Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect. - Wikidata - awgldk - TriplyDB

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

http://www.wikidata.org/entity/Q30443981

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Specificity of the chromodomain Y chromosome family of chromodomains for lysine-methylated ARK(S/T) motifs Molecular interplay of the noncoding RNA ANRIL and methylated histone H3 lysine 27 by polycomb CBX7 in transcriptional silencing of INK4a The functional diversity of protein lysine methylation Epigenetic virtues of chromodomains HP1a: a structural chromosomal protein regulating transcription Structural study of a small molecule receptor bound to dimethyllysine in lysozyme Molecular Basis of Histone H3K4me3 Recognition by ING4 The ankyrin repeat domain of Huntingtin interacting protein 14 contains a surface aromatic cage, a potential site for methyl-lysine binding Structural Insights for MPP8 Chromodomain Interaction with Histone H3 Lysine 9: Potential Effect of Phosphorylation on Methyl-Lysine Binding MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a Chromodomains read the arginine code of post-translational targeting Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain Protein–ligand interactions: Probing the energetics of a putative cation–π interaction From supramolecular chemistry to the nucleosome: studies in biomolecular recognition Multimethylation of Rickettsia OmpB catalyzed by lysine methyltransferases How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers Finding Inspiration in the Protein Data Bank to Chemically Antagonize Readers of the Histone Code.Binding of the CHD4 PHD2 finger to histone H3 is modulated by covalent modifications A case study in cross-talk: the histone lysine methyltransferases G9a and GLP.Keeping it in the family: diverse histone recognition by conserved structural folds How substrate specificity is imposed on a histone demethylase--lessons from KDM2A Writing and rewriting the epigenetic code of cancer cells: from engineered proteins to small molecules Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription.Biophysical probes reveal a "compromise" nature of the methyl-lysine binding pocket in L3MBTL1.Small-molecule modulators of methyl-lysine binding for the CBX7 chromodomain.Histones: at the crossroads of peptide and protein chemistry.Chemical biology of protein arginine modifications in epigenetic regulation Identification and characterization of nardilysin as a novel dimethyl H3K4-binding protein involved in transcriptional regulation.SETD7 Regulates the Differentiation of Human Embryonic Stem Cells.Genetically encoded fluorophenylalanines enable insights into the recognition of lysine trimethylation by an epigenetic reader.Cation-π interactions: computational analyses of the aromatic box motif and the fluorination strategy for experimental evaluation Chemical basis for the recognition of trimethyllysine by epigenetic reader proteins.Discovery of a chemical probe for the L3MBTL3 methyllysine reader domain.Antigen clasping by two antigen-binding sites of an exceptionally specific antibody for histone methylation Serum Stability and Affinity Optimization of an M2 Macrophage-Targeting Peptide (M2pep).Design of highly stabilized beta-hairpin peptides through cation-pi interactions of lysine and n-methyllysine with an aromatic pocket Nucleosome remodeling and transcriptional repression are distinct functions of Isw1 in Saccharomyces cerevisiae.NMR assignments and histone specificity of the ING2 PHD finger Importance of charge independent effects in readout of the trimethyllysine mark by HP1 chromodomain.Structural insight into histone recognition by the ING PHD fingers

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P2860

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

http://www.wikidata.org/entity/Q30443981

description

2007 nî lūn-bûn

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2007 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2007 թվականի հունիսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

@ast

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

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type

label

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

@ast

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

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prefLabel

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

@ast

Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

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Proceedings of the National Academy of Sciences of the United States of America

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Recognition of trimethyllysine by a chromodomain is not driven by the hydrophobic effect.

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Kimberly R Wiggins

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Marcey L Waters

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Robert M Hughes

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Sepideh Khorasanizadeh

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P2860

Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail

Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9

Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains

The language of covalent histone modifications

The Cationminus signpi Interaction

The nucleosome: from genomic organization to genomic regulation

Double chromodomains cooperate to recognize the methylated histone H3 tail

The diverse functions of histone lysine methylation

Regulation of HP1-chromatin binding by histone H3 methylation and phosphorylation

Substituent effects on cation- interactions: A quantitative study

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