Structural basis for spumavirus GAG tethering to chromatin

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Murine leukemia virus p12 tethers the capsid-containing pre-integration complex to chromatin by binding directly to host nucleosomes in mitosis.The invariant arginine within the chromatin-binding motif regulates both nucleolar localization and chromatin binding of Foamy virus Gag.

P2860

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P2860

Structural basis for spumavirus GAG tethering to chromatin

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http://www.wikidata.org/entity/Q33737883

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name

Structural basis for spumavirus GAG tethering to chromatin

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Structural basis for spumavirus GAG tethering to chromatin

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Structural basis for spumavirus GAG tethering to chromatin

@ast

Structural basis for spumavirus GAG tethering to chromatin

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prefLabel

Structural basis for spumavirus GAG tethering to chromatin

@ast

Structural basis for spumavirus GAG tethering to chromatin

@en

P1154

2-s2.0-85019556762

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P1433

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

P1476

Structural basis for spumavirus GAG tethering to chromatin

@en

P2093

Alan N Engelman

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

Daniel P Maskell

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

Erik Serrao

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

Paul Lesbats

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

Valerie E Pye

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

P2860

An integrated encyclopedia of DNA elements in the human genome

HIV-1 capsid-cyclophilin interactions determine nuclear import pathway, integration targeting and replication efficiency

LEDGF/p75 determines cellular trafficking of diverse lentiviral but not murine oncoretroviral integrase proteins and is a component of functional lentiviral preintegration complexes

LEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration

Retroviral DNA integration: ASLV, HIV, and MLV show distinct target site preferences

Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 a resolution

Structure of RCC1 chromatin factor bound to the nucleosome core particle

Structural Basis of Silencing: Sir3 BAH Domain in Complex with a Nucleosome at 3.0 A Resolution

A Conserved Mechanism for Centromeric Nucleosome Recognition by Centromere Protein CENP-C

HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells

P304

5509-5514

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scholarly article

P356

10.1073/PNAS.1621159114

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P407

English

P433

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P478

114

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P50

Dirk Lindemann

Peter Cherepanov

Nicola O'Reilly

P5530

20066468

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P577

2017-05-10T00:00:00Z

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1085464468

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84915313

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28490494

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5448199

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117790/