Evidence map›Paper›PMID 21284899›Full record

ReviewJournal of translational medicine2011

Conformational HIV-1 envelope on particulate structures: a tool for chemokine coreceptor binding studies.

Maria Tagliamonte, Maria Lina Tornesello, Franco M Buonaguro, Luigi Buonaguro

Open access · goldAbstract readReview
In one paragraph

Review in Journal of translational medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-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

3 citing papers in PubMed, 14 citations in OpenAlex.

  1. Unraveling the complexities of neurotropic virus infection and immune evasion.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  2. Article
  3. Article
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

4 authors at 1 institution in 2 countries.

Maria TagliamonteLab, of Molecular Biology and Viral Oncogenesis & AIDS Reference Center, Istituto Nazionale Tumori Fond, G, Pascale, Naples, Italy.
Maria Lina Tornesello
Franco M Buonaguro
Luigi Buonaguro
Istituto Nazionale Tumori IRCCS "Fondazione G. Pascale" · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human immunodeficiency virus type 1 (HIV-1) external envelope glycoprotein gp120 presents conserved binding sites for binding to the primary virus receptor CD4 as well as the major HIV chemokine coreceptors, CCR5 and CXCR4. Concerted efforts are underway to understand the specific interactions between gp120 and coreceptors as well as their contribution to the subsequent membrane fusion process. The present review summarizes the current knowledge on this biological aspect, which represents one of the key and essential points of the HIV-host cell interplay and HIV life cycle. The relevance of conformational HIV-1 Envelope proteins presented on Virus-like Particles for appropriate assessment of this molecular interaction, is also discussed.

Indexed as

AnimalsCD4-Positive T-LymphocytesChemokinesGene Products, envHIV-1HIV Envelope Protein gp120HumansMacaca mulattaProtein BindingProtein ConformationReceptors, CCR5Receptors, CXCR4Vaccines, Virus-Like ParticleChemokinesCXCR4 protein, humanGene Products, envgp120 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120Receptors, CCR5Receptors, CXCR4Vaccines, Virus-Like Particle

Identifiers

PMID21284899
PMCPMC3105500
OpenAlexW2120077970

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.