Evidence map›Paper›PMID 28622976›Full record

ArticleBiochimica et biophysica acta. Biomembranes2017

Differential binding of the HIV-1 envelope to phosphatidylserine receptors.

Linlin Gu, Brian Sims, Alexandre Krendelchtchikov, Edlue Tabengwa, Qiana L Matthews

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Efferocytosis of Pathogen-Infected Cells.Frontiers in immunology · 2017
    Review
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 1 institution in 1 country.

Linlin GuDepartment of Medicine, Division of Infectious Diseases, University of Alabama at Birmingham, USA.
Brian SimsDepartments of Pediatrics, Neurobiology and Cell, Developmental and Integrative Biology, Division of Neonatology, University of Alabama at Birmingham, USA.
Alexandre KrendelchtchikovDepartment of Medicine, Division of Infectious Diseases, University of Alabama at Birmingham, USA; Departments of Pediatrics, Neurobiology and Cell, Developmental and Integrative Biology, Division of Neonatology, University of Alabama at Birmingham, USA.
Edlue TabengwaComprehensive Cancer Center, University of Alabama at Birmingham, USA.
Qiana L MatthewsCenter for AIDS Research, University of Alabama at Birmingham; Birmingham, AL, USA; Microbiology Programs, Department of Biological Sciences, College of Science, Technology, Engineering and Mathematic, Alabama State University, USA. Electronic address: matthewsqiana@gmail.com.
University of Alabama at Birmingham · US

Funding

Virology CoreP30AI027767 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI OLAF KUTSCH · 1988 to 2026
$84.1M
Chimeric adenoviruses for an improved HIV vaccineR01AI089337 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI MATTHEWS, QIANA L · 2011 to 2014
$1.4M
UAB Shared Biacore T100 BiosensorS10RR026935 · NCRR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DAVIS, RANDALL S · 2010 to 2010
$365k
NCRR NIH HHS S10 RR026935NIAID NIH HHS P30 AI027767NIAID NIH HHS R01 AI089337
6 · The paper itself

Abstract

Prior work has shown that the HIV-1 envelope of the human immunodeficiency virus (HIV) interacts directly with T-cell immunoglobulin mucin (TIM) family proteins. Herein, we demonstrate that HIV-1 envelope glycoproteins from varying HIV-1 clades bind differentially to TIM proteins and functionally similar proteins acting as phosphatidylserine (PtdSer) receptors. Using enzyme-linked immunosorbent assay (ELISA) and surface plasmon resonance (SPR) technology, we show that lysate containing HIV-1 envelope and recombinant HIV-1 envelope glycoproteins bind TIM-4 and advanced glycosylation end product-specific receptor (AGER). The complex binding of HIV-1 UG21 gp140 to TIM-4 or AGER suggests a biphasic interaction with these proteins.

Indexed as

Cell LineEnzyme-Linked Immunosorbent AssayHEK293 CellsHIV-1HIV InfectionsHuman Immunodeficiency Virus ProteinsHumansMembrane GlycoproteinsReceptor for Advanced Glycation End ProductsReceptors, Cell SurfaceReceptors, VirusRecombinant ProteinsViral Envelope ProteinsHuman Immunodeficiency Virus ProteinsMembrane Glycoproteinsphosphatidylserine receptorReceptor for Advanced Glycation End ProductsReceptors, Cell SurfaceReceptors, VirusRecombinant ProteinsViral Envelope ProteinsAdvanced glycosylation end product-specific receptorGlycoproteinsHuman immunodeficiency virusPhosphatidylserineSurface plasmon resonanceT-cell immunoglobulin mucin

Identifiers

PMID28622976
PMCPMC5593811
OpenAlexW2624783747

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.