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- Publications
- Influence
p53 Sites Acetylated In Vitro by PCAF and p300 Are Acetylated In Vivo in Response to DNA Damage
- L. Liu, D. M. Scolnick, +4 authors S. Berger
- Biology, Medicine
- Molecular and Cellular Biology
- 1 February 1999
ABSTRACT The p53 tumor suppressor protein is a sequence-specific transcription factor that modulates the response of cells to DNA damage. Recent studies suggest that full transcriptional activity of… Expand
The SET-domain protein superfamily: protein lysine methyltransferases
- S. Dillon, X. Zhang, R. Trievel, X. Cheng
- Biology, Medicine
- Genome Biology
- 2 August 2005
The SET-domain protein methyltransferase superfamily includes all but one of the proteins known to methylate histones on lysine. Histone methylation is important in the regulation of chromatin and… Expand
Phosphorylation of serine 10 in histone H3 is functionally linked in vitro and in vivo to Gcn5-mediated acetylation at lysine 14.
- W. S. Lo, R. Trievel, +5 authors S. Berger
- Biology, Medicine
- Molecular cell
- 1 June 2000
Multiple covalent modifications exist in the amino-terminal tails of core histones, but whether a relationship exists between them is unknown. We examined the relationship between serine 10… Expand
Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide
- J. Rojas, R. Trievel, +5 authors R. Marmorstein
- Chemistry, Medicine
- Nature
- 2 September 1999
Gene activation is a highly regulated process that requires the coordinated action of proteins to relieve chromatin repression and to promote transcriptional activation. Nuclear histone… Expand
Molecular recognition of histone H3 by the WD40 protein WDR5
- Jean-François Couture, E. Collazo, R. Trievel
- Biology, Medicine
- Nature Structural &Molecular Biology
- 9 July 2006
The WD40-repeat protein WDR5 is a conserved subunit of Trithorax (TRX) histone methyltransferase complexes. WDR5 has been reported to selectively bind dimethylated Lys4 (K4me2) in histone H3 to… Expand
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase.
- Jean-François Couture, E. Collazo, J. Brunzelle, R. Trievel
- Biology, Medicine
- Genes & development
- 15 June 2005
SET8 (also known as PR-SET7) is a histone H4-Lys-20-specific methyltransferase that is implicated in cell-cycle-dependent transcriptional silencing and mitotic regulation in metazoans. Herein we… Expand
Catalytic Mechanism and Function of Invariant Glutamic Acid 173 from the Histone Acetyltransferase GCN5 Transcriptional Coactivator*
- Kirk G Tanner, R. Trievel, +5 authors J. Denu
- Biology, Medicine
- The Journal of Biological Chemistry
- 25 June 1999
Within chromatin, reversible acetylation of core histones is critical for transcriptional activation of eukaryotic target genes. The recent identification of intrinsic histone acetyltransferase (HAT)… Expand
Structural basis for the methylation site specificity of SET7/9
- Jean-François Couture, E. Collazo, G. Hauk, R. Trievel
- Biology, Medicine
- Nature Structural &Molecular Biology
- 15 January 2006
Human SET7/9 is a protein lysine methyltransferase (PKMT) that methylates histone H3, the tumor suppressor p53 and the TBP-associated factor TAF10. To elucidate the determinants of its substrate… Expand
Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase
- Jean-François Couture, E. Collazo, Patricia A. Ortiz-Tello, J. Brunzelle, R. Trievel
- Biology, Medicine
- Nature Structural &Molecular Biology
- 1 August 2007
JMJD2A is a JmjC histone demethylase (HDM) that catalyzes the demethylation of di- and trimethylated Lys9 and Lys36 in histone H3 (H3K9me2/3 and H3K36me2/3). Here we present the crystal structures of… Expand
Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase
- R. Trievel, Bridgette M. Beach, L. M. Dirk, R. Houtz, J. Hurley
- Biology, Medicine
- Cell
- 4 October 2002
Protein lysine methylation by SET domain enzymes regulates chromatin structure, gene silencing, transcriptional activation, plant metabolism, and other processes. The 2.6 A resolution structure of… Expand