R
R. M. Renny Feldman
Researcher at California Institute of Technology
Publications - 11
Citations - 2744
R. M. Renny Feldman is an academic researcher from California Institute of Technology. The author has contributed to research in topics: Ubiquitin ligase & Ubiquitin-conjugating enzyme. The author has an hindex of 10, co-authored 11 publications receiving 2687 citations.
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Journal ArticleDOI
A Complex of Cdc4p, Skp1p, and Cdc53p/Cullin Catalyzes Ubiquitination of the Phosphorylated CDK Inhibitor Sic1p
TL;DR: It is shown that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCFCdc4 p, which is sufficient to reconstitute ubiquitination of Cdk-phosphorylated Sic1p.
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Proteasomal Proteomics: Identification of Nucleotide-sensitive Proteasome-interacting Proteins by Mass Spectrometric Analysis of Affinity-purified Proteasomes
Rati Verma,Stephen Chen,R. M. Renny Feldman,David Schieltz,John R. Yates,Juergen Dohmen,Raymond J. Deshaies,Raymond J. Deshaies +7 more
TL;DR: It is demonstrated that nucleotide hydrolysis modulates the association of many proteins with the 26S proteasome, and DALPC is validated as a powerful tool for rapidly identifying stoichiometric and substoichiometric components of large protein assemblies.
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Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34.
Jae Hong Seol,R. M. Renny Feldman,Wolfgang Zachariae,Andrej Shevchenko,Craig C. Correll,Svetlana Lyapina,Y. Chi,Marta Galova,Jonathan A. Claypool,Suzanne Sandmeyer,Kim Nasmyth,Raymond J. Deshaies +11 more
TL;DR: It is concluded that Cdc53/Hrt1 comprise a highly conserved module that serves as the functional core of a broad variety of heteromeric ubiquitin ligases.
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Hid, Rpr and Grim negatively regulate DIAP1 levels through distinct mechanisms
Soon Ji Yoo,Jun R. Huh,Israel Muro,Hong Yu,Lijuan Wang,Susan L. Wang,R. M. Renny Feldman,Rollie J. Clem,H.-Arno J. Müller,Bruce A. Hay +9 more
TL;DR: In this article, it was shown that Head involution defective (Hid), Reaper (Rpr) and Grim downregulate Drosophila melanogaster IAP1 (DIAP) protein levels.
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SIC1 is ubiquitinated in vitro by a pathway that requires CDC4, CDC34, and cyclin/CDK activities.
TL;DR: Reconstituted SIC1 multiubiquitination in DEAE-fractionated yeast extract indicates that the N-terminal 160 residues are both necessary and sufficient to serve as substrate for CDC34-dependent ubiquitination.