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Asymmetric recruitment of cIAPs by TRAF2Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in transStructures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitmentNSP-Cas protein structures reveal a promiscuous interaction module in cell signalingMolecular Mechanism of CCAAT-Enhancer Binding Protein Recruitment by the TRIB1 PseudokinaseSecondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase activityNSP-CAS Protein Complexes: Emerging Signaling Modules in CancerExpedient synthesis of highly potent antagonists of inhibitor of apoptosis proteins (IAPs) with unique selectivity for ML-IAPTumor necrosis factor (TNF) signaling, but not TWEAK (TNF-like weak inducer of apoptosis)-triggered cIAP1 (cellular inhibitor of apoptosis protein 1) degradation, requires cIAP1 RING dimerization and E2 binding.Structural mechanisms in NLR inflammasome signaling.Development and structural analysis of a nanomolar cyclic peptide antagonist for the EphA4 receptorStructure of a HOIP/E2~ubiquitin complex reveals RBR E3 ligase mechanism and regulation.TRAF2 must bind to cellular inhibitors of apoptosis for tumor necrosis factor (tnf) to efficiently activate nf-{kappa}b and to prevent tnf-induced apoptosis.The CARD plays a critical role in ASC foci formation and inflammasome signalling.Noncovalent Ubiquitin Interactions Regulate the Catalytic Activity of Ubiquitin Writers.When Worlds Collide-Mechanisms at the Interface between Phosphorylation and Ubiquitination.Design, synthesis and evaluation of monovalent Smac mimetics that bind to the BIR2 domain of the anti-apoptotic protein XIAP.Structural basis of autoregulatory scaffolding by apoptosis signal-regulating kinase 1.Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization.Activation and specificity of human caspase-10.High resolution structures of the bone morphogenetic protein type II receptor in two crystal forms: implications for ligand binding.Structure-Guided Strategy for the Development of Potent Bivalent ERK Inhibitors.Caspase enzymology and activation mechanisms.The activity of TRAF RING homo- and heterodimers is regulated by zinc finger 1.Live and let die: insights into pseudoenzyme mechanisms from structure.Structural Studies of ERK2 Protein Complexes.Bacterial expression and purification of the ovine type II bone morphogenetic protein receptor ectodomain.A bidentate Polycomb Repressive-Deubiquitinase complex is required for efficient activity on nucleosomesStructure-based mechanism of preferential complex formation by apoptosis signal-regulating kinasesSubstrate binding allosterically relieves autoinhibition of the pseudokinase TRIB1
P50
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P50
description
hulumtues
@sq
onderzoeker
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researcher
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հետազոտող
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name
Peter D. Mace
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Peter D. Mace
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Peter D. Mace
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Peter D. Mace
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Peter D. Mace
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type
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Peter D. Mace
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Peter D. Mace
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Peter D. Mace
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Peter D. Mace
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Peter D. Mace
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prefLabel
Peter D. Mace
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Peter D. Mace
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Peter D. Mace
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Peter D. Mace
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Peter D. Mace
@sl
P106
P1153
15058050600
P21
P31
P496
0000-0003-2175-9537