Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization.
about
Signalling through the grapevinePrinciples of antibody-mediated TNF receptor activationInhibitor of apoptosis (IAP) proteins-modulators of cell death and inflammationWhen ubiquitin meets NF-κB: a trove for anti-cancer drug developmentBIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimerStructural Insight into Inhibitor of Apoptosis Proteins Recognition by a Potent Divalent Smac-MimeticAntagonists induce a conformational change in cIAP1 that promotes autoubiquitinationEssentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3Regulation of ubiquitin transfer by XIAP, a dimeric RING E3 ligaseThe ubiquitin-associated domain of cellular inhibitor of apoptosis proteins facilitates ubiquitylationCharacterization of Potent SMAC Mimetics that Sensitize Cancer Cells to TNF Family-Induced ApoptosisHAX1 regulates E3 ubiquitin ligase activity of cIAPs by promoting their dimerizationMacromolecular juggling by ubiquitylation enzymes.Small-molecule IAP antagonists sensitize cancer cells to TRAIL-induced apoptosis: roles of XIAP and cIAPs.IAPs limit activation of RIP kinases by TNF receptor 1 during development.USP11-dependent selective cIAP2 deubiquitylation and stabilization determine sensitivity to Smac mimetics.Smac mimetic enables the anticancer action of BCG-stimulated neutrophils through TNF-α but not through TRAIL and FasL.Using protein motion to read, write, and erase ubiquitin signals.Targeting inhibitors of apoptosis proteins (IAPs) for new breast cancer therapeuticsCaspase-dependent regulation of the ubiquitin-proteasome system through direct substrate targeting.IAP proteins as targets for drug development in oncologySmac mimetics induce inflammation and necrotic tumour cell death by modulating macrophage activity.Reactivation of Smac-mediated apoptosis in chronic lymphocytic leukemia cells: mechanistic studies of Smac mimetic.Disease-causing mutations in the XIAP BIR2 domain impair NOD2-dependent immune signalling.IAPs: guardians of RIPK1IAPS and ubiquitylation.The TWEAK-Fn14 system as a potential drug target.Specificity and disease in the ubiquitin systemSUMO chain-induced dimerization activates RNF4.Structural insights into the catalysis and regulation of E3 ubiquitin ligases.Ubiquitination profiling identifies sensitivity factors for IAP antagonist treatment.SAHA overcomes FLIP-mediated inhibition of SMAC mimetic-induced apoptosis in mesotheliomaIAPs and Cell Death.TWEAK and cIAP1 regulate myoblast fusion through the noncanonical NF-κB signaling pathway.Characterization of ML-IAP protein stability and physiological role in vivo.The small molecule that packs a punch: ubiquitin-mediated regulation of RIPK1/FADD/caspase-8 complexes.Bivalent IAP antagonists, but not monovalent IAP antagonists, inhibit TNF-mediated NF-κB signaling by degrading TRAF2-associated cIAP1 in cancer cells.The RING-Finger Ubiquitin Ligase HAF1 Mediates Heading date 1 Degradation during Photoperiodic Flowering in Rice.DNA damage and S phase-dependent E2F1 stabilization requires the cIAP1 E3-ubiquitin ligase and is associated with K63-poly-ubiquitination on lysine 161/164 residues.Internal motions prime cIAP1 for rapid activation.
P2860
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P2860
Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization.
description
2011 nî lūn-bûn
@nan
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
2011年论文
@zh
2011年论文
@zh-cn
name
Smac mimetics activate the E3 ...... ting RING domain dimerization.
@en
type
label
Smac mimetics activate the E3 ...... ting RING domain dimerization.
@en
prefLabel
Smac mimetics activate the E3 ...... ting RING domain dimerization.
@en
P2093
P2860
P50
P356
P1476
Smac mimetics activate the E3 ...... ting RING domain dimerization.
@en
P2093
Bodhi Bettjeman
Mark A McKinlay
Rebecca Feltham
Rhesa Budhidarmo
Sarah Shirley
Srinivas K Chunduru
Stephen M Condon
P2860
P304
17015-17028
P356
10.1074/JBC.M111.222919
P407
P577
2011-03-10T00:00:00Z