Conserved residues within the HIV-1 Vpu transmembrane-proximal hinge region modulate BST2 binding and antagonism.

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Conserved residues within the HIV-1 Vpu transmembrane-proximal hinge region modulate BST2 binding and antagonism.

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http://www.wikidata.org/entity/Q38910738

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

@zh-cn

2017年学术文章

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2017年学术文章

@zh-my

2017年学术文章

@zh-sg

2017年學術文章

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2017年學術文章

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2017年學術文章

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name

Conserved residues within the ...... e BST2 binding and antagonism.

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type

Item

label

Conserved residues within the ...... e BST2 binding and antagonism.

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prefLabel

Conserved residues within the ...... e BST2 binding and antagonism.

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P1476

Conserved residues within the ...... te BST2 binding and antagonism

@en

P2093

Sabelo Lukhele

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P2860

HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation

Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps

HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactions

Structural basis of HIV-1 Vpu-mediated BST2 antagonism via hijacking of the clathrin adaptor protein complex 1

Broad-spectrum inhibition of retroviral and filoviral particle release by tetherin

Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism

Silencing of both beta-TrCP1 and HOS (beta-TrCP2) is required to suppress human immunodeficiency virus type 1 Vpu-mediated CD4 down-modulation

The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation

A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif

Mechanism of HIV-1 virion entrapment by tetherin

P2888

s12977-017-0345-6

P304

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P31

scholarly article

P356

10.1186/S12977-017-0345-6

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P433

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P478

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P50

Éric A Cohen

P577

2017-03-14T00:00:00Z

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P6179

1084251560

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P698

28288652

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

P921

transmembrane protein

P932

5348903

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