Characterization of cytoplasmic caspase-2 activation by induced proximity. - Wikidata - awgldk - TriplyDB

Characterization of cytoplasmic caspase-2 activation by induced proximity.

Characterization of cytoplasmic caspase-2 activation by induced proximity.

http://www.wikidata.org/entity/Q30490693

about

Caspase-2-mediated cleavage of Mdm2 creates a p53-induced positive feedback loop Caspase-2 as a tumour suppressor Extracellular Hsp90 (eHsp90) as the actual target in clinical trials: intentionally or unintentionally The PIDDosome, DNA-damage-induced apoptosis and beyond Chaperoning steroidal physiology: lessons from mouse genetic models of Hsp90 and its cochaperones Single-cell imaging of inflammatory caspase dimerization reveals differential recruitment to inflammasomes.The molecular chaperone Hsp90α is required for meiotic progression of spermatocytes beyond pachytene in the mouse Metacaspase Yca1 is required for clearance of insoluble protein aggregates.Caspase-2 is an initiator caspase responsible for pore-forming toxin-mediated apoptosis Approaches for defining the Hsp90-dependent proteome.Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Attenuation of the ELAV1-like protein HuR sensitizes adenocarcinoma cells to the intrinsic apoptotic pathway by increasing the translation of caspase-2L.Caspase-2-mediated cell death is required for deleting aneuploid cells.Caspase 2-mediated tumor suppression involves survivin gene silencing.Putative functions of caspase-2.Ocular neuroprotection by siRNA targeting caspase-2 Activation of caspase-9, but not caspase-2 or caspase-8, is essential for heat-induced apoptosis in Jurkat cells.A novel cell lysis approach reveals that caspase-2 rapidly translocates from the nucleus to the cytoplasm in response to apoptotic stimuli.Caspases: therapeutic targets in neurologic disease.Regulation of PIDD auto-proteolysis and activity by the molecular chaperone Hsp90 Flexible stoichiometry and asymmetry of the PIDDosome core complex by heteronuclear NMR spectroscopy and mass spectrometry.Fatty acid synthase inhibition engages a novel caspase-2 regulatory mechanism to induce ovarian cancer cell death.Inactivation of ceramide transfer protein during pro-apoptotic stress by Golgi disassembly and caspase cleavage.Neuronal caspase 2 activity and function requires RAIDD, but not PIDD Induction of cell death by the novel proteasome inhibitor marizomib in glioblastoma in vitro and in vivo TRIM16 overexpression induces apoptosis through activation of caspase-2 in cancer cells.Mechanisms of neuroprotection from hypoxia-ischemia (HI) brain injury by up-regulation of cytoglobin (CYGB) in a neonatal rat model.Rescuing neuronal cell death by RAIDD- and PIDD- derived peptides and its implications for therapeutic intervention in neurodegenerative diseases.The role of caspase-2 in stress-induced apoptosis.Analysis of the minimal specificity of caspase-2 and identification of Ac-VDTTD-AFC as a caspase-2-selective peptide substrate.Caspase-2: the orphan caspase.The tangled circuitry of metabolism and apoptosis.Caspase-2: the reinvented enzyme.Cell death controlling complexes and their potential therapeutic role.Caspase-like proteins: Acanthamoeba castellanii metacaspase and Dictyostelium discoideum paracaspase, what are their functions?Caspase-2 is required for DNA damage-induced expression of the CDK inhibitor p21(WAF1/CIP1)Role of the nucleus in apoptosis: signaling and execution.Hyperthermia: an effective strategy to induce apoptosis in cancer cells.Cell Death Signaling.CHK1 regulates NF-κB signaling upon DNA damage in p53- deficient cells and associated tumor-derived microvesicles.

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P2860

Characterization of cytoplasmic caspase-2 activation by induced proximity.

http://www.wikidata.org/entity/Q30490693

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Characterization of cytoplasmic caspase-2 activation by induced proximity.

@ast

Characterization of cytoplasmic caspase-2 activation by induced proximity.

@en

type

label

Characterization of cytoplasmic caspase-2 activation by induced proximity.

@ast

Characterization of cytoplasmic caspase-2 activation by induced proximity.

@en

prefLabel

Characterization of cytoplasmic caspase-2 activation by induced proximity.

@ast

Characterization of cytoplasmic caspase-2 activation by induced proximity.

@en

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J.MOLCEL.2009.07.023

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P1476

Characterization of cytoplasmic caspase-2 activation by induced proximity

@en

P2093

Andrew Oberst

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

Christopher P Dillon

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

Gavin P McStay

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

Helen M Beere

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

Jonathan M Flanagan

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

Lisa Bouchier-Hayes

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

Samuel Connell

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

P2860

Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner

The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress

The enigma of caspase-2: the laymen's view

Caspase-2 activation in the absence of PIDDosome formation

Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis

DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance

Negative regulation of the Apaf-1 apoptosome by Hsp70

Mechanisms of caspase activation

Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria

RAIDD is a new 'death' adaptor molecule

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830-840

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6

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35

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Douglas R. Green

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2009-09-01T00:00:00Z

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26838879

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19782032

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2755603

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