Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells. - Wikidata - awgldk - TriplyDB

Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells.

Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells.

http://www.wikidata.org/entity/Q33886502

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Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis Caspase-mediated cleavage of eukaryotic translation initiation factor subunit 2alpha Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis Mitochondrial release of caspase-2 and -9 during the apoptotic process On the Mechanism of Dimethylarginine Dimethylaminohydrolase Inactivation by 4-Halopyridines Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain Trifunctional chemical probes for the consolidated detection and identification of enzyme activities from complex proteomes Peptides from anchovy sauce induce apoptosis in a human lymphoma cell (U937) through the increase of caspase-3 and -8 activities Ethanol-induced apoptosis in mouse liver: Fas- and cytochrome c-mediated caspase-3 activation pathway Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis Dynamic role of postsynaptic caspase-3 and BIRC4 in zebra finch song-response habituation Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype.Chemical approaches for functionally probing the proteome.The Rela(p65) subunit of NF-kappaB is essential for inhibiting double-stranded RNA-induced cytotoxicity.Selective cleavage of BLM, the bloom syndrome protein, during apoptotic cell death.Proteomics meets microbiology: technical advances in the global mapping of protein expression and function.Synthesis of novel caspase inhibitors for characterization of the active caspase proteome in vitro and in vivo Structural and functional definition of the specificity of a novel caspase-3 inhibitor, Ac-DNLD-CHO.Proteomic profiling of proteases: tools for granzyme degradomics.Activation of p73 and induction of Noxa by DNA damage requires NF-kappa B.The effects of diet induced obesity on breast cancer associated pathways in mice deficient in SFRP1.Selective regulation of apoptosis: the cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway The IRF-3 transcription factor mediates Sendai virus-induced apoptosis Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas.Akt/Protein kinase B inhibits cell death by preventing the release of cytochrome c from mitochondria Combined transcriptome and genome analysis of single micrometastatic cells.Effect of deep hypothermic circulatory arrest followed by low-flow cardiopulmonary bypass on brain metabolism in newborn piglets: comparison of pH-stat and α-stat management Chemical proteomics: terra incognita for novel drug target profiling.Assignment of protein function in the postgenomic era.What is your assay for sister-chromatid cohesion?Proapoptotic activity of Caenorhabditis elegans CED-4 protein in Drosophila: implicated mechanisms for caspase activation.Chemical strategies for functional proteomics.Effector caspases and leukemia Protein analysis on a proteomic scale.Effects of sophorae radix on human gastric and colorectal adenocarcinoma cells: sophorae radix and cancer cells.Chemical strategies for activity-based proteomics.Regulation of caspase-9 activity by differential binding to the apoptosome complex Small Molecule Active Site Directed Tools for Studying Human Caspases

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P2860

Multiple species of CPP32 and Mch2 are the major active caspases present in apoptotic cells.

http://www.wikidata.org/entity/Q33886502

description

1997 nî lūn-bûn

@nan

1997 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի մայիսին հրատարակված գիտական հոդված

@hy

1997年の論文

@ja

1997年論文

@yue

1997年論文

@zh-hant

1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

@wuu

name

Multiple species of CPP32 and ...... es present in apoptotic cells.

@ast

Multiple species of CPP32 and ...... es present in apoptotic cells.

@en

type

label

Multiple species of CPP32 and ...... es present in apoptotic cells.

@ast

Multiple species of CPP32 and ...... es present in apoptotic cells.

@en

prefLabel

Multiple species of CPP32 and ...... es present in apoptotic cells.

@ast

Multiple species of CPP32 and ...... es present in apoptotic cells.

@en

P1433

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P1433

The EMBO Journal

P1476

Multiple species of CPP32 and ...... es present in apoptotic cells.

@en

P2093

H Fearnhead

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

L Faleiro

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

R Kobayashi

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

Y Lazebnik

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

P2860

Mch2, a new member of the apoptotic Ced-3/Ice cysteine protease gene family

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

Cleavage 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 apoptosis

CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme

Apoptosis in the pathogenesis and treatment of disease

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

FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex

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

Human ICE/CED-3 protease nomenclature

Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase

P304

2271-2281

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P31

scholarly article

P356

10.1093/EMBOJ/16.9.2271

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P407

P433

9

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P478

16

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P577

1997-05-01T00:00:00Z

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P5875

14048064

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P698

9171342

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

P921

apoptotic process

P932

1169829

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