Search Results - "Trievel, R C"
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Purification, Biochemical Analysis, and Structure Determination of JmjC Lysine Demethylases
Published in Methods in enzymology (2016)“…Jumonji C (JmjC) lysine demethylases (KDMs) catalyze the site- and state-specific demethylation of lysine residues in histone and nonhistone protein…”
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Substrate Specificity Profiling of Histone-Modifying Enzymes by Peptide Microarray
Published in Methods in enzymology (2016)“…The dynamic addition and removal of covalent posttranslational modifications (PTMs) on histone proteins serves as a major mechanism regulating…”
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3
A coupled fluorescent assay for histone methyltransferases
Published in Analytical biochemistry (01-07-2005)“…Histone methyltransferases (HMTs) catalyze the S-adenosylmethionine (AdoMet)-dependent methylation of lysines and arginines in the nucleosomal core histones H3…”
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Phosphorylation of Serine 10 in Histone H3 Is Functionally Linked In Vitro and In Vivo to Gcn5-Mediated Acetylation at Lysine 14
Published in Molecular cell (01-06-2000)“…Multiple covalent modifications exist in the amino-terminal tails of core histones, but whether a relationship exists between them is unknown. We examined the…”
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Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide
Published in Nature (London) (02-09-1999)“…Gene activation is a highly regulated process that requires the coordinated action of proteins to relieve chromatin repression and to promote transcriptional…”
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Structure and function of histone methyltransferases
Published in Critical reviews in eukaryotic gene expression (2004)“…Histones are the major protein constituent of chromatin in the eukaryotic nucleus. These proteins undergo a host of different post-translational modifications,…”
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Catalytic Mechanism and Function of Invariant Glutamic Acid 173 from the Histone Acetyltransferase GCN5 Transcriptional Coactivator
Published in The Journal of biological chemistry (25-06-1999)“…Within chromatin, reversible acetylation of core histones is critical for transcriptional activation of eukaryotic target genes. The recent identification of…”
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Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A
Published in The EMBO journal (01-07-1999)“…The human p300/CBP‐associating factor, PCAF, mediates transcriptional activation through its ability to acetylate nucleosomal histone substrates as well as…”
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p53 Sites Acetylated In Vitro by PCAF and p300 Are Acetylated In Vivo in Response to DNA Damage
Published in Molecular and Cellular Biology (01-02-1999)“…Article Usage Stats Services MCB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Application of a Fluorescent Histone Acetyltransferase Assay to Probe the Substrate Specificity of the Human p300/CBP-Associated Factor
Published in Analytical biochemistry (15-12-2000)“…Histone N-acetyltransferases (HATs) are a group of enzymes which acetylate specific lysine residues in the N-terminal tails of nucleosomal histones to promote…”
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Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator
Published in Proceedings of the National Academy of Sciences - PNAS (03-08-1999)“…The yeast GCN5 (yGCN5) transcriptional co-activator functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Here, we present the…”
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Coexpression of Proteins in Bacteria Using T7-Based Expression Plasmids: Expression of Heteromeric Cell-Cycle and Transcriptional Regulatory Complexes
Published in Protein expression and purification (01-12-2000)“…This report describes the development and application of a dual vector coexpression system for the overproduction of heteromeric cell cycle and transcriptional…”
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13
Role of the Carbonyl Group in Thioester Chain Length Recognition by the Medium Chain Acyl-CoA Dehydrogenase
Published in Biochemistry (Easton) (11-07-1995)“…Medium chain acyl-CoA dehydrogenase from pig kidney catalyzes the oxidation of acyl-CoA thioesters to trans-2-enoyl-CoA derivatives with an optimal chain…”
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Human SFMBT is a transcriptional repressor protein that selectively binds the N-terminal tail of histone H3
Published in FEBS letters (10-07-2007)“…Human SFMBT (hSFMBT) is postulated to be a Polycomb (PcG) protein. Similar to other PcG proteins, we found that hSFMBT displays robust transcriptional…”
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Differential processing and localization of human Nocturnin controls metabolism of mRNA and nicotinamide adenine dinucleotide cofactors
Published in The Journal of biological chemistry (30-10-2020)“…Nocturnin (NOCT) is a eukaryotic enzyme that belongs to a superfamily of exoribonucleases, endonucleases, and phosphatases. In this study, we analyze the…”
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Structural basis for the methylation site specificity of SET7/9
Published in Nature structural & molecular biology (01-02-2006)“…Human SET7/9 is a protein lysine methyltransferase (PKMT) that methylates histone H3, the tumor suppressor p53 and the TBP-associated factor TAF10. To…”
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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
Published in Genes & development (15-06-2005)“…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…”
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Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase
Published in Cell (04-10-2002)“…Protein lysine methylation by SET domain enzymes regulates chromatin structure, gene silencing, transcriptional activation, plant metabolism, and other…”
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The SET-domain protein superfamily: protein lysine methyltransferases
Published in Genome biology (01-01-2005)“…The SET-domain protein methyltransferase superfamily includes all but one of the proteins known to methylate histones on lysine. Histone methylation is…”
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Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
Published in Nature structural biology (01-07-2003)“…SET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet) to specific lysine residues of…”
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