Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance. - Test2 - elhamkhani - TriplyDB

Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

http://www.wikidata.org/entity/Q37338970

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SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse functions Functional coupling between HIV-1 integrase and the SWI/SNF chromatin remodeling complex for efficient in vitro integration into stable nucleosomes Computational modeling of Repeat1 region of INI1/hSNF5: An evolutionary link with ubiquitin.HIV-1 IN inhibitors: 2010 update and perspectives Diverse roles and interactions of the SWI/SNF chromatin remodeling complex revealed using global approaches.Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Inhibition of early stages of HIV-1 assembly by INI1/hSNF5 transdominant negative mutant S6 Characterization of DNA binding property of the HIV-1 host factor and tumor suppressor protein Integrase Interactor 1 (INI1/hSNF5).Reverse Transcriptase and Cellular Factors: Regulators of HIV-1 Reverse Transcription.INI1/hSNF5-interaction defective HIV-1 IN mutants exhibit impaired particle morphology, reverse transcription and integration in vivo An Essential Role of INI1/hSNF5 Chromatin Remodeling Protein in HIV-1 Posttranscriptional Events and Gag/Gag-Pol Stability.A Cas9 Ribonucleoprotein Platform for Functional Genetic Studies of HIV-Host Interactions in Primary Human T Cells.Comparative molecular genetic analysis of simian and human HIV-1 integrase interactor INI1/SMARCB1/SNF5.Cytoplasmic interaction of the tumour suppressor protein hSNF5 with dynamin-2 controls endocytosis.

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Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

http://www.wikidata.org/entity/Q37338970

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 27 April 2009

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

@en

Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

@nl

type

label

Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

@en

Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

@nl

prefLabel

Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

@en

Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

@nl

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Journal of Biological Chemistry

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Multimerization and DNA binding properties of INI1/hSNF5 and its functional significance.

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Ganjam V Kalpana

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Jennifer Cano

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Supratik Das

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P2860

Interaction of E1 and hSNF5 proteins stimulates replication of human papillomavirus DNA

Identification of host proteins required for HIV infection through a functional genomic screen

Specificity of interaction of INI1/hSNF5 with retroviral integrases and its functional significance

Binding and stimulation of HIV-1 integrase by a human homolog of yeast transcription factor SNF5

Constitutional mutations of the hSNF5/INI1 gene predispose to a variety of cancers

A masked NES in INI1/hSNF5 mediates hCRM1-dependent nuclear export: implications for tumorigenesis

Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the human SNF-SWI complex, hSNF5/Ini1

Germline mutation of INI1/SMARCB1 in familial schwannomatosis

Structure-function analysis of integrase interactor 1/hSNF5L1 reveals differential properties of two repeat motifs present in the highly conserved region

c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function

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19903-19914

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scholarly article

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10.1074/JBC.M808141200

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30

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284

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2009-04-27T00:00:00Z

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19398554

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2740416

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