Raymond C. Trievel, Ph.D. - Publications

Affiliations: 
2000 University of Pennsylvania, Philadelphia, PA, United States 
Area:
Biological Chemistry

59 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
2018 Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JCA. Reply to 'Misreading chaperone-substrate complexes from random noise'. Nature Structural & Molecular Biology. PMID 30297780 DOI: 10.1038/s41594-018-0145-2  0.36
2016 Horowitz S, Salmon L, Koldewey P, Ahlstrom LS, Martin R, Quan S, Afonine PV, van den Bedem H, Wang L, Xu Q, Trievel RC, Brooks CL, Bardwell JC. Visualizing chaperone-assisted protein folding. Nature Structural & Molecular Biology. PMID 27239796 DOI: 10.1038/nsmb.3237  0.36
2016 Vander Meulen KA, Horowitz S, Trievel RC, Butcher SE. Measuring the Kinetics of Molecular Association by Isothermal Titration Calorimetry. Methods in Enzymology. 567: 181-213. PMID 26794355 DOI: 10.1016/bs.mie.2015.08.012  1
2016 Krishnan S, Trievel RC. Purification, Biochemical Analysis, and Structure Determination of JmjC Lysine Demethylases Methods in Enzymology. DOI: 10.1016/bs.mie.2016.01.023  1
2015 Fick RJ, Kroner GM, Nepal B, Magnani R, Horowitz S, Houtz RL, Scheiner S, Trievel RC. Sulfur - Oxygen Chalcogen Bonding Mediates AdoMet Recognition in the Lysine Methyltransferase SET7/9. Acs Chemical Biology. PMID 26713889 DOI: 10.1021/acschembio.5b00852  1
2015 Cui S, Lim KC, Shi L, Lee M, Jearawiriyapaisarn N, Myers G, Campbell A, Harro D, Iwase S, Trievel RC, Rivers A, DeSimone J, Lavelle D, Saunthararajah Y, Engel JD. The LSD1 inhibitor RN-1 induces fetal hemoglobin synthesis and reduces disease pathology in sickle cell mice. Blood. 126: 386-96. PMID 26031919 DOI: 10.1182/blood-2015-02-626259  1
2015 Cheng X, Trievel RC. JmjC lysine demethylases Rsc Metallobiology. 2015: 210-245. DOI: 10.1039/9781782621959-00210  1
2015 Yesselman JD, Horowitz S, Brooks CL, Trievel RC. Frequent side chain methyl carbon-oxygen hydrogen bonding in proteins revealed by computational and stereochemical analysis of neutron structures Proteins: Structure, Function and Bioinformatics. 83: 403-410. DOI: 10.1002/prot.24724  1
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  1
2014 Horowitz S, Adhikari U, Dirk LM, Del Rizzo PA, Mehl RA, Houtz RL, Al-Hashimi HM, Scheiner S, Trievel RC. Manipulating unconventional CH-based hydrogen bonding in a methyltransferase via noncanonical amino acid mutagenesis. Acs Chemical Biology. 9: 1692-7. PMID 24914947 DOI: 10.1021/cb5001185  1
2013 Horowitz S, Dirk LM, Yesselman JD, Nimtz JS, Adhikari U, Mehl RA, Scheiner S, Houtz RL, Al-Hashimi HM, Trievel RC. Conservation and functional importance of carbon-oxygen hydrogen bonding in AdoMet-dependent methyltransferases. Journal of the American Chemical Society. 135: 15536-48. PMID 24093804 DOI: 10.1021/ja407140k  1
2013 Bulfer SL, Brunzelle JS, Trievel RC. Crystal structure of Saccharomyces cerevisiae Aro8, a putative α-aminoadipate aminotransferase. Protein Science : a Publication of the Protein Society. 22: 1417-24. PMID 23893908 DOI: 10.1002/pro.2315  1
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  1
2013 Fick RJ, Trievel RC. An overview of chromatin modifications. Biopolymers. 99: 95-7. PMID 23175384 DOI: 10.1002/bip.22158  1
2012 Horowitz S, Trievel RC. Carbon-oxygen hydrogen bonding in biological structure and function. The Journal of Biological Chemistry. 287: 41576-82. PMID 23048026 DOI: 10.1074/jbc.R112.418574  1
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  1
2012 Bulfer SL, Hendershot JM, Trievel RC. Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe. Proteins. 80: 661-6. PMID 22105743 DOI: 10.1002/prot.23231  1
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  1
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  1
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  1
2011 Horowitz S, Yesselman JD, Al-Hashimi HM, Trievel RC. Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9. The Journal of Biological Chemistry. 286: 18658-63. PMID 21454678 DOI: 10.1074/jbc.M111.232876  1
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  1
2011 Bulfer SL, McQuade TJ, Larsen MJ, Trievel RC. Application of a high-throughput fluorescent acetyltransferase assay to identify inhibitors of homocitrate synthase. Analytical Biochemistry. 410: 133-40. PMID 21073853 DOI: 10.1016/j.ab.2010.11.004  1
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  1
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  1
2010 Pagans S, Kauder SE, Kaehlcke K, Sakane N, Schroeder S, Dormeyer W, Trievel RC, Verdin E, Schnolzer M, Ott M. The Cellular lysine methyltransferase Set7/9-KMT7 binds HIV-1 TAR RNA, monomethylates the viral transactivator Tat, and enhances HIV transcription. Cell Host & Microbe. 7: 234-44. PMID 20227666 DOI: 10.1016/j.chom.2010.02.005  1
2010 Bulfer SL, Scott EM, Pillus L, Trievel RC. Structural basis for L-lysine feedback inhibition of homocitrate synthase. The Journal of Biological Chemistry. 285: 10446-53. PMID 20089861 DOI: 10.1074/jbc.M109.094383  1
2010 Rimon G, Sidhu RS, Lauver DA, Lee JY, Sharma NP, Yuan C, Frieler RA, Trievel RC, Lucchesi BR, Smith WL. Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1. Proceedings of the National Academy of Sciences of the United States of America. 107: 28-33. PMID 19955429 DOI: 10.1073/pnas.0909765106  1
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: 10.1074/jbc.M109.046821  1
2009 Trievel RC, Shilatifard A. WDR5, a complexed protein. Nature Structural & Molecular Biology. 16: 678-80. PMID 19578375 DOI: 10.1038/nsmb0709-678  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
2002 Hurley JH, Anderson DE, Beach B, Canagarajah B, Ho YS, Jones E, Miller G, Misra S, Pearson M, Saidi L, Suer S, Trievel R, Tsujishita Y. Structural genomics and signaling domains. Trends in Biochemical Sciences. 27: 48-53. PMID 11796224 DOI: 10.1016/S0968-0004(01)02022-9  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
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  1
1997 Lee SL, Alexander RS, Smallwood A, Trievel R, Mersinger L, Weber PC, Kettner C. New inhibitors of thrombin and other trypsin-like proteases: Hydrogen bonding of an aromatic cyano group with a backbone amide of the P1 binding site replaces binding of a basic side chain Biochemistry. 36: 13180-13186. PMID 9341205 DOI: 10.1021/bi970912m  1
1995 Trievel RC, Wang R, Anderson VE, Thorpe C. Role of the carbonyl group in thioester chain length recognition by the medium chain acyl-CoA dehydrogenase. Biochemistry. 34: 8597-605. PMID 7612601  1
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