Evidence map›Paper›PMID 25866377›Full record

ReviewVirology2015

Viral membrane fusion.

Stephen C Harrison

Open access · hybridAbstract readReview
In one paragraph

Review in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 473 papers.

0numbers the graph read from it
0cells of the map it votes in
473citing papers in PubMed
67.0field-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

473 citing papers in PubMed, 722 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. How endosomal PIKfyve inhibition prevents viral membrane fusion and entry.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Dermcidin has antiviral activity and protects against influenza.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Review

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

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

1 author at 1 institution in 1 country.

Stephen C HarrisonBoston Children׳s Hospital, Harvard Medical School, and Howard Hughes Medical Institute, 3 Blackfan Circle, Boston, MA 02115, United States. Electronic address: harrison@crystal.harvard.edu.
Boston Children's Hospital · US

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WHELAN, SEAN PJ · 2003 to 2013
$113.7M
Virology CoreP01AI089618 · NIAID · BOSTON CHILDREN'S HOSPITAL · PI Jiwon Lee · 2011 to 2026
$40.0M
Small-molecule inhibitors of flavivirus entryU19AI109740 · NIAID · HARVARD MEDICAL SCHOOL · PI WHELAN, SEAN PJ · 2014 to 2018
$23.0M
STRUCTURE AND ASSEMBLY OF VIRUSES AND OF COATED VESICLESR01CA013202 · NCI · HARVARD UNIVERSITY · PI HARRISON, STEPHEN COPLAN · 1985 to 2024
$4.9M
Structure and Assembly of VirusesR37CA013202 · NCI · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2012
$3.7M
Howard Hughes Medical InstituteNCI NIH HHS CA13202NCI NIH HHS R01 CA013202NCI NIH HHS R37 CA013202NIAID NIH HHS AI057159NIAID NIH HHS AI109740NIAID NIH HHS P01 AI089618NIAID NIH HHS U19 AI109740NIAID NIH HHS U54 AI057159
6 · The paper itself

Abstract

Membrane fusion is an essential step when enveloped viruses enter cells. Lipid bilayer fusion requires catalysis to overcome a high kinetic barrier; viral fusion proteins are the agents that fulfill this catalytic function. Despite a variety of molecular architectures, these proteins facilitate fusion by essentially the same generic mechanism. Stimulated by a signal associated with arrival at the cell to be infected (e.g., receptor or co-receptor binding, proton binding in an endosome), they undergo a series of conformational changes. A hydrophobic segment (a "fusion loop" or "fusion peptide") engages the target-cell membrane and collapse of the bridging intermediate thus formed draws the two membranes (virus and cell) together. We know of three structural classes for viral fusion proteins. Structures for both pre- and postfusion conformations of illustrate the beginning and end points of a process that can be probed by single-virion measurements of fusion kinetics.

Indexed as

Host-Pathogen InteractionsVirus InternalizationProtein ConformationViral Fusion ProteinsViral Fusion ProteinsFusion mechanismFusion proteinVirus entry

Identifiers

PMID25866377
PMCPMC4424100
OpenAlexW2048172399

What OpenQuestion holds

Textmetadata
LicenceTDM
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.