Raymond C. Trievel, Ph.D.
Affiliations: | 2000 | University of Pennsylvania, Philadelphia, PA, United States |
Area:
Biological ChemistryGoogle:
"Raymond Trievel"Mean distance: 9.66 | S | N | B | C | P |
Parents
Sign in to add mentorRonen Marmorstein | grad student | 2000 | Penn | |
(Crystal structure, catalytic mechanism, and substrate specificity of the GCN5 histone acetyltransferase family.) |
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Publications
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Haws SA, Miller LJ, La Luz DR, et al. (2023) Intrinsic catalytic properties of histone H3 lysine-9 methyltransferases preserve monomethylation levels under low S-adenosylmethionine. The Journal of Biological Chemistry. 104938 |
Ginnard SM, Winkler AE, Mellado Fritz C, et al. (2021) Molecular investigation of the tandem Tudor domain and plant homeodomain histone binding domains of the epigenetic regulator UHRF2. Proteins |
Raiymbek G, An S, Khurana N, et al. (2020) An H3K9 methylation dependent protein interaction regulates the non-enzymatic function of a putative histone demethylase. Elife. 9 |
T Abshire E, Chasseur J, Bohn JA, et al. (2018) The structure of human Nocturnin reveals a conserved ribonuclease domain that represses target transcript translation and abundance in cells. Nucleic Acids Research |
Fick RJ, Clay MC, Vander Lee L, et al. (2018) Water-Mediated Carbon-Oxygen Hydrogen Bonding Facilitates AdoMet Recognition in the Reactivation Domain of Cobalamin-dependent Methionine Synthase. Biochemistry |
Moritz LE, Trievel RC. (2017) Structure, mechanism, and regulation of polycomb repressive complex 2. The Journal of Biological Chemistry |
Cornett EM, Dickson BM, Vaughan RM, et al. (2016) Substrate Specificity Profiling of Histone-Modifying Enzymes by Peptide Microarray Methods in Enzymology |
Cheng X, Trievel RC. (2015) JmjC lysine demethylases Rsc Metallobiology. 2015: 210-245 |
Del Rizzo PA, Trievel RC. (2014) Molecular basis for substrate recognition by lysine methyltransferases and demethylases. Biochimica Et Biophysica Acta. 1839: 1404-15 |
Krishnan S, Trievel RC. (2013) Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993). 21: 98-108 |