Evidence map›Paper›PMID 18568847›Full record

ReviewCritical reviews in biochemistry and molecular biology

Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme.

Judith M White, Sue E Delos, Matthew Brecher, Kathryn Schornberg

Erratum issuedAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 583 papers.

0numbers the graph read from it
0cells of the map it votes in
583citing papers in PubMed
52.8field-weighted citation impact, top 1% 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

583 citing papers in PubMed, 892 citations in OpenAlex.

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523 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Judith M WhiteDepartment of Cell Biology, University of Virginia, Charlottesville, Virginia 22908-0732, USA. jw7g@virginia.edu
Sue E Delos
Matthew Brecher
Kathryn Schornberg
University of Virginia · US

Funding

Vaccine strategy for broad spectrum protection agains non-typhoidal salmonellU54AI057168 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI LEVINE, MYRON MAX · 2003 to 2013
$91.5M
INFECTIOUS DISEASES TRAINING PROGRAMT32AI007046 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Alison K Criss, William A Petri · 1985 to 2026
$15.3M
Global Biothreats Training ProgramT32AI055432 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI CRISS, ALISON K, PETRI, WILLIAM A · 2003 to 2022
$4.0M
MOLECULAR MECHANISMS OF VIRAL MEMBRANE FUSION PROTEINSR01AI022470 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI WHITE, JUDITH M. · 1985 to 2009
$3.4M
Fusion Mechanism of the Ebola Virus GlycoproteinR21AI055925 · NIAID · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI WHITE, JUDITH M. · 2003 to 2004
$595k
NIAID NIH HHS AI22470NIAID NIH HHS R01 AI022470NIAID NIH HHS R21 AI055925NIAID NIH HHS R21AI055925NIAID NIH HHS T32 AI007046NIAID NIH HHS T32 AI055432NIAID NIH HHS U54 AI057168NIAID NIH HHS U54 AI57168
6 · The paper itself

Abstract

Recent work has identified three distinct classes of viral membrane fusion proteins based on structural criteria. In addition, there are at least four distinct mechanisms by which viral fusion proteins can be triggered to undergo fusion-inducing conformational changes. Viral fusion proteins also contain different types of fusion peptides and vary in their reliance on accessory proteins. These differing features combine to yield a rich diversity of fusion proteins. Yet despite this staggering diversity, all characterized viral fusion proteins convert from a fusion-competent state (dimers or trimers, depending on the class) to a membrane-embedded homotrimeric prehairpin, and then to a trimer-of-hairpins that brings the fusion peptide, attached to the target membrane, and the transmembrane domain, attached to the viral membrane, into close proximity thereby facilitating the union of viral and target membranes. During these conformational conversions, the fusion proteins induce membranes to progress through stages of close apposition, hemifusion, and then the formation of small, and finally large, fusion pores. Clearly, highly divergent proteins have converged on the same overall strategy to mediate fusion, an essential step in the life cycle of every enveloped virus.

Indexed as

Virus InternalizationAnimalsCell MembraneHumansHydrogen-Ion ConcentrationReceptors, VirusViral Fusion ProteinsReceptors, VirusViral Fusion Proteins

Identifiers

PMID18568847
PMCPMC2649671
OpenAlexW2143312809

What OpenQuestion holds

Textmetadata
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.