Evidence map›Paper›PMID 10359599›Full record

ArticleMolecular biology of the cell1999

Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion.

G B Melikyan, S Lin, M G Roth, F S Cohen

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
–field-weighted citation impact
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

79 citing papers in PubMed.

  1. Article
  2. Article
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  4. Article
  5. Article
  6. Computational methods to study enveloped viral entry.Biochemical Society transactions · 2021
    Review
  7. Article
  8. Review
  9. Influenza hemagglutinin drives viral entry via two sequential intramembrane mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

19 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

4 authors.

G B MelikyanDepartment of Molecular Biophysics and Physiology, Rush Medical College, Chicago, Illinois 60612, USA.
S Lin
M G Roth
F S Cohen

Funding

BIOPHYSICS OF PROTEIN-MEDIATED MEMBRANE FUSIONR01GM054787 · NIGMS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI MELIKIAN, GREGORY B · 2000 to 2018
$6.5M
MODEL SYSTEM FOR PHYSIOLOGICAL EXOCYTOSISR01GM027367 · NIGMS · RUSH UNIVERSITY MEDICAL CENTER · PI COHEN, FREDRIC S · 1985 to 2009
$4.2M
RECOGNITION AND SORTING OF GLYCOPROTEINSR01GM037547 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI ROTH, MICHAEL G · 1987 to 2002
$837k
BIOPHYSICS OF PROTEIN MEDIATED MEMBRANE FUSIONR29GM054787 · NIGMS · RUSH UNIVERSITY MEDICAL CENTER · PI MELIKIAN, GREGORY B · 1996 to 1999
–
NIGMS NIH HHS GM-27367NIGMS NIH HHS GM-37547NIGMS NIH HHS GM-54787NIGMS NIH HHS R01 GM027367NIGMS NIH HHS R01 GM054787NIGMS NIH HHS R29 GM054787
6 · The paper itself

Abstract

The amino acid sequence requirements of the transmembrane (TM) domain and cytoplasmic tail (CT) of the hemagglutinin (HA) of influenza virus in membrane fusion have been investigated. Fusion properties of wild-type HA were compared with those of chimeras consisting of the ectodomain of HA and the TM domain and/or CT of polyimmunoglobulin receptor, a nonviral integral membrane protein. The presence of a CT was not required for fusion. But when a TM domain and CT were present, fusion activity was greater when they were derived from the same protein than derived from different proteins. In fact, the chimera with a TM domain of HA and truncated CT of polyimmunoglobulin receptor did not support full fusion, indicating that the two regions are not functionally independent. Despite the fact that there is wide latitude in the sequence of the TM domain that supports fusion, a point mutation of a semiconserved residue within the TM domain of HA inhibited fusion. The ability of a foreign TM domain to support fusion contradicts the hypothesis that a pore is composed solely of fusion proteins and supports the theory that the TM domain creates fusion pores after a stage of hemifusion has been achieved.

Indexed as

Amino Acid SequenceCell MembraneCytoplasmErythrocytesHemagglutinin Glycoproteins, Influenza VirusHumansKineticsMembrane FusionMolecular Sequence DataPoint MutationProtein FoldingRecombinant ProteinsHemagglutinin Glycoproteins, Influenza VirusRecombinant Proteins

Identifiers

PMID10359599
PMCPMC25377

What OpenQuestion holds

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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.