Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine. - Wikidata - wikimedia - TriplyDB

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

http://www.wikidata.org/entity/Q33996526

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Mathematical modeling identifies inhibitors of apoptosis as mediators of positive feedback and bistability The holo-apoptosome: activation of procaspase-9 and interactions with caspase-3 Regulation of the intrinsic apoptosis pathway by reactive oxygen species Death Domain Assembly Mechanism Revealed by Crystal Structure of the Oligomeric PIDDosome Core Complex The crystal structure of caspase-6, a selective effector of axonal degeneration Structure of the Drosophila Apoptosome at 6.9 Å Resolution A Class of Allosteric Caspase Inhibitors Identified by High-Throughput Screening Changes in Apaf-1 Conformation That Drive Apoptosome Assembly Procaspase-3 activation as an anti-cancer strategy: structure-activity relationship of procaspase-activating compound 1 (PAC-1) and its cellular co-localization with caspase-3 Structure of an apoptosome-procaspase-9 CARD complex.Preparation of the caspase-3/7 substrate Ac-DEVD-pNA by solution-phase peptide synthesis Novel water-soluble polyurethane nanomicelles for cancer chemotherapy: physicochemical characterization and cellular activities.Regulation of the Apaf-1-caspase-9 apoptosome Delivery of a monomeric p53 subdomain with mitochondrial targeting signals from pro-apoptotic Bak or Bax.A systems biology analysis of apoptosome formation and apoptosis execution supports allosteric procaspase-9 activation The apoptosome at high resolution.Apoptosome-independent activation of the lysosomal cell death pathway by caspase-9.Crystal structure of caspase recruiting domain (CARD) of apoptosis repressor with CARD (ARC) and its implication in inhibition of apoptosis.Regulation of caspase-9 activity by differential binding to the apoptosome complex Small-Molecule-Induced and Cooperative Enzyme Assembly on a 14-3-3 Scaffold.Fibrils colocalize caspase-3 with procaspase-3 to foster maturation.Efficacy, long-term toxicity, and mechanistic studies of gold nanorods photothermal therapy of cancer in xenograft mice.The apoptosome: emerging insights and new potential targets for drug design Engineering a BCR-ABL-activated caspase for the selective elimination of leukemic cells Caspase activity mediates the differentiation of embryonic stem cells.A near atomic structure of the active human apoptosome.Molecules that modulate Apaf-1 activity.MALT1 small molecule inhibitors specifically suppress ABC-DLBCL in vitro and in vivo Molecular cell death platforms and assemblies.Apoptosome structure, assembly, and procaspase activation.A dimeric Smac/diablo peptide directly relieves caspase-3 inhibition by XIAP. Dynamic and cooperative regulation of XIAP by Smac/Diablo.Direct induction of apoptosis using an optimal mitochondrially targeted p53.A new model for the transition of APAF-1 from inactive monomer to caspase-activating apoptosome.The Apaf-1 apoptosome induces formation of caspase-9 homo- and heterodimers with distinct activities.A biochemical analysis of the activation of the Drosophila caspase DRONC.The docking interaction of caspase-9 with ERK2 provides a mechanism for the selective inhibitory phosphorylation of caspase-9 at threonine 125.Artepillin C as a targeting survivin molecule in oral squamous cell carcinoma cells in vitro: A preliminary study.Caspase-9 swings both ways in the apoptosome.Protease-Activatable Scaffold Proteins as Versatile Molecular Hubs in Synthetic Signaling Networks

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Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

http://www.wikidata.org/entity/Q33996526

description

2006 nî lūn-bûn

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2006 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2006 թվականի ապրիլին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

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Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

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type

label

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

@ast

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

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prefLabel

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

@ast

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

@en

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J.MOLCEL.2006.03.030

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P1476

Caspase-9 holoenzyme is a specific and optimal procaspase-3 processing machine.

@en

P2093

Hao Wu

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

Hyun Ho Park

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

Jee Y Chung

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

Li S da Graca

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

Qian Yin

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

Su-Chang Lin

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

Xuejun Jiang

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

Yu-Chih Lo

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

P2860

Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors

Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis

Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade

Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

Engineering a dimeric caspase-9: a re-evaluation of the induced proximity model for caspase activation

Improved methods for building protein models in electron density maps and the location of errors in these models

The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity

Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding

Dimer formation drives the activation of the cell death protease caspase 9

Structural basis for the activation of human procaspase-7

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10.1016/J.MOLCEL.2006.03.030

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2

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22

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2006-04-01T00:00:00Z

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7149621

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16630893

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2904439

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