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Raymond C. Trievel, Ph.D. - Publications

Affiliations: 
2000 University of Pennsylvania, Philadelphia, PA, United States 
Area:
Biological Chemistry
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48 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2023 Haws SA, Miller LJ, La Luz DR, Kuznetsov VI, Trievel RC, Craciun G, Denu JM. Intrinsic catalytic properties of histone H3 lysine-9 methyltransferases preserve monomethylation levels under low S-adenosylmethionine. The Journal of Biological Chemistry. 104938. PMID 37331600 DOI: 10.1016/j.jbc.2023.104938  0.413
2021 Ginnard SM, Winkler AE, Mellado Fritz C, Bluhm T, Kemmer R, Gilliam M, Butkevich N, Abdrabbo S, Bricker K, Feiler J, Miller I, Zoerman J, El-Mohri Z, Khuansanguan P, Basch M, ... ... Trievel RC, et al. Molecular investigation of the tandem Tudor domain and plant homeodomain histone binding domains of the epigenetic regulator UHRF2. Proteins. PMID 34766381 DOI: 10.1002/prot.26278  0.441
2020 Raiymbek G, An S, Khurana N, Gopinath S, Larkin A, Biswas S, Trievel RC, Cho US, Ragunathan K. An H3K9 methylation dependent protein interaction regulates the non-enzymatic function of a putative histone demethylase. Elife. 9. PMID 32195666 DOI: 10.7554/eLife.53155  0.529
2018 T Abshire E, Chasseur J, Bohn JA, Del Rizzo PA, Freddolino PL, Goldstrohm AC, Trievel RC. The structure of human Nocturnin reveals a conserved ribonuclease domain that represses target transcript translation and abundance in cells. Nucleic Acids Research. PMID 29860338 DOI: 10.1093/Nar/Gky412  0.332
2018 Fick RJ, Clay MC, Vander Lee L, Scheiner S, Al-Hashimi HM, Trievel RC. Water-Mediated Carbon-Oxygen Hydrogen Bonding Facilitates AdoMet Recognition in the Reactivation Domain of Cobalamin-dependent Methionine Synthase. Biochemistry. PMID 29733595 DOI: 10.1021/Acs.Biochem.8B00375  0.305
2017 Moritz LE, Trievel RC. Structure, mechanism, and regulation of polycomb repressive complex 2. The Journal of Biological Chemistry. PMID 28912274 DOI: 10.1074/jbc.R117.800367  0.464
2016 Cornett EM, Dickson BM, Vaughan RM, Krishnan S, Trievel RC, Strahl BD, Rothbart SB. Substrate Specificity Profiling of Histone-Modifying Enzymes by Peptide Microarray Methods in Enzymology. DOI: 10.1016/bs.mie.2016.01.008  0.353
2015 Cheng X, Trievel RC. JmjC lysine demethylases Rsc Metallobiology. 2015: 210-245. DOI: 10.1039/9781782621959-00210  0.452
2014 Del Rizzo PA, Trievel RC. Molecular basis for substrate recognition by lysine methyltransferases and demethylases. Biochimica Et Biophysica Acta. 1839: 1404-15. PMID 24946978 DOI: 10.1016/j.bbagrm.2014.06.008  0.468
2013 Krishnan S, Trievel RC. Structural and functional analysis of JMJD2D reveals molecular basis for site-specific demethylation among JMJD2 demethylases. Structure (London, England : 1993). 21: 98-108. PMID 23219879 DOI: 10.1016/j.str.2012.10.018  0.402
2013 Fick RJ, Trievel RC. An overview of chromatin modifications. Biopolymers. 99: 95-7. PMID 23175384 DOI: 10.1002/bip.22158  0.41
2012 Del Rizzo PA, Krishnan S, Trievel RC. Crystal structure and functional analysis of JMJD5 indicate an alternate specificity and function. Molecular and Cellular Biology. 32: 4044-52. PMID 22851697 DOI: 10.1128/MCB.00513-12  0.574
2012 Krishnan S, Collazo E, Ortiz-Tello PA, Trievel RC. Purification and assay protocols for obtaining highly active Jumonji C demethylases. Analytical Biochemistry. 420: 48-53. PMID 21925481 DOI: 10.1016/j.ab.2011.08.034  0.358
2011 Takahashi YH, Westfield GH, Oleskie AN, Trievel RC, Shilatifard A, Skiniotis G. Structural analysis of the core COMPASS family of histone H3K4 methylases from yeast to human. Proceedings of the National Academy of Sciences of the United States of America. 108: 20526-31. PMID 22158900 DOI: 10.1073/Pnas.1109360108  0.41
2011 Del Rizzo PA, Trievel RC. Substrate and product specificities of SET domain methyltransferases. Epigenetics. 6: 1059-67. PMID 21847010 DOI: 10.4161/epi.6.9.16069  0.454
2011 Krishnan S, Horowitz S, Trievel RC. Structure and function of histone H3 lysine 9 methyltransferases and demethylases. Chembiochem : a European Journal of Chemical Biology. 12: 254-63. PMID 21243713 DOI: 10.1002/Cbic.201000545  0.523
2010 Magnani R, Dirk LM, Trievel RC, Houtz RL. Calmodulin methyltransferase is an evolutionarily conserved enzyme that trimethylates Lys-115 in calmodulin. Nature Communications. 1: 43. PMID 20975703 DOI: 10.1038/ncomms1044  0.325
2010 Del Rizzo PA, Couture JF, Dirk LM, Strunk BS, Roiko MS, Brunzelle JS, Houtz RL, Trievel RC. SET7/9 catalytic mutants reveal the role of active site water molecules in lysine multiple methylation. The Journal of Biological Chemistry. 285: 31849-58. PMID 20675860 DOI: 10.1074/Jbc.M110.114587  0.383
2010 Trievel RC, Del Rizzo P, Couture J, Dirk LM, Strunk B, Roiko M, Brunzelle JS, Houtz RL. Molecular Mechanisms of Lysine Methylation Biophysical Journal. 98: 421a. DOI: 10.1016/J.Bpj.2009.12.2272  0.428
2009 Bulfer SL, Scott EM, Couture JF, Pillus L, Trievel RC. Crystal structure and functional analysis of homocitrate synthase, an essential enzyme in lysine biosynthesis. The Journal of Biological Chemistry. 284: 35769-80. PMID 19776021 DOI: 10.1016/J.Bpj.2009.12.2446  0.397
2009 Trievel RC, Shilatifard A. WDR5, a complexed protein. Nature Structural & Molecular Biology. 16: 678-80. PMID 19578375 DOI: 10.1038/Nsmb0709-678  0.455
2009 Takahashi YH, Lee JS, Swanson SK, Saraf A, Florens L, Washburn MP, Trievel RC, Shilatifard A. Regulation of H3K4 trimethylation via Cps40 (Spp1) of COMPASS is monoubiquitination independent: implication for a Phe/Tyr switch by the catalytic domain of Set1. Molecular and Cellular Biology. 29: 3478-86. PMID 19398585 DOI: 10.1128/Mcb.00013-09  0.4
2009 Raunser S, Magnani R, Huang Z, Houtz RL, Trievel RC, Penczek PA, Walz T. Rubisco in complex with Rubisco large subunit methyltransferase. Proceedings of the National Academy of Sciences of the United States of America. 106: 3160-5. PMID 19208805 DOI: 10.1073/Pnas.0810563106  0.469
2009 Marmorstein R, Trievel RC. Histone modifying enzymes: structures, mechanisms, and specificities. Biochimica Et Biophysica Acta. 1789: 58-68. PMID 18722564 DOI: 10.1016/j.bbagrm.2008.07.009  0.709
2008 Couture JF, Dirk LM, Brunzelle JS, Houtz RL, Trievel RC. Structural origins for the product specificity of SET domain protein methyltransferases. Proceedings of the National Academy of Sciences of the United States of America. 105: 20659-64. PMID 19088188 DOI: 10.1073/pnas.0806712105  0.438
2007 Wu S, Trievel RC, Rice JC. Human SFMBT is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3. Febs Letters. 581: 3289-96. PMID 17599839 DOI: 10.1016/J.Febslet.2007.06.025  0.505
2007 Couture JF, Collazo E, Ortiz-Tello PA, Brunzelle JS, Trievel RC. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nature Structural & Molecular Biology. 14: 689-95. PMID 17589523 DOI: 10.1038/nsmb1273  0.47
2007 Dirk LM, Flynn EM, Dietzel K, Couture JF, Trievel RC, Houtz RL. Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases. Biochemistry. 46: 3905-15. PMID 17338551 DOI: 10.1021/bi6023644  0.321
2006 Dirk LM, Trievel RC, Houtz RL. 7 Non-histone protein lysine methyltransferases: Structure and catalytic roles. The Enzymes. 24: 179-228. PMID 26718041 DOI: 10.1016/S1874-6047(06)80009-0  0.47
2006 Couture JF, Trievel RC. Histone-modifying enzymes: encrypting an enigmatic epigenetic code. Current Opinion in Structural Biology. 16: 753-60. PMID 17070031 DOI: 10.1016/j.sbi.2006.10.002  0.521
2006 Couture JF, Collazo E, Trievel RC. Molecular recognition of histone H3 by the WD40 protein WDR5. Nature Structural & Molecular Biology. 13: 698-703. PMID 16829960 DOI: 10.1038/nsmb1116  0.502
2006 Couture JF, Hauk G, Thompson MJ, Blackburn GM, Trievel RC. Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases. The Journal of Biological Chemistry. 281: 19280-7. PMID 16682405 DOI: 10.1074/Jbc.M602257200  0.317
2006 Couture JF, Collazo E, Hauk G, Trievel RC. Structural basis for the methylation site specificity of SET7/9. Nature Structural & Molecular Biology. 13: 140-6. PMID 16415881 DOI: 10.1038/nsmb1045  0.436
2005 Dillon SC, Zhang X, Trievel RC, Cheng X. The SET-domain protein superfamily: protein lysine methyltransferases. Genome Biology. 6: 227. PMID 16086857 DOI: 10.1186/Gb-2005-6-8-227  0.451
2005 Collazo E, Couture JF, Bulfer S, Trievel RC. A coupled fluorescent assay for histone methyltransferases. Analytical Biochemistry. 342: 86-92. PMID 15958184 DOI: 10.1016/J.Ab.2005.04.007  0.468
2005 Couture JF, Collazo E, Brunzelle JS, Trievel RC. Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase. Genes & Development. 19: 1455-65. PMID 15933070 DOI: 10.1101/gad.1318405  0.439
2004 Trievel RC. Structure and function of histone methyltransferases. Critical Reviews in Eukaryotic Gene Expression. 14: 147-69. PMID 15248813 DOI: 10.1615/CritRevEukaryotGeneExpr.v14.i3.10  0.547
2003 Trievel RC, Flynn EM, Houtz RL, Hurley JH. Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT. Nature Structural Biology. 10: 545-52. PMID 12819771 DOI: 10.1038/Nsb946  0.371
2002 Trievel RC, Beach BM, Dirk LM, Houtz RL, Hurley JH. Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell. 111: 91-103. PMID 12372303 DOI: 10.1016/S0092-8674(02)01000-0  0.448
2000 Trievel RC, Li FY, Marmorstein R. Application of a fluorescent histone acetyltransferase assay to probe the substrate specificity of the human p300/CBP-associated factor. Analytical Biochemistry. 287: 319-28. PMID 11112280 DOI: 10.1006/Abio.2000.4855  0.735
2000 Johnston K, Clements A, Venkataramani RN, Trievel RC, Marmorstein R. Coexpression of proteins in bacteria using T7-based expression plasmids: expression of heteromeric cell-cycle and transcriptional regulatory complexes. Protein Expression and Purification. 20: 435-43. PMID 11087683 DOI: 10.1006/Prep.2000.1313  0.626
2000 Lo WS, Trievel RC, Rojas JR, Duggan L, Hsu JY, Allis CD, Marmorstein R, Berger SL. Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14. Molecular Cell. 5: 917-26. PMID 10911986 DOI: 10.1016/S1097-2765(00)80257-9  0.78
2000 Rojas JR, Yan Y, Trievel RC, Clements A, Zhou J, Barlev N, Lo W, Sterner D, Wang L, Berger SL, Allis CD, Marmorstein R. Structure of the Histone Acetyltransferase Domains of the GCN5, P/CAF and ESA1 Transcriptional Coactivators Biochemical Society Transactions. 28: A106-A106. DOI: 10.1042/Bst028A106  0.774
1999 Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R. Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide. Nature. 401: 93-8. PMID 10485713 DOI: 10.1038/43487  0.785
1999 Trievel RC, Rojas JR, Sterner DE, Venkataramani RN, Wang L, Zhou J, Allis CD, Berger SL, Marmorstein R. Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator. Proceedings of the National Academy of Sciences of the United States of America. 96: 8931-6. PMID 10430873 DOI: 10.1073/Pnas.96.16.8931  0.651
1999 Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R. Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A. The Embo Journal. 18: 3521-32. PMID 10393169 DOI: 10.1093/Emboj/18.13.3521  0.814
1999 Tanner KG, Trievel RC, Kuo MH, Howard RM, Berger SL, Allis CD, Marmorstein R, Denu JM. Catalytic mechanism and function of invariant glutamic acid 173 from the histone acetyltransferase GCN5 transcriptional coactivator. The Journal of Biological Chemistry. 274: 18157-60. PMID 10373413 DOI: 10.1074/jbc.274.26.18157  0.714
1999 Liu L, Scolnick DM, Trievel RC, Zhang HB, Marmorstein R, Halazonetis TD, Berger SL. p53 sites acetylated in vitro by PCAF and p300 are acetylated in vivo in response to DNA damage. Molecular and Cellular Biology. 19: 1202-9. PMID 9891054 DOI: 10.1128/Mcb.19.2.1202  0.598
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