Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
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Btg1 is Required to Maintain the Pool of Stem and Progenitor Cells of the Dentate Gyrus and Subventricular ZoneAnterior gradient protein-2 is a regulator of cellular adhesion in prostate cancerOrdering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent mannerPresence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cellsAlternatively spliced products CC3 and TC3 have opposing effects on apoptosisThe prodomain of caspase-1 enhances Fas-mediated apoptosis through facilitation of caspase-8 activationTelomeric protein Pin2/TRF1 induces mitotic entry and apoptosis in cells with short telomeres and is down-regulated in human breast tumorsInvolvement of alpha-PAK-interacting exchange factor in the PAK1-c-Jun NH(2)-terminal kinase 1 activation and apoptosis induced by benzo[a]pyreneProstate-derived sterile 20-like kinase 2 (PSK2) regulates apoptotic morphology via C-Jun N-terminal kinase and Rho kinase-1Mdm4 (Mdmx) regulates p53-induced growth arrest and neuronal cell death during early embryonic mouse development.Dectin-1 is an extracellular pathogen sensor for the induction and processing of IL-1β via a noncanonical caspase-8 inflammasomeTranscriptomic and proteomic approach to studying SNX-2112-induced K562 cells apoptosis and anti-leukemia activity in K562-NOD/SCID miceCIDE, a novel family of cell death activators with homology to the 45 kDa subunit of the DNA fragmentation factorIn vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domainsThe 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosisDJ-1 inhibits TRAIL-induced apoptosis by blocking pro-caspase-8 recruitment to FADDIdentification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell death protein Ced-3 is activated during Fas- and tumor necrosis factor-induced apoptosisp28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulumICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme BGeneration of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis, and caspase-3 cleavageCaspases: the executioners of apoptosisCaspase-1 (interleukin-1beta-converting enzyme) is inhibited by the human serpin analogue proteinase inhibitor 9The large subunit of replication factor C is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during Fas-mediated apoptosisThe c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspasesCaspase-mediated activation and induction of apoptosis by the mammalian Ste20-like kinase Mst1Dominant-interfering forms of MEF2 generated by caspase cleavage contribute to NMDA-induced neuronal apoptosisHsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis.Designed FHIT alleles establish that Fhit-induced apoptosis in cancer cells is limited by substrate bindingCaspase 3 cleavage of the Ste20-related kinase SLK releases and activates an apoptosis-inducing kinase domain and an actin-disassembling regionCleavage of sterol regulatory element binding proteins (SREBPs) by CPP32 during apoptosisp53-dependent ceramide response to genotoxic stressPurification and cDNA cloning of a second apoptosis-related cysteine protease that cleaves and activates sterol regulatory element binding proteinsWhite tea extract induces apoptosis in non-small cell lung cancer cells: the role of peroxisome proliferator-activated receptor-{gamma} and 15-lipoxygenasesNew insights into the mechanisms of green tea catechins in the chemoprevention of prostate cancerCleavage of lamin A by Mch2 alpha but not CPP32: multiple interleukin 1 beta-converting enzyme-related proteases with distinct substrate recognition properties are active in apoptosisModulation of Akt kinase activity by binding to Hsp90The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosisTargeted cell killing by reconstituted caspasesERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis
P2860
Q21129361-E21A330E-77C7-4E7C-A475-BFFDA8DA9A52Q21132306-01EB6A1F-962B-4AD2-B45D-CAE6F768C53DQ22008727-8F36E44A-2ABE-4BB4-A26C-35B647870A58Q22009395-9CFDCD0D-7657-4ADB-AA44-683874280D8AQ22010984-D738B849-BF3C-46E3-8C3B-DD46DCE720C9Q22254032-0A69A01C-5EFE-41B8-B83A-D1C95DE649DEQ24291157-31DCA851-9F7F-4744-9388-1A2A3B6FBF70Q24291712-6544EFC3-0056-41DB-ABF3-01A9DF848B3EQ24300825-C909F3B2-E881-411C-8D5F-F1DD1D99B36BQ24300985-2882C873-1DF2-4191-BA4D-E6712A2F6F11Q24303046-D1B1CEB4-A1A0-4919-BFF8-27EAA38C9B03Q24309051-7D3829A8-3801-4317-9EBE-6DA92B6D904CQ24310562-4481AB17-2000-4C80-858E-71E2AE8D4AA7Q24315787-4C153282-5A6B-4648-A60F-2168B67931A1Q24316760-11EB056C-C677-4170-8E13-19FD7904E513Q24316876-B5B466D2-1D82-4CC1-BAFA-6DE09C6D2644Q24317687-BE1932F8-608C-4044-BABE-9A42273A0189Q24318803-1A108264-8DE0-4DD7-9DEF-B1B42B0A6AC2Q24318875-DFD4BCB4-286A-4A7A-8428-8768C0CC836FQ24321471-61E87571-4541-432D-9826-1B49A849A6E2Q24322944-0D653AA2-5A93-4DCD-BD2F-202FA184016EQ24530218-9994BCAB-4A25-4A7C-96E3-1797646B3C6AQ24531784-C363A493-8815-465C-BF2C-4165D732E98DQ24532811-DB9D95FB-8D07-4DB3-B8EA-F27D21ED26F8Q24532851-1D32F3BE-B23A-499A-AED5-5EE489432CB1Q24533217-1085EAC4-9343-48AD-842D-7E1E9F7E6AB7Q24534050-FF41D2E7-CD30-4012-B2C4-7595FFCE7570Q24534085-A6A188A8-4725-4BC0-B9F2-C262BDD65D80Q24550737-7CC475F2-4EF9-40BC-87F9-394F03F10B05Q24554338-C295F466-8402-44FD-81A6-C89D9A44B5D0Q24563244-90CA42F7-99A7-480C-A86E-A90B4FBE97EFQ24564604-B658125D-D2E3-41F3-BE16-5D0DC335585CQ24604930-4E385912-176A-4926-9193-FAEA576BBD5BQ24618321-B2551F64-0B26-4328-87FD-17C0B2F07C77Q24619151-E121A2A9-41D1-40C7-9B38-FCC582D9C6E3Q24629239-2853D01A-AD6D-49B0-9E5F-9085E24ADF08Q24648565-B17BACD9-152C-4913-B1B9-24A46953E2AAQ24653321-71124EA9-76A4-48E2-A53E-1BD1B263145FQ24671860-348645C1-4DD2-4405-B3B1-5E0F8820BC0CQ24676652-225CB758-FD9B-4AC4-8F33-97271158F9DA
P2860
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
name
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@ast
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@en
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@nl
type
label
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@ast
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@en
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@nl
prefLabel
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@ast
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@en
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@nl
P2093
P3181
P356
P1433
P1476
Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
@en
P2093
D W Nicholson
J P Vaillancourt
N A Thornberry
P R Griffin
Y A Lazebnik
P2888
P3181
P356
10.1038/376037A0
P407
P577
1995-07-06T00:00:00Z
P5875
P6179
1038492988