Welcome to the laboratory of Cynthia Wolberger, located in the Department of Biophysics and Biophysical Chemistry. Our research is focused on the structural and mechanistic basis of transcriptional regulation and ubiquitin signaling. We use a combination of x-ray crystallography, cryo-EM, and a variety of biophysical and biochemical approaches to gain insights into the fundamental mechanisms underlying these processes. Please follow the links on this page to learn more about our research and lab members. Prospective graduate students should visit the web sites of the Program in Biochemistry, Cellular and Molecular Biology, the Program in Molecular Biophysics, or the Chemistry-Biology Interface Program.
Student Sara Haile has been awarded a Gilliam Graduate Fellowship for Advanced Study from the Howard Hughes Medical Institute. Congratulations,
More than 100 requests for our plasmid expressing human E1 enzyme.
Sara Haile, a student in the Biochemistry, Cellular and Molecular Biology Program (BCMB) has joined the lab. Welcome, Sara!
Morgan MT, Haj-Yahya M, Ringel AE, Bandi P, Brik A, Wolberger C (2016) Structural basis for histone H2B deubiquitination by the SAGA DUB module. Science 351:725-8.
Ringel AE, Cieniewicz AM, Taverna SD, Wolberger C. (2015) Nucleosome competition reveals processive acetylation by the SAGA HAT module. Proc Nat Acad Sci USA, Proc Natl Acad Sci U S A 112:E5461-70.
Wiener W, DiBello AT, Lombardi PM, Guzzo CM, Zhang X, Matunis MJ, Wolberger C (2013) E2 ubiquitin conjugating enzymes regulate the deubiquitinating activity of OTUB1. Nature Structural and Molecular Biology 20:1033-9
Berndsen CE, Wiener R, Yu IW, Ringel AE, Wolberger C (2013) A conserved asparagine has a structural role in ubiquitin-conjugating enzymes. Nature Chemical Biology 9:154-6.
Wiener R, Zhang X, Wang T, Wolberger C. (2012) The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature 483: 618-22.
Samara NL, Datta AB, Berndsen CE, Zhang X, Yao T, Cohen RE, and Wolberger C (2010) Structural insights into the assembly and function of the SAGA deubiquitinating module. Science 328:1025-1029.