Evidence map›Paper›PMID 26362058›Full record

ArticleBiochimica et biophysica acta2015

Structural determination of virus protein U from HIV-1 by NMR in membrane environments.

Hua Zhang, Eugene C Lin, Bibhuti B Das, Ye Tian, Stanley J Opella

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PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. The soluble state of the HIV-1 Vpu protein forms a complex with CaProtein science : a publication of the Protein Society · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Hua Zhang *Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307.
Eugene C Lin *Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307.
Bibhuti B DasDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307.
Ye TianDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307.
Stanley J OpellaDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0307.
University of California San Diego · USSanford Burnham Prebys Medical Discovery Institute · US

Funding

RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
Structure, Dynamics, and Functions of the Viroporins Vpu from HIV and p7 from HCVR01GM066978 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2016
$3.5M
Vpu inhibits NK cell function through down regulation of NTB-AR01AI065361 · NIAID · UPSTATE MEDICAL UNIVERSITY · PI BARKER, EDWARD · 2006 to 2016
$2.9M
Structure Determination of Membrane Proteins in Phospholipid BilyaersR01GM099986 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2012 to 2015
$1.1M
NIAID NIH HHS R01 AI065361NIAID NIH HHS R01AI065361NIBIB NIH HHS P41 EB002031NIBIB NIH HHS P41EB002031NIGMS NIH HHS R01 GM066978NIGMS NIH HHS R01GM066978NIGMS NIH HHS R01 GM099986NIGMS NIH HHS R01GM099986
6 · The paper itself

Abstract

Virus protein U (Vpu) from HIV-1, a small membrane protein composed of a transmembrane helical domain and two α-helices in an amphipathic cytoplasmic domain, down modulates several cellular proteins, including CD4, BST-2/CD317/tetherin, NTB-A, and CCR7. The interactions of Vpu with these proteins interfere with the immune system and enhance the release of newly synthesized virus particles. It is essential to characterize the structure and dynamics of Vpu in order to understand the mechanisms of the protein-protein interactions, and potentially to discover antiviral drugs. In this article, we describe investigations of the cytoplasmic domain of Vpu as well as full-length Vpu by NMR spectroscopy. These studies are complementary to earlier analysis of the transmembrane domain of Vpu. The results suggest that the two helices in the cytoplasmic domain form a U-shape. The length of the inter-helical loop in the cytoplasmic domain and the orientation of the third helix vary with the lipid composition, which demonstrate that the C-terminal helix is relatively flexible, providing accessibility for interaction partners.

Indexed as

Cell MembraneCircular DichroismDiffusionDimyristoylphosphatidylcholineHIV-1Human Immunodeficiency Virus ProteinsHumansKineticsMagnetic Resonance SpectroscopyMembrane ProteinsMicellesModels, MolecularPhospholipid EthersProtein BindingProtein Structure, SecondaryProtein Structure, Tertiary1,2-dihexadecyl-sn-glycero-3-phosphocholineDimyristoylphosphatidylcholineHuman Immunodeficiency Virus ProteinsMembrane ProteinsMicellesPhospholipid EthersProteolipidsproteoliposomesViral Regulatory and Accessory ProteinsViroporin Proteinsvpu protein, Human immunodeficiency virus 1Human immunodeficiency virus (HIV)Lipid bilayersMembrane proteinNuclear magnetic resonance (NMR)Viral protein U (Vpu)

Identifiers

PMID26362058
PMCPMC4623708
OpenAlexW2233751927

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.