HIV-1 encoded virus protein U (Vpu) solution structure of the 41-62 hydrophilic region containing the phosphorylated sites Ser52 and Ser56. (Q43917228)

28 November 2017

HIV-1 encoded virus protein U (Vpu) solution structure of the 41-62 hydrophilic region containing the phosphorylated sites Ser52 and Ser56. (English)

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28 November 2017

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Gaël Coadou

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28 November 2017

Nathalie Evrard-Todeschi

2

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28 November 2017

Josyane Gharbi-Benarous

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28 November 2017

Richard Benarous

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28 November 2017

Jean Pierre Girault

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28 November 2017

1 March 2002

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International Journal of Biological Macromolecules

28 November 2017

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28 November 2017

30

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28 November 2017

1

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28 November 2017

23-40

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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

28 November 2017

1 reference

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Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments

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Solution structure of the cytoplasmic domain of the human immunodeficiency virus type 1 encoded virus protein U (Vpu).

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https://api.crossref.org/works/10.1016%2FS0141-8130%2801%2900184-2

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Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution

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The human immunodeficiency virus type 1 encoded Vpu protein is phosphorylated by casein kinase-2 (CK-2) at positions Ser52 and Ser56 within a predicted alpha-helix-turn-alpha-helix-motif

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The human immunodeficiency virus type 1 Vpu protein: a potential regulator of proteolysis and protein transport in the mammalian secretory pathway

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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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Putative alpha-helical structures in the human immunodeficiency virus type 1 Vpu protein and CD4 are involved in binding and degradation of the CD4 molecule

1 reference

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Interaction between the Cytoplasmic Domains of HIV-1 Vpu and CD4: Role of Vpu Residues Involved in CD4 Interaction andin VitroCD4 Degradation

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CD4 glycoprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway

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Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors

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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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Solution structure of the hydrophilic region of HIV-1 encoded virus protein U (Vpu) by CD and lH NMR spectroscopy

1 reference

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7 January 2021

Membrane interactions and alignment of structures within the HIV-1 Vpu cytoplasmic domain: effect of phosphorylation of serines 52 and 56

1 reference

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1 reference

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Structure and energetics of ligand binding to proteins: Escherichia coli dihydrofolate reductase-trimethoprim, a drug-receptor system.

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Protein structure determination in solution by nuclear magnetic resonance spectroscopy

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Random-coil chemical shifts of phosphorylated amino acids.

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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy

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Studies of synthetic helical peptides using circular dichroism and nuclear magnetic resonance

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Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

1 reference

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A partially folded state of hen egg white lysozyme in trifluoroethanol: structural characterization and implications for protein folding

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Relationship between nuclear magnetic resonance chemical shift and protein secondary structure

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The application of different solvation and electrostatic models in molecular dynamics simulations of ubiquitin: how well is the X-ray structure "maintained"?

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Molecular dynamics simulations of human prion protein: importance of correct treatment of electrostatic interactions

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DOI

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28 November 2017

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