JP2006515159A5 - - Google Patents
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- JP2006515159A5 JP2006515159A5 JP2004526272A JP2004526272A JP2006515159A5 JP 2006515159 A5 JP2006515159 A5 JP 2006515159A5 JP 2004526272 A JP2004526272 A JP 2004526272A JP 2004526272 A JP2004526272 A JP 2004526272A JP 2006515159 A5 JP2006515159 A5 JP 2006515159A5
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- JP
- Japan
- Prior art keywords
- protein
- complex
- pharmaceutical composition
- shc
- hph2
- 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- Withdrawn
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- 108090000623 proteins and genes Proteins 0.000 claims description 92
- 102000004169 proteins and genes Human genes 0.000 claims description 92
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 31
- 238000000034 method Methods 0.000 claims description 25
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 25
- 101000583616 Homo sapiens Polyhomeotic-like protein 2 Proteins 0.000 claims description 21
- 102100030903 Polyhomeotic-like protein 2 Human genes 0.000 claims description 21
- 229920001184 polypeptide Polymers 0.000 claims description 20
- 230000000694 effects Effects 0.000 claims description 19
- 150000007523 nucleic acids Chemical class 0.000 claims description 14
- 150000001413 amino acids Chemical group 0.000 claims description 13
- 108020004707 nucleic acids Proteins 0.000 claims description 13
- 102000039446 nucleic acids Human genes 0.000 claims description 13
- 230000003993 interaction Effects 0.000 claims description 12
- 206010061218 Inflammation Diseases 0.000 claims description 11
- 102000037865 fusion proteins Human genes 0.000 claims description 11
- 108020001507 fusion proteins Proteins 0.000 claims description 11
- 230000004054 inflammatory process Effects 0.000 claims description 11
- 238000003556 assay Methods 0.000 claims description 8
- 230000015572 biosynthetic process Effects 0.000 claims description 7
- 102000005720 Glutathione transferase Human genes 0.000 claims description 4
- 108010070675 Glutathione transferase Proteins 0.000 claims description 4
- 108091000080 Phosphotransferase Proteins 0.000 claims description 4
- 239000002299 complementary DNA Substances 0.000 claims description 4
- 238000012217 deletion Methods 0.000 claims description 4
- 230000037430 deletion Effects 0.000 claims description 4
- 208000014674 injury Diseases 0.000 claims description 4
- 102000020233 phosphotransferase Human genes 0.000 claims description 4
- 239000012634 fragment Substances 0.000 claims description 3
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- 206010009900 Colitis ulcerative Diseases 0.000 claims description 2
- 208000011231 Crohn disease Diseases 0.000 claims description 2
- 206010014561 Emphysema Diseases 0.000 claims description 2
- 102000004190 Enzymes Human genes 0.000 claims description 2
- 108090000790 Enzymes Proteins 0.000 claims description 2
- KOSRFJWDECSPRO-WDSKDSINSA-N Glu-Glu Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(O)=O KOSRFJWDECSPRO-WDSKDSINSA-N 0.000 claims description 2
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 claims description 2
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 claims description 2
- 208000022559 Inflammatory bowel disease Diseases 0.000 claims description 2
- 208000013616 Respiratory Distress Syndrome Diseases 0.000 claims description 2
- 102000002933 Thioredoxin Human genes 0.000 claims description 2
- 101710120037 Toxin CcdB Proteins 0.000 claims description 2
- 206010053613 Type IV hypersensitivity reaction Diseases 0.000 claims description 2
- 201000006704 Ulcerative Colitis Diseases 0.000 claims description 2
- 208000027418 Wounds and injury Diseases 0.000 claims description 2
- 201000000028 adult respiratory distress syndrome Diseases 0.000 claims description 2
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 claims description 2
- 208000006673 asthma Diseases 0.000 claims description 2
- 230000006378 damage Effects 0.000 claims description 2
- 108010055341 glutamyl-glutamic acid Proteins 0.000 claims description 2
- 229920002704 polyhistidine Polymers 0.000 claims description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 2
- 239000000758 substrate Substances 0.000 claims description 2
- 201000000596 systemic lupus erythematosus Diseases 0.000 claims description 2
- 108060008226 thioredoxin Proteins 0.000 claims description 2
- 229940094937 thioredoxin Drugs 0.000 claims description 2
- 230000008733 trauma Effects 0.000 claims description 2
- 230000006433 tumor necrosis factor production Effects 0.000 claims description 2
- 238000010396 two-hybrid screening Methods 0.000 claims description 2
- 230000005951 type IV hypersensitivity Effects 0.000 claims description 2
- 208000027930 type IV hypersensitivity disease Diseases 0.000 claims description 2
- 150000001875 compounds Chemical class 0.000 claims 30
- 239000008194 pharmaceutical composition Substances 0.000 claims 28
- 229940079593 drug Drugs 0.000 claims 6
- 239000003814 drug Substances 0.000 claims 6
- 150000003384 small molecules Chemical class 0.000 claims 6
- 239000000126 substance Substances 0.000 claims 4
- 230000009918 complex formation Effects 0.000 claims 3
- 239000013043 chemical agent Substances 0.000 claims 2
- 238000001727 in vivo Methods 0.000 claims 2
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- 239000002773 nucleotide Substances 0.000 claims 2
- 125000003729 nucleotide group Chemical group 0.000 claims 2
- 238000006467 substitution reaction Methods 0.000 claims 2
- 238000003160 two-hybrid assay Methods 0.000 claims 2
- 108010085220 Multiprotein Complexes Proteins 0.000 claims 1
- 102000007474 Multiprotein Complexes Human genes 0.000 claims 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims 1
- 229940124599 anti-inflammatory drug Drugs 0.000 claims 1
- 239000003795 chemical substances by application Substances 0.000 claims 1
- 238000001514 detection method Methods 0.000 claims 1
- 239000003937 drug carrier Substances 0.000 claims 1
- 238000007877 drug screening Methods 0.000 claims 1
- 238000000338 in vitro Methods 0.000 claims 1
- 230000004968 inflammatory condition Effects 0.000 claims 1
- 230000002401 inhibitory effect Effects 0.000 claims 1
- 230000005764 inhibitory process Effects 0.000 claims 1
- 108091033319 polynucleotide Proteins 0.000 claims 1
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- 239000002157 polynucleotide Substances 0.000 claims 1
- 239000011541 reaction mixture Substances 0.000 claims 1
- 238000007423 screening assay Methods 0.000 claims 1
- 238000001086 yeast two-hybrid system Methods 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 10
- 108020004414 DNA Proteins 0.000 description 9
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 6
- 210000000056 organ Anatomy 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 102220216937 rs780197027 Human genes 0.000 description 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 108010077850 Nuclear Localization Signals Proteins 0.000 description 3
- 102100040247 Tumor necrosis factor Human genes 0.000 description 3
- 239000013592 cell lysate Substances 0.000 description 3
- OPIFSICVWOWJMJ-YGEXGZRRSA-N 5-bromo-4-chloro-3-indolyl alpha-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-YGEXGZRRSA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 208000035143 Bacterial infection Diseases 0.000 description 2
- 102000014914 Carrier Proteins Human genes 0.000 description 2
- 102100025064 Cellular tumor antigen p53 Human genes 0.000 description 2
- 101000721661 Homo sapiens Cellular tumor antigen p53 Proteins 0.000 description 2
- 102000006835 Lamins Human genes 0.000 description 2
- 108010047294 Lamins Proteins 0.000 description 2
- 108060001084 Luciferase Proteins 0.000 description 2
- 239000005089 Luciferase Substances 0.000 description 2
- 101150010110 Map3k8 gene Proteins 0.000 description 2
- 102100026907 Mitogen-activated protein kinase kinase kinase 8 Human genes 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 208000022362 bacterial infectious disease Diseases 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 230000003197 catalytic effect Effects 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 210000005053 lamin Anatomy 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- YKJYKKNCCRKFSL-RDBSUJKOSA-N (-)-anisomycin Chemical compound C1=CC(OC)=CC=C1C[C@@H]1[C@H](OC(C)=O)[C@@H](O)CN1 YKJYKKNCCRKFSL-RDBSUJKOSA-N 0.000 description 1
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- YKJYKKNCCRKFSL-UHFFFAOYSA-N Anisomycin Natural products C1=CC(OC)=CC=C1CC1C(OC(C)=O)C(O)CN1 YKJYKKNCCRKFSL-UHFFFAOYSA-N 0.000 description 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- 241000186779 Listeria monocytogenes Species 0.000 description 1
- 101100058550 Mus musculus Bmi1 gene Proteins 0.000 description 1
- 108091028043 Nucleic acid sequence Proteins 0.000 description 1
- 108700008625 Reporter Genes 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
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000000749 co-immunoprecipitation Methods 0.000 description 1
- 239000013068 control sample Substances 0.000 description 1
- 230000016396 cytokine production Effects 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 239000012133 immunoprecipitate Substances 0.000 description 1
- 230000000415 inactivating effect Effects 0.000 description 1
- GQPLMRYTRLFLPF-UHFFFAOYSA-N nitrous oxide Inorganic materials [O-][N+]#N GQPLMRYTRLFLPF-UHFFFAOYSA-N 0.000 description 1
- 230000025308 nuclear transport Effects 0.000 description 1
- 102000002574 p38 Mitogen-Activated Protein Kinases Human genes 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000006916 protein interaction Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 238000003260 vortexing Methods 0.000 description 1
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US40004402P | 2002-08-02 | 2002-08-02 | |
| PCT/US2003/023981 WO2004012660A2 (en) | 2002-08-02 | 2003-08-01 | Mk2 interacting proteins |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2006515159A JP2006515159A (ja) | 2006-05-25 |
| JP2006515159A5 true JP2006515159A5 (https=) | 2006-08-31 |
Family
ID=31495774
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2004526272A Withdrawn JP2006515159A (ja) | 2002-08-02 | 2003-08-01 | Ｍｋ２相互作用タンパク質 |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US7364870B2 (https=) |
| EP (1) | EP1572092A4 (https=) |
| JP (1) | JP2006515159A (https=) |
| CN (1) | CN1735687A (https=) |
| AU (1) | AU2003257962A1 (https=) |
| BR (1) | BR0313209A (https=) |
| CA (1) | CA2494577A1 (https=) |
| IL (1) | IL166610A0 (https=) |
| MX (1) | MXPA05001364A (https=) |
| WO (1) | WO2004012660A2 (https=) |
Families Citing this family (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK2617431T3 (en) | 2007-01-10 | 2017-07-10 | Purdue Research Foundation | Polypeptide inhibitors of HSP27 kinase and applications therefor |
| WO2009021137A2 (en) | 2007-08-07 | 2009-02-12 | Purdue Research Foundation | Kinase inhibitors and uses thereof |
| EP2378875B1 (en) * | 2008-12-10 | 2018-05-30 | Purdue Research Foundation | Cell-permeant peptide-based inhibitor of kinases |
| US9890195B2 (en) | 2009-07-27 | 2018-02-13 | Purdue Research Foundation | MK2 inhibitor compositions and methods to enhance neurite outgrowth, neuroprotection, and nerve regeneration |
| EP2790018B1 (en) | 2011-12-05 | 2017-05-03 | Medical and Biological Laboratories Co., Ltd. | Method for detecting protein-protein interaction |
| WO2013134636A1 (en) | 2012-03-09 | 2013-09-12 | Purdue Research Foundation | Compositions and methods for delivery of kinase inhibiting peptides |
| JP5904638B2 (ja) * | 2012-04-11 | 2016-04-13 | 株式会社日本マイクロニクス | 多層配線基板とその製造方法 |
| US11726081B2 (en) | 2019-02-15 | 2023-08-15 | Regents Of The University Of Minnesota | Methods to identify modulators of tau protein structure |
| US11656221B2 (en) * | 2019-06-11 | 2023-05-23 | Regents Of The University Of Minnesota | Methods to identify modulators of actin-binding proteins |
| WO2025215156A1 (en) * | 2024-04-11 | 2025-10-16 | Universitetet I Tromsø - Norges Arktiske Universitet | Biomarker of mk2 activity |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4554101A (en) | 1981-01-09 | 1985-11-19 | New York Blood Center, Inc. | Identification and preparation of epitopes on antigens and allergens on the basis of hydrophilicity |
| US4640835A (en) | 1981-10-30 | 1987-02-03 | Nippon Chemiphar Company, Ltd. | Plasminogen activator derivatives |
| EP0098110B1 (en) | 1982-06-24 | 1989-10-18 | NIHON CHEMICAL RESEARCH KABUSHIKI KAISHA also known as JAPAN CHEMICAL RESEARCH CO., LTD | Long-acting composition |
| US4522811A (en) | 1982-07-08 | 1985-06-11 | Syntex (U.S.A.) Inc. | Serial injection of muramyldipeptides and liposomes enhances the anti-infective activity of muramyldipeptides |
| US4766106A (en) | 1985-06-26 | 1988-08-23 | Cetus Corporation | Solubilization of proteins for pharmaceutical compositions using polymer conjugation |
| AU597574B2 (en) | 1986-03-07 | 1990-06-07 | Massachusetts Institute Of Technology | Method for enhancing glycoprotein stability |
| US4791192A (en) | 1986-06-26 | 1988-12-13 | Takeda Chemical Industries, Ltd. | Chemically modified protein with polyethyleneglycol |
| US5116944A (en) | 1989-12-29 | 1992-05-26 | Neorx Corporation | Conjugates having improved characteristics for in vivo administration |
| US5414135A (en) | 1991-12-30 | 1995-05-09 | Sterling Winthrop Inc. | Vinyl sulfone coupling of polyoxyalkylenes to proteins |
| US5624899A (en) | 1994-07-20 | 1997-04-29 | Genentech Inc. | Method for using Htk ligand |
| US6420338B1 (en) * | 1997-06-13 | 2002-07-16 | New York University Medical Center | Inhibition of the Src kinase family pathway as a method of treating HBV infection and hepatocellular carcinoma |
-
2003
- 2003-08-01 JP JP2004526272A patent/JP2006515159A/ja not_active Withdrawn
- 2003-08-01 US US10/523,014 patent/US7364870B2/en not_active Expired - Fee Related
- 2003-08-01 MX MXPA05001364A patent/MXPA05001364A/es not_active Application Discontinuation
- 2003-08-01 EP EP03767026A patent/EP1572092A4/en not_active Withdrawn
- 2003-08-01 CA CA002494577A patent/CA2494577A1/en not_active Withdrawn
- 2003-08-01 WO PCT/US2003/023981 patent/WO2004012660A2/en not_active Ceased
- 2003-08-01 AU AU2003257962A patent/AU2003257962A1/en not_active Withdrawn
- 2003-08-01 CN CNA038237008A patent/CN1735687A/zh not_active Withdrawn
- 2003-08-01 BR BRPI0313209-9A patent/BR0313209A/pt not_active IP Right Cessation
-
2005
- 2005-01-31 IL IL16661005A patent/IL166610A0/xx unknown
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