C
Christopher E. Berndsen
Researcher at James Madison University
Publications - 46
Citations - 2264
Christopher E. Berndsen is an academic researcher from James Madison University. The author has contributed to research in topics: Ectodomain & Ubiquitin. The author has an hindex of 17, co-authored 39 publications receiving 1965 citations. Previous affiliations of Christopher E. Berndsen include Johns Hopkins University School of Medicine & University of Wisconsin-Madison.
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Journal ArticleDOI
New insights into ubiquitin E3 ligase mechanism
TL;DR: E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine.
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Histone H3-K56 Acetylation Is Catalyzed by Histone Chaperone-Dependent Complexes
Toshiaki Tsubota,Christopher E. Berndsen,Judith A. Erkmann,Carolyn L. Smith,Lanhao Yang,Michael A. Freitas,John M. Denu,Paul D. Kaufman +7 more
TL;DR: It is shown here that H3-K56 acetylation is catalyzed when Rtt109, a protein that lacks significant homology to known acetyltransferases, forms an active complex with either of two histone binding proteins, Asf1 or Vps75.
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Catalysis and substrate selection by histone/protein lysine acetyltransferases.
TL;DR: The ability of some HATs to utilize longer chain acyl-CoA as alternative substrates suggests a potential direct link between the metabolic state of the cell and transcriptional regulation.
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Structural insights into the assembly and function of the SAGA deubiquitinating module.
Nadine L. Samara,Ajit B. Datta,Christopher E. Berndsen,Xiangbin Zhang,Tingting Yao,Robert E. Cohen,Cynthia Wolberger +6 more
TL;DR: The structure of the SAGA deubiquitinating module (DUBm), a four-protein subcomplex, is reported, revealing an arrangement of protein domains that gives rise to a highly interconnected complex, which is stabilized by eight structural zinc atoms that are critical for enzymatic activity.
Journal ArticleDOI
RNF4-Dependent Hybrid SUMO-Ubiquitin Chains Are Signals for RAP80 and Thereby Mediate the Recruitment of BRCA1 to Sites of DNA Damage
Catherine M. Guzzo,Christopher E. Berndsen,Jianmei Zhu,Vibhor Gupta,Ajit B. Datta,Roger A. Greenberg,Cynthia Wolberger,Michael J. Matunis +7 more
TL;DR: These findings connect ubiquitin- and SUMO-dependent DSB recognition, revealing that RNF4-synthesized hybridsumO-ubiquitin chains are recognized by RAP80 to promote BRCA1 recruitment and DNA repair.