Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S - Test2 - elhamkhani - TriplyDB

Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S

Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S

http://www.wikidata.org/entity/Q27652290

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Molecular basis for H3K36me3 recognition by the Tudor domain of PHF1 An H3K36 methylation-engaging Tudor motif of polycomb-like proteins mediates PRC2 complex targeting PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53 Epigenetic virtues of chromodomains Molecular Basis of the Interaction of Saccharomyces cerevisiae Eaf3 Chromo Domain with Methylated H3K36 Structural and biochemical studies of the 5′→3′ exoribonuclease Xrn1 Solution Structure of the mSin3A PAH2–Pf1 SID1 Complex: A Mad1/Mxd1-Like Interaction Disrupted by MRG15 in the Rpd3S/Sin3S Complex Structural and Histone Binding Ability Characterizations of Human PWWP Domains Structural Basis for Specific Binding of Human MPP8 Chromodomain to Histone H3 Methylated at Lysine 9 Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2/3 Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology Structural Insight into Recognition of Methylated Histone Tails by Retinoblastoma-binding Protein 1 Structural Basis of the Chromodomain of Cbx3 Bound to Methylated Peptides from Histone H1 and G9a A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions.Eaf5/7/3 form a functionally independent NuA4 submodule linked to RNA polymerase II-coupled nucleosome recycling.SETD2: an epigenetic modifier with tumor suppressor functionality Chemical and biological tools for the preparation of modified histone proteins Preparation of recombinant peptides with site- and degree-specific lysine (13)C-methylation.The Dnmt3a PWWP domain reads histone 3 lysine 36 trimethylation and guides DNA methylation.Arabidopsis MRG domain proteins bridge two histone modifications to elevate expression of flowering genes Keeping it in the family: diverse histone recognition by conserved structural folds Structural and biochemical studies on the chromo-barrel domain of male specific lethal 3 (MSL3) reveal a binding preference for mono- or dimethyllysine 20 on histone H4.Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription.Towards understanding methyllysine readout.Nucleosome contact triggers conformational changes of Rpd3S driving high-affinity H3K36me nucleosome engagement.Structure and nucleosome interaction of the yeast NuA4 and Piccolo-NuA4 histone acetyltransferase complexes.Combined Interactions of Plant Homeodomain and Chromodomain Regulate NuA4 Activity at DNA Double-Strand Breaks.Perceiving the epigenetic landscape through histone readers.Histone tails: ideal motifs for probing epigenetics through chemical biology approaches.X chromosomal regulation in flies: when less is more.NuA4 and SWR1-C: two chromatin-modifying complexes with overlapping functions and components.Physiological roles of class I HDAC complex and histone demethylase.Transcription-associated histone modifications and cryptic transcription.Systematic analysis of histone modification readout.Tudor: a versatile family of histone methylation 'readers'.Touch, act and go: landing and operating on nucleosomes.A Structural Perspective on Readout of Epigenetic Histone and DNA Methylation Marks.Shaping the cellular landscape with Set2/SETD2 methylation.Structural Basis for Multi-specificity of MRG Domains.Histone H3 lysine 36 methylation targets the Isw1b remodeling complex to chromatin.

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Structural Basis for the Recognition of Methylated Histone H3K36 by the Eaf3 Subunit of Histone Deacetylase Complex Rpd3S

http://www.wikidata.org/entity/Q27652290

description

2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2008 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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Structural Basis for the Recog ...... tone Deacetylase Complex Rpd3S

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J.STR.2008.08.008

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Structural basis for the recog ...... tone deacetylase complex Rpd3S

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Gaofeng Cui

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Georges Mer

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Maria Victoria Botuyan

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Crystal structure of the nucleosome core particle at 2.8 A resolution

NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p

Distinct binding modes specify the recognition of methylated histones H3K4 and H4K20 by JMJD2A-tudor

Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair

Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA

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

L3MBTL1 recognition of mono- and dimethylated histones

Structural Basis for Lower Lysine Methylation State-Specific Readout by MBT Repeats of L3MBTL1 and an Engineered PHD Finger

The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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1740-1750

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10.1016/J.STR.2008.08.008

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18818090

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structural biology

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2582589

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