Activation of caspase-2 in apoptosis - Wikidata - awgldk - TriplyDB

Activation of caspase-2 in apoptosis

Activation of caspase-2 in apoptosis

http://www.wikidata.org/entity/Q28611454

about

Molecular cloning and characterization of DEFCAP-L and -S, two isoforms of a novel member of the mammalian Ced-4 family of apoptosis proteins Characterization of a novel proapoptotic caspase-2- and caspase-9-binding protein Cdk5 activator-binding protein C53 regulates apoptosis induced by genotoxic stress via modulating the G2/M DNA damage checkpoint Evaluation of Nod-like receptor (NLR) effector domain interactions Tumor suppressor protein C53 antagonizes checkpoint kinases to promote cyclin-dependent kinase 1 activation Caspase-mediated cleavage of C53/LZAP protein causes abnormal microtubule bundling and rupture of the nuclear envelope HOXA5-induced apoptosis in breast cancer cells is mediated by caspases 2 and 8 Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis Mitochondrial release of caspase-2 and -9 during the apoptotic process Crystal structure of an invertebrate caspase Caspase-2-induced apoptosis is dependent on caspase-9, but its processing during UV- or tumor necrosis factor-dependent cell death requires caspase-3 Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy Shigella-induced apoptosis is dependent on caspase-1 which binds to IpaB The 72-kDa component of signal recognition particle is cleaved during apoptosis Single-wall carbon nanohorns inhibited activation of microglia induced by lipopolysaccharide through blocking of Sirt3 Single-walled carbon nanohorn (SWNH) aggregates inhibited proliferation of human liver cell lines and promoted apoptosis, especially for hepatoma cell lines Two caspase-2 transcripts are expressed in rat hippocampus after global cerebral ischemia ATM Signaling Pathway Caspase-2 mediated apoptotic and necrotic murine macrophage cell death induced by rough Brucella abortus Caspase 2-mediated tumor suppression involves survivin gene silencing.The baculovirus PE38 protein augments apoptosis induced by transactivator IE1.Human rabaptin-5 is selectively cleaved by caspase-3 during apoptosis.Subcellular localization and CARD-dependent oligomerization of the death adaptor RAIDD.Cyclin D3 activates Caspase 2, connecting cell proliferation with cell death.Tumour necrosis factors receptor associated signalling molecules and their role in activation of apoptosis, JNK and NF-kappaB.Membrane lipidome reorganization correlates with the fate of neuroblastoma cells supplemented with fatty acids.Accelerated degradation of FADD and procaspase 8 in cells expressing human papilloma virus 16 E6 impairs TRAIL-mediated apoptosis.Defects in regulation of apoptosis in caspase-2-deficient mice.Tiam1-regulated osteopontin in senescent fibroblasts contributes to the migration and invasion of associated epithelial cells.Involvement of oxidative stress and caspase 2-mediated intrinsic pathway signaling in age-related increase in muscle cell apoptosis in mice.The PIDDosome mediates delayed death of hippocampal CA1 neurons after transient global cerebral ischemia in rats.MicroRNA-210 induces apoptosis in colorectal cancer via induction of reactive oxygen.SIRT3 regulates cell proliferation and apoptosis related to energy metabolism in non-small cell lung cancer cells through deacetylation of NMNAT2 Death by caspase dimerization.Robo1 modulates proliferation and neurogenesis in the developing neocortex.Cleavage of Mcl-1 by caspases impaired its ability to counteract Bim-induced apoptosis.Involvement of caspase-2 activation in aurora kinase inhibitor-induced cell death in axin-expressing L929 cells.TAp73alpha protects small cell lung carcinoma cells from caspase-2 induced mitochondrial mediated apoptotic cell death.Proteolysis of the human DNA polymerase epsilon catalytic subunit by caspase-3 and calpain specifically during apoptosis.

P2860

Q24290511-C5D08E2C-B6FD-424B-A1F5-17C50DE949E5 Q24291224-21C74429-75B4-4676-8BC7-2F77B38AEBD3 Q24298740-358199E8-2FE8-4695-84E8-C8714D5BBF8D Q24311368-4AF757F9-51D0-4282-B59E-5ACDF7380A03 Q24311887-407B3183-1406-488D-ADB2-6D31B183FAB1 Q24324145-40A9394F-99BE-4C98-9BBD-104D53CDC281 Q24603691-9B85C847-D3F8-4F94-AF61-AAD4D19D6FED Q24669697-0E2A9429-3F94-4DEB-AEE1-6B7745CE21F5 Q24676806-8D46EDA6-F6D6-4A3E-A168-C7650DE2C86D Q27642657-E6D5DA09-3091-46BD-B667-D5DD17CDEAA7 Q28201157-4BEB8532-FE20-4B92-BD81-81D4B7E3D553 Q28217828-F8EB2752-8888-419B-AB32-05A5A1AC111E Q28254596-0AE34F19-BC0A-4468-A77D-77EF56588D1A Q28289989-A9BF6FFA-1DEE-4204-9803-1AEF62498EE2 Q28291832-54DDBA5B-7562-434A-A28E-D8AD0DA175B5 Q28395706-06D5965D-48ED-4C00-B4E3-B6E71A5211F1 Q28395783-8AD2D73D-EF23-4B18-91E9-3803BF0AA3E0 Q28576206-97F6961A-F95F-4507-925D-864E2A189B32 Q30225510-3B737302-3C21-4DF6-9046-14C1F360E006 Q33497936-0EFB98C9-43C7-415A-82FF-475E6A06E756 Q33705936-4882E5C7-0EF7-4B6B-A4E4-A5CF1D5ABCA2 Q33817426-AD869B33-E65D-4963-8F7D-4127C18093F3 Q33884548-0499BE10-0197-4D22-AAA0-3E8BE00DE6E6 Q33893107-A3B23C1C-065E-472D-80E1-90D1B20A77CB Q34067710-6B271BC0-C8DD-462F-8DB4-617CE24A2FDA Q34071248-E72186AE-A87F-45A0-B26A-419849BC4F4F Q34584299-418B641B-9B14-4FBA-BFF7-912615F36AA4 Q35082804-099D2D90-695F-4E8E-AF2A-B0A6E0557D03 Q35198808-E655C17D-AACA-4529-AE4E-063E4D77079C Q35770221-5DDE1AFD-C156-46C9-A3BC-73F4C831D0EF Q36519843-C4702069-F1E1-4E2D-B99F-C8E6B799C41A Q36932474-D3A499DE-F879-4DED-9DE0-0A78B7E8F136 Q36991225-D9C56B95-734E-4894-A0AA-4DB3FE42006E Q37296133-1C7E36EF-1E85-47FF-94EB-BEE12189F7D4 Q37425093-C2632D53-9F12-443B-823C-81E1C380CA7B Q37705521-FF32CC94-C306-42F9-8556-8CFBF4B4888A Q38336443-979AC5E4-B17F-4DBB-B72B-15F94799A75E Q39052359-86B78A72-EAD6-4485-B767-F575A77C6225 Q39421785-4A1559A8-A388-442F-A478-F14838BAAC4D Q39597504-E1FDB827-7DF8-4214-BAE1-ECFF6E324286

P2860

Activation of caspase-2 in apoptosis

http://www.wikidata.org/entity/Q28611454

description

1997 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

artículu científicu espublizáu en 1997

@ast

im August 1997 veröffentlichter wissenschaftlicher Artikel

@de

scientific journal article

@en

vedecký článok (publikovaný 1997/08/22)

@sk

vědecký článek publikovaný v roce 1997

@cs

wetenschappelijk artikel (gepubliceerd op 1997/08/22)

@nl

наукова стаття, опублікована в серпні 1997

@uk

name

Activation of caspase-2 in apoptosis

@ast

Activation of caspase-2 in apoptosis

@en

Activation of caspase-2 in apoptosis

@nl

type

label

Activation of caspase-2 in apoptosis

@ast

Activation of caspase-2 in apoptosis

@en

Activation of caspase-2 in apoptosis

@nl

prefLabel

Activation of caspase-2 in apoptosis

@ast

Activation of caspase-2 in apoptosis

@en

Activation of caspase-2 in apoptosis

@nl

P1433

Q28611454-EFB281E2-7B26-484C-9336-8F5FA3EA500E

P1476

Q28611454-8A254259-6794-403E-BF2F-9804562501AA

P2093

Q28611454-3BFC6579-C819-4DB9-94D7-91D32CAB9BAC

Q28611454-76305E12-F95E-4FE2-8816-615A7C727E8D

Q28611454-8C53D726-6006-410B-AA9F-D1B71872F943

Q28611454-97E10A00-A8F1-4BBD-96F2-BE1B0F50B48D

Q28611454-BF8A77A4-73A7-4061-A27F-84D6E3C7F9FB

Q28611454-C1DFDC8E-1640-471A-A0C2-F7C600B5A4BD

Q28611454-C8FFA654-A58C-4A0D-B73F-F05A31567CEC

Q28611454-CC1BA525-1B57-4683-947A-E38DB5D99528

P2860

Q28611454-0896A7ED-1486-4B6B-AC0D-1B8AFEBF0181

Q28611454-125D7CA0-959E-43AE-B344-B436B6A45F5A

Q28611454-1AA6F6EB-B5C3-45C5-8724-910DF2C8E69D

Q28611454-1BF76F34-2DF7-4833-A15C-247008A8E01A

Q28611454-1C207711-8B9E-447E-8EDA-56D0EADA3F62

Q28611454-258B8978-7F28-49E9-9992-0CF12F5CC143

Q28611454-26900D52-1BF3-4F70-B214-BDAF21CB4A27

Q28611454-2828C080-9392-4FBB-B183-430C1A335F9F

Q28611454-2D7CC326-DFF0-41AC-BD21-803C775CB546

Q28611454-3723037B-B971-485C-8F9E-D264B6FB9C7E

P304

Q28611454-53CF1EA2-225E-47C5-B7A6-09143A8BDF1A

P31

Q28611454-05F5E4F8-0A06-48DE-BE4E-584B0DD7FEEC

P3181

Q28611454-892B1C99-0921-4C8E-A447-63C4601A28EA

P356

Q28611454-EDF78EDE-FC56-436E-9C0B-0E09D81785C3

P407

Q28611454-C6921579-8EEE-412F-B0F2-F930AD0A0A13

P433

Q28611454-5120E376-98A5-4E1E-8701-172601FF4571

P478

Q28611454-DE554350-2369-405A-863D-FA5D53536243

P577

Q28611454-EA890B31-176A-453F-B8B4-AC4022BF3AA2

P5875

Q28611454-1F1C2B3E-9A00-47C1-A8B5-2E6D9726B6C8

P698

Q28611454-5E740F4F-119D-44F8-9893-D8F2EEA7C1A7

P921

Q28611454-3D2F5378-9E06-4FF8-B847-FE458AC5F584

P3181

P356

JBC.272.34.21010

P1433

Journal of Biological Chemistry

P1476

Activation of caspase-2 in apoptosis

@en

P2093

A. Greenberg

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

H. Li

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

H. Zhu

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

J. Yuan

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

L. Bergeron

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

L. Shi

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

M. S. Pasternack

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

V. Cryns

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

P2860

Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c

In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains

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

ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosis

ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B

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

Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death

Molecular cloning of the interleukin-1 beta converting enzyme

Purification of three cytotoxic lymphocyte granule serine proteases that induce apoptosis through distinct substrate and target cell interactions

P304

21010–21017

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

P31

scholarly article

P3181

869852

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

P356

10.1074/JBC.272.34.21010

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

P407

P433

34

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

P478

272

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

P577

1997-08-22T00:00:00Z

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

P5875

13959336

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

P698

9261102

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

P921

apoptotic process