Structure of the chromatin binding (chromo) domain from mouse modifier protein 1. - Test2 - elhamkhani - TriplyDB

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

http://www.wikidata.org/entity/Q33886560

about

The two faces of Alba: the evolutionary connection between proteins participating in chromatin structure and RNA metabolism The Heterochromatin Protein 1 family Functional mammalian homologues of the Drosophila PEV-modifier Su(var)3-9 encode centromere-associated proteins which complex with the heterochromatin component M31 Dynamic associations of heterochromatin protein 1 with the nuclear envelope Selective interaction between the chromatin-remodeling factor BRG1 and the heterochromatin-associated protein HP1alpha.Molecular determinants for targeting heterochromatin protein 1-mediated gene silencing: direct chromoshadow domain-KAP-1 corepressor interaction is essential Structure-function analysis of SUV39H1 reveals a dominant role in heterochromatin organization, chromosome segregation, and mitotic progression.Cellular senescence and tumor suppressor gene p16 Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer The MRG domain of human MRG15 uses a shallow hydrophobic pocket to interact with the N-terminal region of PAM14 Chromodomain helicase DNA-binding proteins in stem cells and human developmental diseases Epigenetic virtues of chromodomains Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9 Solution structure of human cofilin: actin binding, pH sensitivity, and relationship to actin-depolymerizing factor Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin Mammalian chromodomain proteins: their role in genome organisation and expression Binding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulin MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1 Structure of the chromo barrel domain from the MOF acetyltransferase.Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3.A structural tree for proteins containing S-like beta-sheets.Does heterochromatin protein 1 always follow code?Phosphorylation site mutations in heterochromatin protein 1 (HP1) reduce or eliminate silencing activity.Functional characterization of recombinant chloroplast signal recognition particle.The hinge and chromo shadow domain impart distinct targeting of HP1-like proteins Conservation of heterochromatin protein 1 function Protein modules that manipulate histone tails for chromatin regulation.Keeping it in the family: diverse histone recognition by conserved structural folds New partners in regulation of gene expression: the enhancer of Trithorax and Polycomb Corto interacts with methylated ribosomal protein l12 via its chromodomain.Cyclin-dependent kinase-mediated phosphorylation of RBP1 and pRb promotes their dissociation to mediate release of the SAP30·mSin3·HDAC transcriptional repressor complex.A DNA methyltransferase homolog with a chromodomain exists in multiple polymorphic forms in Arabidopsis Drosophila rhino encodes a female-specific chromo-domain protein that affects chromosome structure and egg polarity Structural plasticity in human heterochromatin protein 1β Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription.Specificity, propagation, and memory of pericentric heterochromatin.The Drosophila Corto protein interacts with Polycomb-group proteins and the GAGA factor.Histones: at the crossroads of peptide and protein chemistry.Chromodomain protein Tcd1 is required for macronuclear genome rearrangement and repair in Tetrahymena

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P2860

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

http://www.wikidata.org/entity/Q33886560

description

1997 nî lūn-bûn

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1997 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

1997 թվականի մայիսին հրատարակված գիտական հոդված

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1997年の論文

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1997年論文

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1997年論文

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1997年論文

@zh-hk

1997年論文

@zh-mo

1997年論文

@zh-tw

1997年论文

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name

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

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Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

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type

label

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

@ast

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

@en

prefLabel

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

@ast

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

@en

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The EMBO Journal

P1476

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1.

@en

P2093

A R Raine

http://www.w3.org/2001/XMLSchema#string

E D Laue

http://www.w3.org/2001/XMLSchema#string

F J Stott

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L J Ball

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N V Murzina

http://www.w3.org/2001/XMLSchema#string

P B Singh

http://www.w3.org/2001/XMLSchema#string

P J Domaille

http://www.w3.org/2001/XMLSchema#string

R W Broadhurst

http://www.w3.org/2001/XMLSchema#string

S J Archer

http://www.w3.org/2001/XMLSchema#string

P2860

Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1

Mutation in a heterochromatin-specific chromosomal protein is associated with suppression of position-effect variegation in Drosophila melanogaster

A mammalian DNA-binding protein that contains a chromodomain and an SNF2/SWI2-like helicase domain

The chromo shadow domain, a second chromo domain in heterochromatin-binding protein 1, HP1

A sequence motif found in a Drosophila heterochromatin protein is conserved in animals and plants

PROCHECK: a program to check the stereochemical quality of protein structures

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius

Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus

Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy

P304

2473-2481

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scholarly article

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10.1093/EMBOJ/16.9.2473

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P433

9

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16

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Alexey G. Murzin

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1997-05-01T00:00:00Z

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14048082

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9171360

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protein structure

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1169847

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