Structure, mechanism, and regulation of polycomb-repressive complex 2 von Moritz, Lindsay E., Trievel, Raymond C.

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Structural and Functional Analysis of JMJD2D Reveals Molecular Basis for Site-Specific Demethylation among JMJD2 Demethylases von Krishnan, Swathi, Trievel, Raymond C.

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Crystallographic and Computational Characterization of Methyl Tetrel Bonding in S-Adenosylmethionine-Dependent Methyltransferases von Trievel, Raymond C, Scheiner, Steve

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Molecular basis for substrate recognition by lysine methyltransferases and demethylases von Del Rizzo, Paul A., Trievel, Raymond C.

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Carbon-Oxygen Hydrogen Bonding in Biological Structure and Function von Horowitz, Scott, Trievel, Raymond C.

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The LSD1 inhibitor RN-1 induces fetal hemoglobin synthesis and reduces disease pathology in sickle cell mice von Cui, Shuaiying, Lim, Kim-Chew, Shi, Lihong, Lee, Mary, Jearawiriyapaisarn, Natee, Myers, Greggory, Campbell, Andrew, Harro, David, Iwase, Shigeki, Trievel, Raymond C., Rivers, Angela, DeSimone, Joseph, Lavelle, Donald, Saunthararajah, Yogen, Engel, James Douglas

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Crystal Structure and Functional Analysis of JMJD5 Indicate an Alternate Specificity and Function von Del Rizzo, Paul A., Krishnan, Swathi, Trievel, Raymond C.

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Substrate and product specificities of SET domain methyltransferases von Del Rizzo, Paul A., Trievel, Raymond C.

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Structural analysis of the core COMPASS family of histone H3K4 methylases from yeast to human von Takahashi, Yoh-hei, Westfield, Gerwin H, Oleskie, Austin N, Trievel, Raymond C, Shilatifard, Ali, Skiniotis, Georgios

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An H3K9 methylation-dependent protein interaction regulates the non-enzymatic functions of a putative histone demethylase von Raiymbek, Gulzhan, An, Sojin, Khurana, Nidhi, Gopinath, Saarang, Larkin, Ajay, Biswas, Saikat, Trievel, Raymond C, Cho, Uhn-Soo, Ragunathan, Kaushik

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Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase von Ortiz-Tello, Patricia A, Brunzelle, Joseph S, Collazo, Evys, Trievel, Raymond C, Couture, Jean-François

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Molecular recognition of histone H3 by the WD40 protein WDR5 von Trievel, Raymond C, Couture, Jean-François, Collazo, Evys

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Coxibs interfere with the action of aspirin by binding tightly to one monomer of cyclooxygenase-1 von Rimon, Gilad, Sidhu, Ranjinder S, Lauver, D. Adam, Lee, Jullia Y, Sharma, Narayan P, Yuan, Chong, Frieler, Ryan A, Trievel, Raymond C, Lucchesi, Benedict R, Smith, William L

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Molecular investigation of the tandem Tudor domain and plant homeodomain histone binding domains of the epigenetic regulator UHRF2 von Ginnard, Shane M., Winkler, Alyssa E., Mellado Fritz, Carlos, Bluhm, Tatum, Kemmer, Ray, Gilliam, Marisa, Butkevich, Nick, Abdrabbo, Sara, Bricker, Kaitlyn, Feiler, Justin, Miller, Isaak, Zoerman, Jenna, El‐Mohri, Zeineb, Khuansanguan, Panida, Basch, Madyson, Petzold, Timothy, Kostoff, Matthew, Konopka, Sean, Kociba, Brendon, Gillis, Thomas, Heyl, Deborah L., Trievel, Raymond C., Albaugh, Brittany N.

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Structural basis for the methylation site specificity of SET7/9 von Trievel, Raymond C, Couture, Jean-François, Collazo, Evys, Hauk, Glenn

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase von Couture, Jean-François, Collazo, Evys, Brunzelle, Joseph S, Trievel, Raymond C

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Structural origins for the product specificity of SET domain protein methyltransferases von Couture, Jean-François, Dirk, Lynnette M.A, Brunzelle, Joseph S, Houtz, Robert L, Trievel, Raymond C

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The Cellular lysine methyltransferase Set7/9-KMT7 binds HIV-1 TAR RNA, monomethylates the viral transactivator Tat, and enhances HIV transcription von Pagans, Sara, Kauder, Steven E, Kaehlcke, Katrin, Sakane, Naoki, Schroeder, Sebastian, Dormeyer, Wilma, Trievel, Raymond C, Verdin, Eric, Schnolzer, Martina, Ott, Melanie

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The SET-domain protein superfamily: protein lysine methyltransferases von Dillon, Shane C, Zhang, Xing, Trievel, Raymond C, Cheng, Xiaodong

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Measuring the Kinetics of Molecular Association by Isothermal Titration Calorimetry von Vander Meulen, Kirk A, Horowitz, Scott, Trievel, Raymond C, Butcher, Samuel E

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