Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition - Wikidata - awgldk - TriplyDB

Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition

Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition

http://www.wikidata.org/entity/Q29035696

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Neurodegeneration in Alzheimer's disease: caspases and synaptic element interdependence FAST is a survival protein that senses mitochondrial stress and modulates TIA-1-regulated changes in protein expression The developmentally active and stress-inducible noncoding hsromega gene is a novel regulator of apoptosis in Drosophila Inhibition of Translation and Induction of Apoptosis by Bunyaviral Nonstructural Proteins Bearing Sequence Similarity to Reaper Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination Apoptosis in Cellular Society: Communication between Apoptotic Cells and Their Neighbors The polypeptide chain-releasing factor GSPT1/eRF3 is proteolytically processed into an IAP-binding protein A novel ubiquitin fusion system bypasses the mitochondria and generates biologically active Smac/DIABLO The tumor suppressor WARTS activates the Omi / HtrA2-dependent pathway of cell death Cell death in the nervous system Molecular mechanisms of caspase regulation during apoptosis The role of the RING-finger protein Elfless in Drosophila spermatogenesis and apoptosis Mitochondrial fusion is regulated by Reaper to modulate Drosophila programmed cell death.p42MAPK-mediated phosphorylation of xEIAP/XLX in Xenopus cytostatic factor-arrested egg extracts.echinus, required for interommatidial cell sorting and cell death in the Drosophila pupal retina, encodes a protein with homology to ubiquitin-specific proteases.Functional interactions between the erupted/tsg101 growth suppressor gene and the DaPKC and rbf1 genes in Drosophila imaginal disc tumors The role of ubiquitylation for the control of cell death in Drosophila Monomerization of cytosolic mature smac attenuates interaction with IAPs and potentiation of caspase activation Rho1 regulates apoptosis via activation of the JNK signaling pathway at the plasma membrane.The Drosophila casein kinase Iepsilon/delta Discs overgrown promotes cell survival via activation of DIAP1 expression.Multiple mechanisms modulate distinct cellular susceptibilities toward apoptosis in the developing Drosophila eye.Drosophila IAP1-mediated ubiquitylation controls activation of the initiator caspase DRONC independent of protein degradation.The HIV-1 Vpu protein induces apoptosis in Drosophila via activation of JNK signaling The domains of apoptosis: a genomics perspective.A balance between the diap1 death inhibitor and reaper and hid death inducers controls steroid-triggered cell death in Drosophila Michelob_x is the missing inhibitor of apoptosis protein antagonist in mosquito genomes Drosophila IAP antagonists form multimeric complexes to promote cell death.Physiological apoptosis of polar cells during Drosophila oogenesis is mediated by Hid-dependent regulation of Diap1.Regulation of apoptosis by ubiquitination.Dpp-expressing and non-expressing cells: two different populations of growing cells in Drosophila.Induction of reaper ortholog mx in mosquito midgut cells following baculovirus infection.Role of the deubiquitylating enzyme DmUsp5 in coupling ubiquitin equilibrium to development and apoptosis in Drosophila melanogaster.Regulation of apoptosis proteins in cancer cells by ubiquitin.NOPO modulates Egr-induced JNK-independent cell death in Drosophila.Caspase levels and execution efficiencies determine the apoptotic potential of the cell Pelle Modulates dFoxO-Mediated Cell Death in Drosophila.Key note lecture: toward a mechanistic taxonomy for cell death programs.Caspase activation, inhibition, and reactivation: a mechanistic view.The genetics of cell death: approaches, insights and opportunities in Drosophila.Thiostrepton interacts covalently with Rpt subunits of the 19S proteasome and proteasome substrates.

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P2860

Reaper eliminates IAP proteins through stimulated IAP degradation and generalized translational inhibition

http://www.wikidata.org/entity/Q29035696

description

2002 nî lūn-bûn

@nan

2002 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Reaper eliminates IAP proteins ...... lized translational inhibition

@ast

Reaper eliminates IAP proteins ...... lized translational inhibition

@en

type

label

Reaper eliminates IAP proteins ...... lized translational inhibition

@ast

Reaper eliminates IAP proteins ...... lized translational inhibition

@en

prefLabel

Reaper eliminates IAP proteins ...... lized translational inhibition

@ast

Reaper eliminates IAP proteins ...... lized translational inhibition

@en

P1433

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P1433

Nature Cell Biology

P1476

Reaper eliminates IAP proteins ...... lized translational inhibition

@en

P2093

Daniel A Colón-Ramos

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

Michael R Olson

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

Sally Kornbluth

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

P2860

Structural basis of caspase-7 inhibition by XIAP

Structural basis of caspase inhibition by XIAP: differential roles of the linker versus the BIR domain

Structural basis for the inhibition of caspase-3 by XIAP

A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death

The serine protease Omi/HtrA2 regulates apoptosis by binding XIAP through a reaper-like motif

Structural basis of IAP recognition by Smac/DIABLO

Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides

Ubiquitin protein ligase activity of IAPs and their degradation in proteasomes in response to apoptotic stimuli

Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins

Cyclin is degraded by the ubiquitin pathway

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P304

439-444

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scholarly article

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10.1038/NCB798

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

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6

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

P478

4

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

P50

Christopher L Holley

P577

2002-06-01T00:00:00Z

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11349731

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1021732222

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12021770

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P932

2713440

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