ArticleJournal of virology2006
Antibody binding is a dominant determinant of the efficiency of human immunodeficiency virus type 1 neutralization.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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.
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.
Who cites it
34 citing papers in PubMed.
- Magnitude and breadth of the neutralizing antibody response in the RV144 and Vax003 HIV-1 vaccine efficacy trials.The Journal of infectious diseases · 2012Trial
- Magnitude and breadth of a nonprotective neutralizing antibody response in an efficacy trial of a candidate HIV-1 gp120 vaccine.The Journal of infectious diseases · 2010Trial
- Article
- Inhibition of human immunodeficiency virus (HIV-1) infectivity by expression of poorly or broadly neutralizing antibodies against Env in virus-producing cells.Journal of virology · 2024Article
- Article
- Dual Pathways of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trafficking Modulate the Selective Exclusion of Uncleaved Oligomers from Virions.Journal of virology · 2021Article
- The Conformational States of the HIV-1 Envelope Glycoproteins.Trends in microbiology · 2020Review
- Antibody responses to the HIV-1 envelope high mannose patch.Advances in immunology · 2019Review
- Bacterially expressed HIV-1 gp120 outer-domain fragment immunogens with improved stability and affinity for CD4-binding site neutralizing antibodies.The Journal of biological chemistry · 2018Article
- Comparison of Uncleaved and Mature Human Immunodeficiency Virus Membrane Envelope Glycoprotein Trimers.Journal of virology · 2018Article
- Article
- HIV-1 Consensus Envelope-Induced Broadly Binding Antibodies.AIDS research and human retroviruses · 2017Article
- HIV-host interactome revealed directly from infected cells.Nature microbiology · 2016Article
- Broadly Neutralizing Antibodies to HIV and Their Role in Vaccine Design.Annual review of immunology · 2016Review
- The V4 and V5 Variable Loops of HIV-1 Envelope Glycoprotein Are Tolerant to Insertion of Green Fluorescent Protein and Are Useful Targets for Labeling.The Journal of biological chemistry · 2015Article
- Article
- Modeling virus- and antibody-specific factors to predict human immunodeficiency virus neutralization efficiency.Cell host & microbe · 2013Article
- Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120.Nature structural & molecular biology · 2013Article
- The highly conserved layer-3 component of the HIV-1 gp120 inner domain is critical for CD4-required conformational transitions.Journal of virology · 2013Article
- Proteolytic processing of the human immunodeficiency virus envelope glycoprotein precursor decreases conformational flexibility.Journal of virology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Primary and laboratory-adapted variants of human immunodeficiency virus type 1 (HIV-1) exhibit a wide range of sensitivities to neutralization by antibodies directed against the viral envelope glycoproteins. An antibody directed against an artificial FLAG epitope inserted into the envelope glycoproteins of three HIV-1 isolates with vastly different neutralization sensitivities inhibited all three viruses equivalently. Thus, naturally occurring HIV-1 isolates that are neutralization resistant are not necessarily more impervious to the inhibitory consequences of bound antibody. Moreover, the binding affinity of the anti-FLAG antibody correlated with neutralizing potency, underscoring the dominant impact on neutralization of antibody binding to the envelope glycoproteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.