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 (Q28276184)

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S P Bour

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H Durand

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L Selig

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V Richard

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D Thomas

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K Strebel

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R Benarous

SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box

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language of work or name

English

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publication date

March 1998

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published in

Molecular Cell

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volume

1

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issue

4

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page(s)

565-74

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cites work

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

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Human immunodeficiency virus type 1 Vpu protein induces degradation of CD4 in vitro: the cytoplasmic domain of CD4 contributes to Vpu sensitivity

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Identification of a protein encoded by the vpu gene of HIV-1.

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A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p

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Fission yeast WD-repeat protein pop1 regulates genome ploidy through ubiquitin-proteasome-mediated degradation of the CDK inhibitor Rum1 and the S-phase initiator Cdc18.

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Grr1 of Saccharomyces cerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: coupling glucose sensing to gene expression and the cell cycle

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Phosphorylation of both phosphoacceptor sites in the HIV-1 Vpu cytoplasmic domain is essential for Vpu-mediated ER degradation of CD4

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

9660940

1 reference

Consolidated OpenCitations Corpus – April 2017