IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms. - Wikidata - wikimedia - TriplyDB

IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms.

IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms.

http://www.wikidata.org/entity/Q42820922

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Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family Ubiquitin-Mediated Regulation of Cell Death, Inflammation, and Defense of Homeostasis Inhibitor of apoptosis (IAP) proteins-modulators of cell death and inflammation Structural mechanisms of DIAP1 auto-inhibition and DIAP1-mediated inhibition of drICE Primary cross-resistance to BRAFV600E-, MEK1/2- and PI3K/mTOR-specific inhibitors in BRAF-mutant melanoma cells counteracted by dual pathway blockade A fluorescent reporter of caspase activity for live imaging.An unconventional IAP-binding motif revealed by target-assisted iterative screening (TAIS) of the BIR3-cIAP1 domain.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.Analysis of inhibitor of apoptosis protein family expression during mammary gland development.The role of ubiquitylation for the control of cell death in Drosophila The Drosophila effector caspase Dcp-1 regulates mitochondrial dynamics and autophagic flux via SesB The Drosophila casein kinase Iepsilon/delta Discs overgrown promotes cell survival via activation of DIAP1 expression.Host insect inhibitor-of-apoptosis SfIAP functionally replaces baculovirus IAP but is differentially regulated by Its N-terminal leader.Inhibition of the inflammatory cytokine TNF-α increases adenovirus activity in ovarian cancer via modulation of cIAP1/2 expression.Drosophila IAP antagonists form multimeric complexes to promote cell death.The role of IAP antagonist proteins in the core apoptosis pathway of the mosquito disease vector Aedes aegypti.Differential Expression Profile of Chicken Embryo Fibroblast DF-1 Cells Infected with Cell-Adapted Infectious Bursal Disease Virus.The mitochondrial death pathway: a promising therapeutic target in diseases IAPs limit activation of RIP kinases by TNF receptor 1 during development.The Smac mimetic RMT5265.2HCL induces apoptosis in EBV and HTLV-I associated lymphoma cells by inhibiting XIAP and promoting the mitochondrial release of cytochrome C and Smac.Baculovirus caspase inhibitors P49 and P35 block virus-induced apoptosis downstream of effector caspase DrICE activation in Drosophila melanogaster cells Flock house virus induces apoptosis by depletion of Drosophila inhibitor-of-apoptosis protein DIAP1 DIAP2 functions as a mechanism-based regulator of drICE that contributes to the caspase activity threshold in living cells Caspase signalling in the absence of apoptosis drives Jnk-dependent invasion.TWEAK-FN14 signaling induces lysosomal degradation of a cIAP1-TRAF2 complex to sensitize tumor cells to TNFalpha.The effector caspases drICE and dcp-1 have partially overlapping functions in the apoptotic pathway in Drosophila CasExpress reveals widespread and diverse patterns of cell survival of caspase-3 activation during development in vivo.Viral subversion of apoptotic enzymes: escape from death row.Molecularly targeted radiosensitization of human prostate cancer by modulating inhibitor of apoptosis.Inhibitor of apoptosis proteins and apoptosis.Caspase-dependent regulation of the ubiquitin-proteasome system through direct substrate targeting.Genetic characterization of two gain-of-function alleles of the effector caspase DrICE in Drosophila The interaction of DIAP1 with dOmi/HtrA2 regulates cell death in Drosophila.IAP proteins as targets for drug development in oncology X-linked inhibitor of apoptosis deficiency in the TRAMP mouse prostate cancer model Inactivation of effector caspases through nondegradative polyubiquitylation.Inhibitor of apoptosis proteins in eukaryotic evolution and development: a model of thematic conservation Enhanced cytoprotective effects of the inhibitor of apoptosis protein cellular IAP1 through stabilization with TRAF2.Osthole induces lung cancer cell apoptosis through inhibition of inhibitor of apoptosis family proteins

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P2860

IAPs are functionally non-equivalent and regulate effector caspases through distinct mechanisms.

http://www.wikidata.org/entity/Q42820922

description

2004 nî lūn-bûn

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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2004年论文

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2004年论文

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name

IAPs are functionally non-equi ...... s through distinct mechanisms.

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IAPs are functionally non-equi ...... s through distinct mechanisms.

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type

label

IAPs are functionally non-equi ...... s through distinct mechanisms.

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IAPs are functionally non-equi ...... s through distinct mechanisms.

@nl

prefLabel

IAPs are functionally non-equi ...... s through distinct mechanisms.

@en

IAPs are functionally non-equi ...... s through distinct mechanisms.

@nl

P1433

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P356

P1433

Nature Cell Biology

P1476

IAPs are functionally non-equi ...... s through distinct mechanisms.

@en

P2093

Anna Zachariou

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

Mark Ditzel

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

Rebecca Wilson

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

Tencho Tenev

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

P2860

Structural basis of caspase-7 inhibition by XIAP

Structural basis for the inhibition of caspase-3 by XIAP

Mechanism of XIAP-mediated inhibition of caspase-9

Structural basis of IAP recognition by Smac/DIABLO

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

A generic protein purification method for protein complex characterization and proteome exploration

Mechanisms of caspase activation and inhibition during apoptosis.

X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and -7 in distinct modes

A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis

In vivo half-life of a protein is a function of its amino-terminal residue

P2888

P304

70-77

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P31

scholarly article

P356

10.1038/NCB1204

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1

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P478

7

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P577

2004-12-05T00:00:00Z

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P698

15580265

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