K6 linked polyubiquitylation of FADD by CHIP prevents death inducing signaling complex formation suppressing cell death

Caspase-8 Acts in a Non-enzymatic Role as a Scaffold for Assembly of a Pro-inflammatory “FADDosome” Complex upon TRAIL Stimulation

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CHIP controls necroptosis through ubiquitylation- and lysosome-dependent degradation of RIPK3

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USP8 suppresses death receptor-mediated apoptosis by enhancing FLIPL stability

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Phosphorylation of CHIP at Ser20 by Cdk5 promotes tAIF-mediated neuronal death

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A CHIPotle in physiology and disease

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USP8 regulates mitophagy by removing K6-linked ubiquitin conjugates from parkin

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Ca2+/S100 Proteins Act as Upstream Regulators of the Chaperone-associated Ubiquitin Ligase CHIP (C Terminus of Hsc70-interacting Protein)

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A20 Ubiquitin Ligase–Mediated Polyubiquitination of RIP1 Inhibits Caspase-8 Cleavage and TRAIL-Induced Apoptosis in Glioblastoma

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The BRCA1 ubiquitin ligase and homologous recombination repair

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Ube2w and Ataxin-3 Coordinately Regulate the Ubiquitin Ligase CHIP

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Ubiquitinylation of α-Synuclein by Carboxyl Terminus Hsp70-Interacting Protein (CHIP) Is Regulated by Bcl-2-Associated Athanogene 5 (BAG5)

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The Fas–FADD death domain complex structure reveals the basis of DISC assembly and disease mutations

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S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains

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Cellular IAPs inhibit a cryptic CD95-induced cell death by limiting RIP1 kinase recruitment

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Membrane-Bound Fas Ligand Requires RIP1 for Efficient Activation of Caspase-8 within the Death-Inducing Signaling Complex

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The Fas–FADD death domain complex structure unravels signalling by receptor clustering

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