P
Peter D. Mace
Researcher at University of Otago
Publications - 63
Citations - 2549
Peter D. Mace is an academic researcher from University of Otago. The author has contributed to research in topics: Ubiquitin ligase & Inhibitor of apoptosis. The author has an hindex of 24, co-authored 53 publications receiving 2078 citations. Previous affiliations of Peter D. Mace include Sanford-Burnham Institute for Medical Research & Discovery Institute.
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Journal ArticleDOI
Structure of the MDM2/MDMX RING domain heterodimer reveals dimerization is required for their ubiquitylation in trans
TL;DR: The crystal structure of the MDM2/MDMX RING domain heterodimer and map residues required for functional interaction with the E2 are reported and it is shown that these residues are part of an extended surface that is essential for ubiquitylation in trans.
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TRAF2 Must Bind to Cellular Inhibitors of Apoptosis for Tumor Necrosis Factor (TNF) to Efficiently Activate NF-κB and to Prevent TNF-induced Apoptosis
James E Vince,Delara Pantaki,Rebecca Feltham,Peter D. Mace,Stephanie M. Cordier,Anna C. Schmukle,Angelina J. Davidson,Bernard A. Callus,W. Wei-Lynn Wong,Ian E Gentle,Holly Carter,Erinna F. Lee,Henning Walczak,Catherine L. Day,David L. Vaux,John Silke +15 more
TL;DR: Results show that TRAF2 has anti-apoptotic signaling roles in addition to promoting NF-κB signaling and that efficient activation of NF-σB by TNFR1 requires the recruitment of cIAP1/2 by TRAf2.
Journal ArticleDOI
Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment.
Peter D. Mace,K. Linke,Rebecca Feltham,Frances-Rose Schumacher,Clyde A. Smith,David L. Vaux,John Silke,Catherine L. Day +7 more
TL;DR: It is demonstrated that disruption of E2 binding, or dimerization, stabilizes IAP proteins against IAP antagonists in vivo and shows that autoubiquitylation is required for regulation of IAP abundance.
Journal ArticleDOI
Smac Mimetics Activate the E3 Ligase Activity of cIAP1 Protein by Promoting RING Domain Dimerization
Rebecca Feltham,Bodhi Bettjeman,Rhesa Budhidarmo,Peter D. Mace,Sarah Shirley,Stephen M. Condon,Srinivas K. Chunduru,Mark A. McKinlay,David L. Vaux,John Silke,Catherine L. Day +10 more
TL;DR: It is shown that RING dimerization is essential for the E3 ligase activity of cI AP1 and cIAP2 because monomeric RING mutants could not interact with the ubiquitin-charged E2 enzyme and were resistant to Smac mimetic-induced autoubiquitylation.
Journal ArticleDOI
The CARD plays a critical role in ASC foci formation and inflammasome signalling.
TL;DR: The results of the present study depict a central role of CARDs in the formation of ASC signalling platforms and provide an important tool for investigation of CARD-dependent networks.