | 2006-12-26 | 2011-05-17 | National Cheng Kung University | Disintegrin variants and their use in treating osteoporosis-induced bone loss and angiogenesis-related diseases |
| US8802394B2 (en) | 2008-11-13 | 2014-08-12 | Radu O. Minea | Method of expressing proteins with disulfide bridges with enhanced yields and activity |
| US8470554B2 (en) * | 2008-12-22 | 2013-06-25 | St. Jude Children's Research Hospital | Prokaryotic expression of soluble, active Dkk |
| CA2789679A1 (en) | 2010-02-11 | 2011-08-18 | University Of Southern California | Modified adam disintegrin domain polypeptides and uses thereof |
| CN102154336A (zh) * | 2011-01-25 | 2011-08-17 | 国家海洋局第三海洋研究所 | 嗜酸硫化芽孢杆菌硫氧还蛋白还原酶基因及其重组蛋白 |
| EP2527424A1 (en) * | 2011-05-26 | 2012-11-28 | Richter-Helm Bio Tec GmbH & Co. KG | Recombinant expression of soluble Interferon |
| WO2013076580A2 (en) * | 2011-11-23 | 2013-05-30 | Bioven 3 Limited | Recombinant proteins and their therapeutic uses |
| US20170054032A1 (en) | 2015-01-09 | 2017-02-23 | SanDisk Technologies, Inc. | Non-volatile memory having individually optimized silicide contacts and process therefor |
| CN105039377A (zh) * | 2015-08-24 | 2015-11-11 | 武汉真福医药股份有限公司 | 溶栓酶基因qk-02的表达方法及专用表达载体和工程菌 |
| WO2017083699A1 (en) * | 2015-11-13 | 2017-05-18 | University Of Southern California | Radiolabeled disintegrins as brachytherapy agents |
| US10258567B1 (en) | 2016-11-17 | 2019-04-16 | Grace Procurements Llc | Vaginal probiotic products and related processes |
| CN107384934A (zh) * | 2017-08-18 | 2017-11-24 | 安徽安科生物工程（集团）股份有限公司 | 重组人干扰素α2b的制备方法 |
| US11169583B2 (en) * | 2018-08-07 | 2021-11-09 | Western Digital Technologies, Inc. | Methods and apparatus for mitigating temperature increases in a solid state device (SSD) |
| EP3856760A1 (en) * | 2018-09-25 | 2021-08-04 | AbSci, LLC | Protein purification methods |
| IL282875B2 (en) * | 2018-11-08 | 2026-05-01 | Sutro Biopharma Inc | E. coli strains with oxygenated cytoplasm |
| US12351850B2 (en) | 2020-04-30 | 2025-07-08 | Sutro Biopharma, Inc. | Methods of producing full-length antibodies using E. coli |
| CN114107353B (zh) * | 2021-10-29 | 2024-07-23 | 成都佩德生物医药有限公司 | 一种高效表达多肽毒素的质粒及其制备方法与应用 |
| EP4361172A3 (en) | 2022-10-27 | 2024-05-29 | Science4Beauty Sp. z o.o. | Expression vector for recombinant u-conotoxin tiiia or tiiialamut expression in e.coli |
| CN117756949B (zh) * | 2024-02-21 | 2024-10-15 | 中国人民解放军军事科学院军事医学研究院 | 一种正痘病毒属融合抗原及应用 |
| CN120118913B (zh) * | 2025-05-14 | 2025-09-02 | 中国科学院苏州纳米技术与纳米仿生研究所 | 一种编码人防御素的核酸分子及制备人防御素方法和应用 |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2000245467A (ja) * | 1999-02-26 | 2000-09-12 | Agency Of Ind Science & Technol | Ｓｐａｒｃ融合タンパク質およびその製造方法 |
| JP2002528058A (ja) * | 1998-09-29 | 2002-09-03 | ザ・ユニバーシティー・オブ・サザン・カリフォルニア | コントートロスタチン（ｃｎ）、並びに転移及び他の症状の抑制におけるその使用方法 |
| JP2004500357A (ja) * | 1999-12-10 | 2004-01-08 | ザ・ユニバーシティー・オブ・サザン・カリフォルニア | コントートロスタチン（ｃｎ）並びに転移及びその他の症状の予防におけるその使用法 |
Family Cites Families (106)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4610879A (en) | 1984-01-06 | 1986-09-09 | University Of Southern California | Fibrinolytic enzyme from snake vernom |
| US5066592A (en) | 1988-03-08 | 1991-11-19 | Temple University Of The Commonwealth System Of Higher Education | Trigramin - a platelet aggregation inhibiting polypeptide |
| US6133029A (en) | 1988-03-21 | 2000-10-17 | Chiron Corporation | Replication defective viral vectors for infecting human cells |
| US5703055A (en) | 1989-03-21 | 1997-12-30 | Wisconsin Alumni Research Foundation | Generation of antibodies through lipid mediated DNA delivery |
| US5278324A (en) | 1990-08-28 | 1994-01-11 | Virginia Tech Intellectual Properties, Inc. | Water soluble derivatives of taxol |
| US5250683A (en) | 1991-09-23 | 1993-10-05 | Florida State University | Certain substituted taxanes and pharmaceutical compositions containing them |
| US5227400A (en) | 1991-09-23 | 1993-07-13 | Florida State University | Furyl and thienyl substituted taxanes and pharmaceutical compositions containing them |
| US5272171A (en) | 1992-02-13 | 1993-12-21 | Bristol-Myers Squibb Company | Phosphonooxy and carbonate derivatives of taxol |
| US5248796A (en) | 1992-06-18 | 1993-09-28 | Bristol-Myers Squibb Company | Taxol derivatives |
| US5254580A (en) | 1993-01-19 | 1993-10-19 | Bristol-Myers Squibb Company | 7,8-cyclopropataxanes |
| FR2705686B1 (fr) | 1993-05-28 | 1995-08-18 | Transgene Sa | Nouveaux adénovirus défectifs et lignées de complémentation correspondantes. |
| US6080569A (en) | 1993-06-24 | 2000-06-27 | Merck & Co., Inc. | Adenovirus vectors generated from helper viruses and helper-dependent vectors |
| US5814609A (en) * | 1993-10-22 | 1998-09-29 | University Of Southern California | Compositions containing a disintegrin and methods for its use in preventing metastasis and other conditions |
| US6710030B1 (en) * | 1993-10-22 | 2004-03-23 | University Of Southern California | Contortrostain (CN) and methods for its use in preventing metastasis and other conditions |
| US20030186884A1 (en) * | 2000-06-08 | 2003-10-02 | Markland Francis S. | Contortrostatin (CN) and methods for its use in preventing metastasis and other conditions |
| US7220724B2 (en) * | 1993-10-22 | 2007-05-22 | University Of Southern California | Contortrostatin CN and methods for its use in preventing metastasis and other conditions |
| US5731288A (en) * | 1993-10-22 | 1998-03-24 | University Of Southern California | Compositions containing contortrostatin and methods for the use thereof |
| US5658785A (en) | 1994-06-06 | 1997-08-19 | Children's Hospital, Inc. | Adeno-associated virus materials and methods |
| FR2725726B1 (fr) | 1994-10-17 | 1997-01-03 | Centre Nat Rech Scient | Vecteurs viraux et utilisation en therapie genique |
| US5641665A (en) | 1994-11-28 | 1997-06-24 | Vical Incorporated | Plasmids suitable for IL-2 expression |
| US6040295A (en) | 1995-01-13 | 2000-03-21 | Genemedicine, Inc. | Formulated nucleic acid compositions and methods of administering the same for gene therapy |
| AU695762B2 (en) | 1995-05-22 | 1998-08-20 | Government Of The United States Of America, As Represented By The Secretary Of The Department Of Health And Human Services, The | Retrovirus vectors derived from avian sarcoma leukosis viruses permitting transfer of genes into mammalian cells and therapeutic uses thereof |
| WO1998021350A1 (en) | 1996-11-13 | 1998-05-22 | Board Of Regents, The University Of Texas System | Diminishing viral gene expression by promoter replacement |
| US6660758B1 (en) | 1996-12-13 | 2003-12-09 | The Scripps Research Institute | Epothilone analogs |
| US6380394B1 (en) | 1996-12-13 | 2002-04-30 | The Scripps Research Institute | Epothilone analogs |
| US6441186B1 (en) | 1996-12-13 | 2002-08-27 | The Scripps Research Institute | Epothilone analogs |
| US6034072A (en) | 1997-02-10 | 2000-03-07 | Genemedicine, Inc. | IL-2 gene expression and delivery systems and uses |
| DE19713213A1 (de) | 1997-03-28 | 1998-10-01 | Ruebben Alexander Dr Med | Metallstent zur verlängerten Offenhaltung von Hohlorganen |
| AUPO742497A0 (en) * | 1997-06-18 | 1997-07-10 | N.J. Phillips Pty. Limited | An applicator |
| US6605599B1 (en) | 1997-07-08 | 2003-08-12 | Bristol-Myers Squibb Company | Epothilone derivatives |
| ES2290993T3 (es) | 1997-08-09 | 2008-02-16 | Bayer Schering Pharma Aktiengesellschaft | Nuevos derivados de epotilona, proceso para su produccion y su utilizacion farmaceutica. |
| US6365749B1 (en) | 1997-12-04 | 2002-04-02 | Bristol-Myers Squibb Company | Process for the preparation of ring-opened epothilone intermediates which are useful for the preparation of epothilone analogs |
| US6399638B1 (en) | 1998-04-21 | 2002-06-04 | Bristol-Myers Squibb Company | 12,13-modified epothilone derivatives |
| US6498257B1 (en) | 1998-04-21 | 2002-12-24 | Bristol-Myers Squibb Company | 2,3-olefinic epothilone derivatives |
| DE19820599A1 (de) | 1998-05-08 | 1999-11-11 | Biotechnolog Forschung Gmbh | Epothilonderivate, Verfahren zu deren Herstellung und deren Verwendung |
| DE19826988A1 (de) | 1998-06-18 | 1999-12-23 | Biotechnolog Forschung Gmbh | Epothilon-Nebenkomponenten |
| DE19848306A1 (de) | 1998-10-14 | 2000-04-20 | Schering Ag | Verfahren zur Herstellung von Epothilon B und Derivaten sowie Zwischenprodukte für dieses Verfahren |
| US6440944B2 (en) | 1998-10-16 | 2002-08-27 | Genvec, Inc. | Methods of administering adenoviral vectors |
| CN100381566C (zh) | 1998-11-20 | 2008-04-16 | 科森生物科学公司 | 产生环氧噻酮及其衍生物的重组方法和材料 |
| BR9916833A (pt) | 1998-12-22 | 2001-09-25 | Novartis Ag | Derivados de epotilona e seu uso como agentes antitumor |
| US6780620B1 (en) | 1998-12-23 | 2004-08-24 | Bristol-Myers Squibb Company | Microbial transformation method for the preparation of an epothilone |
| US6596875B2 (en) | 2000-02-07 | 2003-07-22 | James David White | Method for synthesizing epothilones and epothilone analogs |
| EE200100422A (et) | 1999-02-11 | 2002-12-16 | Schering Aktiengesellschaft | Epotilooni derivaadid, nende valmistamismeetod jafarmatseutiline kasutamine |
| EE200100431A (et) | 1999-02-18 | 2002-12-16 | Schering Aktiengesellschaft | 16-halogenoepotilooni derivaadid, nende valmistamismeetod ja farmatseutiline kasutamine |
| US6406722B1 (en) | 1999-02-18 | 2002-06-18 | Robert G. Gallaher | Method of treating viral infections and lesions with taxane compounds |
| US6387664B1 (en) * | 1999-02-26 | 2002-05-14 | Secretary Of Agency Of Industrial Science And Technology | Sparc fusion protein and method for producing the same |
| US7125893B1 (en) | 1999-04-30 | 2006-10-24 | Schering Ag | 6-alkenyl-, 6-alkinyl- and 6-epoxy-epothilone derivatives, process for their production, and their use in pharmaceutical preparations |
| US6878699B1 (en) | 1999-05-21 | 2005-04-12 | University Of Hawaii | Taccalonolide microtubule stabilizing agents |
| US20050042275A1 (en) | 1999-08-04 | 2005-02-24 | Jean-Claude Sonntag | Epothilone compositions |
| US6294374B1 (en) | 1999-10-08 | 2001-09-25 | The Scripps Research Institute | Use of catalytic antibodies for synthesizing epothilone |
| US6518421B1 (en) | 2000-03-20 | 2003-02-11 | Bristol-Myers Squibb Company | Process for the preparation of epothilone analogs |
| US6593115B2 (en) | 2000-03-24 | 2003-07-15 | Bristol-Myers Squibb Co. | Preparation of epothilone intermediates |
| TWI310684B (en) | 2000-03-27 | 2009-06-11 | Bristol Myers Squibb Co | Synergistic pharmaceutical kits for treating cancer |
| DE10020517A1 (de) | 2000-04-19 | 2001-10-25 | Schering Ag | Neue Epothilon-Derivate, Verfahren zu deren Herstellung und ihre pharmazeutische Verwendung |
| US6489314B1 (en) | 2001-04-03 | 2002-12-03 | Kosan Biosciences, Inc. | Epothilone derivatives and methods for making and using the same |
| US6998256B2 (en) | 2000-04-28 | 2006-02-14 | Kosan Biosciences, Inc. | Methods of obtaining epothilone D using crystallization and /or by the culture of cells in the presence of methyl oleate |
| US6589968B2 (en) | 2001-02-13 | 2003-07-08 | Kosan Biosciences, Inc. | Epothilone compounds and methods for making and using the same |
| US20020045609A1 (en) | 2000-05-26 | 2002-04-18 | Gary Ashley | Epothilone derivatives and methods for making and using the same |
| US6638742B1 (en) | 2000-07-07 | 2003-10-28 | University Of Portland | Methods for obtaining taxanes |
| UA75365C2 (en) | 2000-08-16 | 2006-04-17 | Bristol Myers Squibb Co | Epothilone analog polymorph modifications, a method for obtaining thereof (variants), a pharmaceutical composition based thereon |
| AU2002221693A1 (en) | 2000-10-16 | 2002-04-29 | Morphochem Ag | Epothilone synthesis components iii and iv: asymmetrically substituted acyloins and acyloin derivatives, method for the production thereof and method for the production of epithilone b, d and epothilone derivatives |
| WO2002042432A2 (en) | 2000-11-22 | 2002-05-30 | Novartis Ag | Epothilone resistant cell lines |
| CA2436326C (en) | 2001-01-09 | 2012-08-14 | Merck Patent Gesellschaft Mit Beschraenkter Haftung | Combination therapy using receptor tyrosine kinase inhibitors and angiogenesis inhibitors |
| SK8552003A3 (en) | 2001-01-25 | 2004-06-08 | Bristol Myers Squibb Co | Parenteral formulation containing epothilone analogs |
| DE60225666T2 (de) | 2001-01-25 | 2009-04-16 | Bristol-Myers Squibb Co. | Verfahren zur herstellung von pharmazeutischen zusammensetzungen enthaltend epothilon-analoga zur krebsbehandlung |
| US20030004338A1 (en) | 2001-02-01 | 2003-01-02 | Li Wen Sen | Process for the preparation of epothilone analogs |
| US6893859B2 (en) | 2001-02-13 | 2005-05-17 | Kosan Biosciences, Inc. | Epothilone derivatives and methods for making and using the same |
| EE200300397A (et) | 2001-02-20 | 2003-12-15 | Bristol-Myers Squibb Company | Epotilooni derivaadid refraktaarsete kasvajate raviks |
| IL156988A0 (en) | 2001-02-20 | 2004-02-08 | Bristol Myers Squibb Co | Pharmaceutical compositions containing epothilone derivatives |
| PL207197B1 (pl) | 2001-02-27 | 2010-11-30 | Novartis Ag | Połączenie obejmujące inhibitor przekazywania sygnału i pochodną epotylonową, kompozycja farmaceutyczna zawierająca to połączenie oraz zastosowanie połączenia |
| ATE554756T1 (de) | 2001-03-14 | 2012-05-15 | Bristol Myers Squibb Co | Kombination aus epothilon-analog und chemotherapeutika zur behandlung von proliferativen erkrankungen |
| EP1372650B1 (en) | 2001-03-19 | 2008-11-19 | Novartis AG | Combinations comprising an antidiarrheal agent and an epothilone or an epothilone derivative |
| US6906188B2 (en) | 2001-04-30 | 2005-06-14 | State Of Oregon Acting By And Through The State Board Of Higher Education On Behalf Of Oregon State University | Method for synthesizing epothilones and epothilone analogs |
| US20030023082A1 (en) | 2001-05-15 | 2003-01-30 | Gary Ashley | Epothilone derivatives and methods for making and using the same |
| US6800653B2 (en) | 2001-06-01 | 2004-10-05 | Bristol-Myers Squibb Compnay | Epothilone derivatives |
| DE10138347A1 (de) | 2001-08-03 | 2003-02-27 | Schering Ag | Geschützte 3,5-Dihydroxy-2,2-dimethyl-valeronitrile für die Synthese von Epothilonen- und Derivaten und Verfahren zur Herstellung |
| ES2315399T3 (es) | 2001-08-23 | 2009-04-01 | Novartis Ag | Analogos de epotilona ciclobutilo y ciclopropilo. |
| US20030186334A1 (en) | 2001-09-12 | 2003-10-02 | Temple University - Of The Commonwealth System Of Higher Education | KTS-disintegrins |
| WO2003029195A1 (en) | 2001-09-28 | 2003-04-10 | Sumika Fine Chemicals Co., Ltd. | Intermediates for epothilone derivative and process for producing these |
| US7070964B2 (en) | 2001-11-15 | 2006-07-04 | Kosan Biosciences Incorporated | Epothilone compounds and methods for making the same |
| TW200408407A (en) | 2001-11-30 | 2004-06-01 | Dana Farber Cancer Inst Inc | Methods and compositions for modulating the immune system and uses thereof |
| DE10164592A1 (de) | 2001-12-21 | 2003-07-03 | Schering Ag | C1-C6-Epothilon-Fragmente und Verfahren für die Herstellung von C1-C6-Fragmenten von Epothilonen und deren Derivaten |
| TW200303202A (en) | 2002-02-15 | 2003-09-01 | Bristol Myers Squibb Co | Method of preparation of 21-amino epothilone derivatives |
| US6900331B2 (en) | 2002-03-01 | 2005-05-31 | University Of Notre Dame | Derivatives of epothilone B and D and synthesis thereof |
| AU2003218110A1 (en) | 2002-03-12 | 2003-09-29 | Bristol-Myers Squibb Company | C3-cyano epothilone derivatives |
| US7211593B2 (en) | 2002-03-12 | 2007-05-01 | Bristol-Myers Squibb Co. | C12-cyano epothilone derivatives |
| CN1649585A (zh) | 2002-05-01 | 2005-08-03 | 诺瓦提斯公司 | 用于治疗肝脏肿瘤和其它癌症疾病的埃坡霉素衍生物 |
| TW200400191A (en) | 2002-05-15 | 2004-01-01 | Bristol Myers Squibb Co | Pharmaceutical compositions and methods of using C-21 modified epothilone derivatives |
| AU2003296878A1 (en) | 2002-05-20 | 2004-12-13 | Kosan Biosciences, Inc. | Methods to administer epothilone d |
| US7799561B2 (en) | 2002-06-12 | 2010-09-21 | Sigma-Aldrich, Co. | Affinity peptides and method for purification of recombinant proteins |
| WO2003105828A1 (en) | 2002-06-14 | 2003-12-24 | Bristol-Myers Squibb Company | Combination of epothilone analogs and chemotherapeutic agents for the treatment of proliferative diseases |
| ES2297189T3 (es) | 2002-08-02 | 2008-05-01 | Novartis Ag | Derivados de epotilona. |
| US7053201B2 (en) | 2002-08-30 | 2006-05-30 | National Defense Medical Center | Nucleic acid molecules and polypeptides related to h-ADAM7 |
| HRP20050278A2 (en) | 2002-09-23 | 2005-10-31 | Bristol-Myers Squibb Company | Methods for the preparation, isolation and purification of epothilone b, and x-ray crystal structures of epothilone b |
| GB0230024D0 (en) | 2002-12-23 | 2003-01-29 | Novartis Ag | Organic compounds |
| JP2004217535A (ja) | 2003-01-10 | 2004-08-05 | Nec Soft Ltd | 蛋白質ｔｒｉｍｅｓｔａｔｉｎの結晶化、構造座標の決定、構造座標の使用 |
| US7763430B2 (en) * | 2003-04-22 | 2010-07-27 | Baxter International Inc. | Diagnostic assay for anti-von Willebrand Factor cleaving protease (ADAMTS13) antibodies |
| AU2004275881A1 (en) | 2003-09-25 | 2005-04-07 | Tapestry Pharmaceuticals, Inc. | 9,10-alpha,alpha-OH-taxane analogs and methods for production thereof |
| AU2005316217A1 (en) | 2004-12-17 | 2006-06-22 | Memorial Sloan Kettering Cancer Center | Regulation of metalloprotease cleavage of cell surface proteins |
| EP2634252B1 (en) | 2005-02-11 | 2018-12-19 | University of Southern California | Method of expressing proteins with disulfide bridges |
| US9265933B2 (en) | 2005-09-08 | 2016-02-23 | Massachusetts Eye And Ear Infirmary | Cochlear implants containing biological cells and uses thereof |
| US8008256B2 (en) * | 2006-05-01 | 2011-08-30 | University Of Southern California | Combination therapy for treatment of cancer |
| US8852290B2 (en) | 2007-03-02 | 2014-10-07 | Doheny Eye Institute | Biocompatible implants and methods of making and attaching the same |
| US8802394B2 (en) | 2008-11-13 | 2014-08-12 | Radu O. Minea | Method of expressing proteins with disulfide bridges with enhanced yields and activity |
| WO2010093468A1 (en) | 2009-02-12 | 2010-08-19 | University Of Southern California | Bioadhesive patch for sutureless closure of soft tissue |
| CA2789679A1 (en) | 2010-02-11 | 2011-08-18 | University Of Southern California | Modified adam disintegrin domain polypeptides and uses thereof |
-
2006
- 2006-02-09 EP EP13157149.9A patent/EP2634252B1/en not_active Expired - Lifetime
- 2006-02-09 EP EP06849695A patent/EP1856255A4/en not_active Withdrawn
- 2006-02-09 CN CNA2006800117606A patent/CN101535492A/zh active Pending
- 2006-02-09 AU AU2006336468A patent/AU2006336468B2/en not_active Ceased
- 2006-02-09 JP JP2007556197A patent/JP2008536479A/ja active Pending
- 2006-02-09 CA CA002597647A patent/CA2597647A1/en not_active Abandoned
- 2006-02-09 WO PCT/US2006/004413 patent/WO2007086879A2/en not_active Ceased
- 2006-02-09 US US11/351,311 patent/US7754850B2/en not_active Expired - Fee Related
-
2010
- 2010-07-06 US US12/831,226 patent/US8110542B2/en not_active Expired - Fee Related
-
2012
- 2012-02-06 US US13/367,267 patent/US8338365B2/en not_active Expired - Fee Related
- 2012-11-20 US US13/682,470 patent/US8685668B2/en not_active Expired - Fee Related
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2002528058A (ja) * | 1998-09-29 | 2002-09-03 | ザ・ユニバーシティー・オブ・サザン・カリフォルニア | コントートロスタチン（ｃｎ）、並びに転移及び他の症状の抑制におけるその使用方法 |
| JP2000245467A (ja) * | 1999-02-26 | 2000-09-12 | Agency Of Ind Science & Technol | Ｓｐａｒｃ融合タンパク質およびその製造方法 |
| JP2004500357A (ja) * | 1999-12-10 | 2004-01-08 | ザ・ユニバーシティー・オブ・サザン・カリフォルニア | コントートロスタチン（ｃｎ）並びに転移及びその他の症状の予防におけるその使用法 |
Non-Patent Citations (8)
| Title |
|---|
| JPN6011063282; Ｊ．Ｂｉｏｌ．Ｃｈｅｍ．，Ｖｏｌ．２７４，Ｎｏ．５３（１９９９）ｐ．３７８０９-３７８１４ * |
| JPN6011063283; Ａｒｃｈ．Ｂｉｏｃｈｅｍ．Ｂｉｏｐｈｙｓ．，Ｖｏｌ．３６９，Ｎｏ．２（１９９９）ｐ．２９５-３０１ * |
| JPN6011063284; Ｐａｔｈｏｐｈｙｓｉｏｌ．Ｈａｅｍｏｓｔ．Ｔｈｒｏｍｂ．，Ｖｏｌ．３４，Ｎｏ．４-５（２００５）ｐ．１７７-１８３ * |
| JPN6011063285; Ｊ．Ｂｉｏｌ．Ｃｈｅｍ．，Ｖｏｌ．２７０，Ｎｏ．４３（１９９５）ｐ．２５３２８-２５３３１ * |
| JPN6011063286; Ｐｒｏｔｅｉｎ Ｅｘｐｒ．Ｐｕｒｉｆ．，Ｖｏｌ．３５，Ｎｏ．２（２００４）ｐ．３４４-３５２ * |
| JPN6011063287; Ｍｉｃｒｏｂｉｏｌ．Ｒｅｖ．，Ｖｏｌ．６０，Ｎｏ．３（１９９６）ｐ．５１２-５３８ * |
| JPN6011063288; Ｐｒｏｔｅｉｎ Ｅｘｐｒ．Ｐｕｒｉｆ．，Ｖｏｌ．３８，Ｎｏ．１（２００４）ｐ．５１-６０ * |
| JPN6011063289; Ｊ．Ｇｅｎ．Ｖｉｒｏｌ．，Ｖｏｌ．７３，Ｐｔ．４（１９９２）ｐ．７７５-７８３ * |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2019526253A (ja) * | 2016-08-25 | 2019-09-19 | ネクスゼン バイオテクノロジーズ インコーポレイテッドＮｅｘｇｅｎ Ｂｉｏｔｅｃｈｎｏｌｏｇｉｅｓ， Ｉｎｃ． | 皮膚細胞の増殖効果が増大したサソリ毒融合タンパク質及びそれを有効成分として含有するシワ改善、皮膚弾力の増大及びアンチエイジング化粧料組成物 |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2007086879A3 (en) | 2009-06-11 |
| CA2597647A1 (en) | 2007-08-02 |
| AU2006336468A2 (en) | 2010-04-29 |
| US8338365B2 (en) | 2012-12-25 |
| EP2634252B1 (en) | 2018-12-19 |
| US8685668B2 (en) | 2014-04-01 |
| US20060246541A1 (en) | 2006-11-02 |
| AU2006336468B2 (en) | 2012-04-12 |
| AU2006336468A1 (en) | 2007-08-02 |
| US20120301453A1 (en) | 2012-11-29 |
| EP2634252A2 (en) | 2013-09-04 |
| US7754850B2 (en) | 2010-07-13 |
| CN101535492A (zh) | 2009-09-16 |
| EP2634252A3 (en) | 2013-11-13 |
| US20110097388A1 (en) | 2011-04-28 |
| EP1856255A4 (en) | 2010-01-27 |
| US8110542B2 (en) | 2012-02-07 |
| US20130345399A1 (en) | 2013-12-26 |
| WO2007086879A2 (en) | 2007-08-02 |
| EP1856255A2 (en) | 2007-11-21 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US8338365B2 (en) | Inhibiting integrin receptor binding with non-native monomeric disintegrin or monomeric disintegrin domains | |
| Minea et al. | Development of a novel recombinant disintegrin, contortrostatin, as an effective anti-tumor and anti-angiogenic agent | |
| KR100361049B1 (ko) | 천연적으로 폴딩 및 분비되는 단백질의 제조방법 | |
| Fathi-Roudsari et al. | Auto-induction for high level production of biologically active reteplase in Escherichia coli | |
| US8802394B2 (en) | Method of expressing proteins with disulfide bridges with enhanced yields and activity | |
| Akiyama et al. | Polypeptide binding of Escherichia coli FtsH (HflB) | |
| JP2004513648A (ja) | 原核生物における大量タンパク質生産方法 | |
| EP2363469B1 (en) | Process for preparing inclusion body-forming protein | |
| HK1189033A (en) | Method of expressing proteins with disulfide bridges | |
| HK1189033B (en) | Method of expressing proteins with disulfide bridges | |
| Peisley et al. | High-level expression of a soluble and functional fibronectin type II domain from MMP-2 in the Escherichia coli cytoplasm for solution NMR studies | |
| EP1407030B1 (en) | Methods for large scale production of recombinant dna-derived tpa or k2s molecules | |
| Pourani et al. | Efficient periplasmic expression of active lysyl endopeptidase and optimizing the purification methods | |
| AU2002221815A1 (en) | Methods for large scale production of recombinant DNA-derived tPA or K2S molecules | |
| Yu et al. | Enhanced expression of an antibody-targeted plasminogen activator in Escherichia coli by fusion to decorsin | |
| Zhan | Genetic and biochemical studies of disulfide bond isomerization in Escherichia coli | |
| Dorfman | Purification and characterization of the dimer interaction of the apple 4 domain of human blood coagulation factor XI |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20090209 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20090209 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20110201 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20110203 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20111206 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20120302 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20120309 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20120606 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20130402 |