The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis - Wikidata - wikimedia - TriplyDB

The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

http://www.wikidata.org/entity/Q27732868

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Caspase-3-mediated cleavage of Akt: involvement of non-consensus sites and influence of phosphorylation Generation of anti-apoptotic presenilin-2 polypeptides by alternative transcription, proteolysis, and caspase-3 cleavage Caspases: the executioners of apoptosis 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 The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis.A-kinase-anchoring protein 95 functions as a potential carrier for the nuclear translocation of active caspase 3 through an enzyme-substrate-like association.Caspases: pharmacological manipulation of cell death Caspases are activated in a branched protease cascade and control distinct downstream processes in Fas-induced apoptosis Targeted cell killing by reconstituted caspases A cloning method for caspase substrates that uses the yeast two-hybrid system: cloning of the antiapoptotic gene gelsolin A novel method for evaluation and screening of caspase inhibitory peptides by the amino acid positional fitness score Fanconi anemia complementation group A cells are hypersensitive to chromium(VI)-induced toxicity.Crystal structure of baculovirus P35: role of a novel reactive site loop in apoptotic caspase inhibition Dimer formation drives the activation of the cell death protease caspase 9 Structural basis for the activation of human procaspase-7 Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway Crystal structure of an invertebrate caspase Substrate-Induced Conformational Changes Occur in All Cleaved Forms of Caspase-6 Thermodynamic, enzymatic and structural effects of removing a salt bridge at the base of loop 4 in (pro)caspase-3.In silicoidentification and crystal structure validation of caspase-3 inhibitors without a P1 aspartic acid moiety Molecular insight into the role of the leucine residue on the L2 loop in the catalytic activity of caspases 3 and 7 Structural asymmetry of procaspase-7 bound to a specific inhibitor Structure of recombinant human CPP32 in complex with the tetrapeptide acetyl-Asp-Val-Ala-Asp fluoromethyl ketone Caspases: opening the boxes and interpreting the arrows CASH, a novel caspase homologue with death effector domains Dentatorubral pallidoluysian atrophy (DRPLA) protein is cleaved by caspase-3 during apoptosis Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract Caspase-14 is a novel developmentally regulated protease WD-40 repeat region regulates Apaf-1 self-association and procaspase-9 activation Thioredoxin catalyzes the S-nitrosation of the caspase-3 active site cysteine Fas-associated death domain protein interleukin-1beta-converting enzyme 2 (FLICE2), an ICE/Ced-3 homologue, is proximally involved in CD95- and p55-mediated death signaling Induction of an apoptotic program in cell-free extracts by 2-chloro-2'-deoxyadenosine 5'-triphosphate and cytochrome c Substrate-driven mapping of the degradome by comparison of sequence logos Characterization of a novel isoform of caspase-9 that inhibits apoptosis Confinement of caspase-12 proteolytic activity to autoprocessing A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis Molecular mechanisms of caspase regulation during apoptosis Discovery of an allosteric site in the caspases

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

http://www.wikidata.org/entity/Q27732868

description

1996 nî lūn-bûn

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1996 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի հուլիսին հրատարակված գիտական հոդված

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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name

The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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type

label

The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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prefLabel

The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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Nature structural biology

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The three-dimensional structure of apopain/CPP32, a key mediator of apoptosis

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P2093

D M Rasper

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

D W Nicholson

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

E P Peterson

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

J P Vaillancourt

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

J Rotonda

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

J W Becker

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

K M Fazil

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

M Gallant

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

M Labelle

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

N A Thornberry

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P2860

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

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

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

Crystal structure of the cysteine protease interleukin-1 beta-converting enzyme: a (p20/p10)2 homodimer

Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of the C. elegans cell death gene ced-3

Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE

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619-25

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scholarly article

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10.1038/NSB0796-619

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P433

7

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P478

3

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1996-07-01T00:00:00Z

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14527349

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8673606

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P921

apoptotic process