Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination - Wikidata - awgldk - TriplyDB

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

http://www.wikidata.org/entity/Q27675192

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Structure of a RING E3 trapped in action reveals ligation mechanism for the ubiquitin-like protein NEDD8 Drugging the undruggables: exploring the ubiquitin system for drug development Modulation of Protein-Protein Interactions for the Development of Novel Therapeutics Principles of antibody-mediated TNF receptor activation Inhibitor of apoptosis (IAP) proteins-modulators of cell death and inflammation RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination Small-molecule SMAC mimetics as new cancer therapeutics Programmed necrosis in the cross talk of cell death and inflammation Structure of a Glomulin-RBX1-CUL1 Complex: Inhibition of a RING E3 Ligase through Masking of Its E2-Binding Surface Structure of HHARI, a RING-IBR-RING Ubiquitin Ligase: Autoinhibition of an Ariadne-Family E3 and Insights into Ligation Mechanism Structure of the caspase-recruitment domain from a zebrafish guanylate-binding protein Novel Disulfide Bond-Mediated Dimerization of the CARD Domain Was Revealed by the Crystal Structure of CARMA1 CARD Regulation of ubiquitin transfer by XIAP, a dimeric RING E3 ligase Targeting Non-proteolytic Protein Ubiquitination for the Treatment of Diffuse Large B Cell Lymphoma Hemi-methylated DNA regulates DNA methylation inheritance through allosteric activation of H3 ubiquitylation by UHRF1 Changes in PUB22 Ubiquitination Modes Triggered by MITOGEN-ACTIVATED PROTEIN KINASE3 Dampen the Immune Response.Label free fragment screening using surface plasmon resonance as a tool for fragment finding - analyzing parkin, a difficult CNS target High-throughput SAXS for the characterization of biomolecules in solution: a practical approach The ubiquitin-associated domain of cellular inhibitor of apoptosis proteins facilitates ubiquitylation Small-molecule inhibitors of protein-protein interactions: progressing toward the reality.Nuclear factor-κB-inducing kinase (NIK) contains an amino-terminal inhibitor of apoptosis (IAP)-binding motif (IBM) that potentiates NIK degradation by cellular IAP1 (c-IAP1).Cbl-c ubiquitin ligase activity is increased via the interaction of its RING finger domain with a LIM domain of the paxillin homolog, Hic 5.Characterization of Potent SMAC Mimetics that Sensitize Cancer Cells to TNF Family-Induced Apoptosis HAX1 regulates E3 ubiquitin ligase activity of cIAPs by promoting their dimerization Macromolecular juggling by ubiquitylation enzymes.Small-molecule IAP antagonists sensitize cancer cells to TRAIL-induced apoptosis: roles of XIAP and cIAPs.Inhibitor of apoptosis proteins as intracellular signaling intermediates.Role of melanoma inhibitor of apoptosis (ML-IAP) protein, a member of the baculoviral IAP repeat (BIR) domain family, in the regulation of C-RAF kinase and cell migration Using protein motion to read, write, and erase ubiquitin signals.The Roles of MDM2 and MDMX Phosphorylation in Stress Signaling to p53.Targeting inhibitors of apoptosis proteins (IAPs) for new breast cancer therapeutics Caspase-dependent regulation of the ubiquitin-proteasome system through direct substrate targeting.IAP proteins as targets for drug development in oncology Zinc-dependent interaction between JAB1 and pre-S2 mutant large surface antigen of hepatitis B virus and its implications for viral hepatocarcinogenesis.Ceramide targets xIAP and cIAP1 to sensitize metastatic colon and breast cancer cells to apoptosis induction to suppress tumor progression The Inhibitor of Apoptosis (IAPs) in Adaptive Response to Cellular Stress ChIP-seq analysis of histone H3K9 trimethylation in peripheral blood mononuclear cells of membranous nephropathy patients.Disease-causing mutations in the XIAP BIR2 domain impair NOD2-dependent immune signalling.Smac mimetics synergize with immune checkpoint inhibitors to promote tumour immunity against glioblastoma.NAIPs: building an innate immune barrier against bacterial pathogens. NAIPs function as sensors that initiate innate immunity by detection of bacterial proteins in the host cell cytosol.

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P2860

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

http://www.wikidata.org/entity/Q27675192

description

2011 nî lūn-bûn

@nan

2011 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@ast

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@en

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@nl

type

label

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@ast

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@en

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@nl

prefLabel

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@ast

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@en

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@nl

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SCIENCE.1207862

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P1476

Antagonists induce a conformational change in cIAP1 that promotes autoubiquitination

@en

P2093

Allyn J Schoeffler

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

Andreas Lingel

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

Anna V Fedorova

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

Anthony M Giannetti

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

Brigitte Maurer

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

Domagoj Vucic

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

Erin C Dueber

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

Eugene Varfolomeev

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

Heidi J A Wallweber

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

J Michael Elliott

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

P2860

Distinct BIR domains of cIAP1 mediate binding to and ubiquitination of tumor necrosis factor receptor-associated factor 2 and second mitochondrial activator of caspases

IAP antagonists induce autoubiquitination of c-IAPs, NF-kappaB activation, and TNFalpha-dependent apoptosis

IAP antagonists target cIAP1 to induce TNFalpha-dependent apoptosis

The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9

Determination of domain structure of proteins from X-ray solution scattering

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Processing of X-ray diffraction data collected in oscillation mode

Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain

Structural basis of IAP recognition by Smac/DIABLO

Design, synthesis, and biological activity of a potent Smac mimetic that sensitizes cancer cells to apoptosis by antagonizing IAPs

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376-80

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scholarly article

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3575559

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10.1126/SCIENCE.1207862

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6054

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334

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2011-10-21T00:00:00Z

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51737197

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22021857

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