Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases. - Wikidata - wikimedia - TriplyDB

Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases.

Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases.

http://www.wikidata.org/entity/Q55066927

about

Caspase-1 (interleukin-1beta-converting enzyme) is inhibited by the human serpin analogue proteinase inhibitor 9 Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8 Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome In situ assembly of enzyme inhibitors using extended tethering Autocrine human growth hormone inhibits placental transforming growth factor-beta gene transcription to prevent apoptosis and allow cell cycle progression of human mammary carcinoma cells A single BIR domain of XIAP sufficient for inhibiting caspases ERICE, a novel FLICE-activatable caspase Inactivation of farnesyltransferase and geranylgeranyltransferase I by caspase-3: cleavage of the common alpha subunit during apoptosis Activation of caspase-2 in apoptosis Effects of delayed NSAID administration after experimental eccentric contraction injury – A cellular and proteomics study Characterization of nicotinamidases: steady state kinetic parameters, classwide inhibition by nicotinaldehydes, and catalytic mechanism.Atypical apoptosis in L929 cells induced by evodiamine isolated from Evodia rutaecarpa.Synthesis of novel caspase inhibitors for characterization of the active caspase proteome in vitro and in vivo Anti-viral strategies of cytotoxic T lymphocytes are manifested through a variety of granule-bound pathways of apoptosis induction.Activation of caspases in pig kidney cells infected with wild-type and CrmA/SPI-2 mutants of cowpox and rabbitpox viruses Commitment and effector phases of the physiological cell death pathway elucidated with respect to Bcl-2 caspase, and cyclin-dependent kinase activities.Activation of apoptosis and its inhibition.Pro-B-cell-specific transcription and proapoptotic function of protein kinase Ceta Molecular mechanisms of tamoxifen therapy for cholangiocarcinoma: role of calmodulin.PARP1-driven apoptosis in chronic lymphocytic leukemia.Structure based development of phenylimidazole-derived inhibitors of indoleamine 2,3-dioxygenase.DNA mismatch repair gene MLH1 induces apoptosis in prostate cancer cells.Peptides in apoptosis research.Apoptotic and antiapoptotic activity of L protein of Theiler's murine encephalomyelitis virus.Small Molecule Active Site Directed Tools for Studying Human Caspases A genetic screen for the isolation and characterization of site-specific proteases.Conditional expression of mitogen-activated protein kinase phosphatase-1, MKP-1, is cytoprotective against UV-induced apoptosis.Roles of inflammatory caspases during processing of zebrafish interleukin-1β in Francisella noatunensis infection Nonpathogenic Lactobacillus rhamnosus activates the inflammasome and antiviral responses in human macrophages.HIV-1 directly kills CD4+ T cells by a Fas-independent mechanism.The p42 variant of ETS1 protein rescues defective Fas-induced apoptosis in colon carcinoma cells.Caspases as therapeutic targets.VX-166: a novel potent small molecule caspase inhibitor as a potential therapy for sepsis.AP1 transcription factors are required to maintain the peripheral taste system.PARP-1 cleavage fragments: signatures of cell-death proteases in neurodegeneration Role of poly(ADP-ribose) polymerases in male reproduction.STAT1 is inactivated by a caspase.Structural modeling and functional analysis of the essential ribosomal processing protease Prp from Staphylococcus aureus.Melatonin induces apoptosis through a caspase-dependent but reactive oxygen species-independent mechanism in human leukemia Molt-3 cells.Enhanced heterodimerization of Bax by Bcl-2 mutants improves irradiated cell survival.

P2860

Q24531784-9BD0F9DD-DE9A-4F34-AC95-87CEBB5E7530 Q24532133-C9C891A8-20CC-4BAE-AEA3-6F823332B2D6 Q24655696-62728B18-861E-4E94-B6AC-9D4D262B547B Q27640418-A9FA6F89-FB25-45BD-B79F-1B7E1AE1EDFF Q28216713-27857763-0D54-4379-900F-3C4990665ABC Q28266409-E248F477-CFA9-48F4-BE8F-AD5E13AE9104 Q28273537-17220337-0EF9-43B5-8337-5CF73E7657F5 Q28580707-DBC5DA77-0F2F-4996-803F-E46417073713 Q28611454-A822636A-7091-438A-967B-687280213789 Q29248906-0119367D-7293-4277-8FAD-B44B9D96C860 Q30429278-705CC3AB-955C-4AD8-9787-0B5931A356D0 Q33198727-5BDCB490-F245-4C57-B1E8-5CDBF5CC56BE Q33267135-00FBA0D3-CA14-4FDC-955C-4273ED5AAD03 Q33547796-608D31F9-4DC5-4706-BD29-1ED5778F8826 Q33782567-A0ACA27E-53F1-419A-AC84-CAC243DC8EA0 Q33786573-47224C94-FCA0-4942-BB7A-A12DFEB06ECF Q33833384-AF04BCA6-ACB3-4243-AFA7-16E440CAB547 Q33958951-393B944B-B680-440E-89D8-F6F695774AE7 Q34000409-A2F0F46D-BB77-4B23-8A5E-5924570B5019 Q34064532-512C91F5-AF0C-4E0B-9853-D191D9409A16 Q34802685-66D3BAB0-36AF-4150-A1E4-CA1F6304B53E Q34956579-9FDE655D-67D9-48C1-BD4E-66A02869F1BB Q35008585-4474438D-643A-4149-AB14-BBFCA6885ACC Q35077733-DBF203D5-40D5-43BF-9A88-1C9CD1575FB5 Q35836079-6C690BE0-50F3-4611-81EA-3B2BB627440D Q35972875-93C07923-FEA9-4479-A937-A7C78C2DB2B2 Q35977354-B28FA109-B2C0-4C36-8A22-B994B2B118C1 Q36211076-93D925CA-0201-4AA6-8634-AA050103F060 Q36392069-A4211DA1-06C8-455F-B2C1-4685FF19AF9D Q36400607-83615257-6EB9-4A44-9846-F8D5F8914117 Q36453914-E423525F-B601-4C46-9D42-F25FBBF52EE7 Q37094016-14DF5B75-4F45-4D6C-A505-6DCC38EBD225 Q37443049-DF880D4B-09FE-4D9C-B720-7E21D0557A5B Q37465983-2CFE81EC-B7D1-43E3-B106-15F8C1EDA1DD Q37822920-E4471008-4B48-45D7-BBE6-51EC9B7C17DD Q38124033-4E34CAA3-E956-44DA-9FFA-708CB7F1C926 Q38337795-88706AF0-3931-4AAF-844E-5EA0A575500B Q38967047-C9C3BA3B-71A4-43F7-8DA1-A1BA235033A7 Q39145326-78BCE5A7-38BB-4C70-90EA-467A46743B72 Q39244154-3ECCF357-D9D5-45AC-9D8E-645E1D28A734

P2860

Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases.

http://www.wikidata.org/entity/Q55066927

description

1997 nî lūn-bûn

@nan

1997年の論文

@ja

1997年学术文章

@wuu

1997年学术文章

@zh

1997年学术文章

@zh-cn

1997年学术文章

@zh-hans

1997年学术文章

@zh-my

1997年学术文章

@zh-sg

1997年學術文章

@yue

1997年學術文章

@zh-hant

name

Substrate and inhibitor specif ...... g enzyme and related caspases.

@en

Substrate and inhibitor specif ...... g enzyme and related caspases.

@nl

type

label

Substrate and inhibitor specif ...... g enzyme and related caspases.

@en

Substrate and inhibitor specif ...... g enzyme and related caspases.

@nl

prefLabel

Substrate and inhibitor specif ...... g enzyme and related caspases.

@en

Substrate and inhibitor specif ...... g enzyme and related caspases.

@nl

P1433

Q55066927-CC311E33-9277-4BF8-9F56-31C881AD7312

P1476

Q55066927-7B92FFF8-2F53-4CBC-9AF0-C9DD35B6DF1B

P2093

Q55066927-36113C4D-C2EB-4273-B57A-332AD03B25F7

Q55066927-7A497E9B-FE1B-4ADE-9DE9-045ED001B0AB

Q55066927-953B4119-DE1C-46AF-82B4-498405C73B00

Q55066927-9EF23ADE-8D66-481A-A619-022396C3C69E

Q55066927-AE596D4C-37C6-48D9-8F0C-16160F5657AB

Q55066927-D8580298-9D5B-4CE6-8799-245B4E1A29E2

Q55066927-EE45A342-B1D9-451A-A8AF-45D6EBE74EE6

P2860

Q55066927-0B0562E5-712F-4282-BA5E-BCB4C7B2BFD4

Q55066927-0BB14DE9-845A-4DC0-837B-D5C80F2BDE58

Q55066927-10D56A0C-3333-4143-9B96-19DB3BBD6F77

Q55066927-1DF11AB1-FFC8-4125-960A-04F28895EA25

Q55066927-1F7201C7-2CE9-40DD-9DA6-63417B2A0422

Q55066927-2B27B280-AEC7-4AFB-B672-26FFF6AF45CF

Q55066927-32178AB4-AA07-4C6A-A297-DDFBB8FC4439

Q55066927-3346053F-664D-412F-B69B-F8C2B46E3613

Q55066927-36A53BC2-A643-4953-8111-B3D0721622AC

Q55066927-508AD844-88F7-449D-9AC0-63CD10C9EE78

P304

Q55066927-D1C391C7-9BBE-447D-9E19-BB82FD4DAC73

P31

Q55066927-4EA73875-57A6-4FF8-A06F-018F7F2934DB

P356

Q55066927-FA3071E7-46E2-4CD6-8C20-199F673FE8D2

P407

Q55066927-303D5180-8CBC-492C-A664-AA7A3CAFE92E

P433

Q55066927-47CB8393-FE05-432F-A4F5-E0E3B59C6438

P478

Q55066927-3F237525-917A-4CA0-9322-DD9F682E0CD7

P577

Q55066927-8AE5F4A4-BD96-46AB-B633-64EF10307A12

P5875

Q55066927-C529DBBC-7075-4CEB-833A-3CB8F53357DD

P698

Q55066927-520A745A-2DE1-4011-A851-F22AB8022850

P921

Q55066927-82478ce8-efb9-494d-abc3-ce3419439c58

P356

JBC.272.11.7223

P1433

Journal of Biological Chemistry

P1476

Substrate and inhibitor specif ...... g enzyme and related caspases.

@en

P2093

Chen W

http://www.w3.org/2001/XMLSchema#string

Fox T

http://www.w3.org/2001/XMLSchema#string

Gu Y

http://www.w3.org/2001/XMLSchema#string

Livingston DJ

http://www.w3.org/2001/XMLSchema#string

Margolin N

http://www.w3.org/2001/XMLSchema#string

Raybuck SA

http://www.w3.org/2001/XMLSchema#string

Wilson KP

http://www.w3.org/2001/XMLSchema#string

P2860

Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32

Identification and characterization of ICH-2, a novel member of the interleukin-1 beta-converting enzyme family of cysteine proteases

Molecular cloning and pro-apoptotic activity of ICErelII and ICErelIII, members of the ICE/CED-3 family of cysteine proteases

Molecular cloning of the interleukin-1 beta converting enzyme

Structure and mechanism of interleukin-1 beta converting enzyme

A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes

The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta-converting enzyme

Altered cytokine export and apoptosis in mice deficient in interleukin-1 beta converting enzyme

Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis

Human ICE/CED-3 protease nomenclature

P304

7223-7228

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.272.11.7223

http://www.w3.org/2001/XMLSchema#string

P407

P433

11

http://www.w3.org/2001/XMLSchema#string

P478

272

http://www.w3.org/2001/XMLSchema#string

P577

1997-03-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

14157900

http://www.w3.org/2001/XMLSchema#string

P698

9054418

http://www.w3.org/2001/XMLSchema#string

P921