ReviewThe FEBS journal2017
Structure of the transmembrane domain of HIV-1 envelope glycoprotein.
Review in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed, 22 citations in OpenAlex.
- Oral yeast-displayed SARS-CoV-2 spike protein vaccine enhanced by trimerization and flagellin peptide.Scientific reports · 2026Article
- Purification and characterization of the Lassa virus transmembrane domain.Biochemistry and biophysics reports · 2023Article
- A trimeric hydrophobic zipper mediates the intramembrane assembly of SARS-CoV-2 spike.bioRxiv : the preprint server for biology · 2021Article
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- HIV-1 Envelope and MPER Antibody Structures in Lipid Assemblies.Cell reports · 2020Article
- Structural Basis for Broad HIV-1 Neutralization by the MPER-Specific Human Broadly Neutralizing Antibody LN01.Cell host & microbe · 2019Article
- HIV-1 Envelope Glycoprotein Amino Acids Signatures Associated with Clade B Transmitted/Founder and Recent Viruses.Viruses · 2019Article
- Structural Variability in the RLR-MAVS Pathway and Sensitive Detection of Viral RNAs.Medicinal chemistry (Shariqah (United Arab Emirates)) · 2019Review
- Role of the HIV-1 envelope transmembrane domain in intracellular sorting.BMC cell biology · 2018Article
- Stability and Water Accessibility of the Trimeric Membrane Anchors of the HIV-1 Envelope Spikes.Journal of the American Chemical Society · 2017Article
- Antigenicity-defined conformations of an extremely neutralization-resistant HIV-1 envelope spike.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
HIV-1 envelope spike (Env) is a heavily glycosylated, type I membrane protein that mediates fusion of viral and cell membranes to initiate infection. It is also a primary target of neutralizing antibodies and thus an important candidate for vaccine development. We have recently reported a nuclear magnetic resonance structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in a membrane-like environment. Taking HIV-1 as an example, we discuss here how a TM domain can anchor, stabilize, and modulate a viral envelope spike and how its high-resolution structure can contribute to understanding viral membrane fusion and to immunogen design.
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.