Evidence map›Paper›PMID 10590134›Full record

ArticleJournal of virology2000

Role of the cytoplasmic tail of ecotropic moloney murine leukemia virus Env protein in fusion pore formation.

G B Melikyan, R M Markosyan, S A Brener, Y Rozenberg, F S Cohen

Abstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

39 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Virus-Induced Cell Fusion and Syncytia Formation.Results and problems in cell differentiation · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Class II fusion proteins.Advances in experimental medicine and biology · 2013
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Viral membrane fusion.Nature structural & molecular biology · 2008
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

5 authors at 2 institutions in 1 country.

G B MelikyanDepartment of Molecular Biophysics and Physiology, Rush Medical College, Chicago, Illinois 60612, USA.
R M Markosyan
S A Brener
Y Rozenberg
F S Cohen
Rush University Medical Center · USUSC Norris Comprehensive Cancer Center · US

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
BIOPHYSICS OF PROTEIN MEDIATED MEMBRANE FUSIONR29GM054787 · NIGMS · RUSH UNIVERSITY MEDICAL CENTER · PI MELIKIAN, GREGORY B · 1996 to 1999
–
NIGMS NIH HHS GM27367NIGMS NIH HHS GM54787NIGMS NIH HHS R01 GM027367NIGMS NIH HHS R01 GM054787NIGMS NIH HHS R29 GM054787
6 · The paper itself

Abstract

Fusion between cells expressing envelope protein (Env) of Moloney murine leukemia virus and target cells were studied by use of video fluorescence microscopy and electrical capacitance measurements. When the full-length 632-amino-acid residue Env was expressed, fusion did not occur at all for 3T3 cells as target and only somewhat for XC6 cells. Expression of Env 616*-a construct of Env with the last 16 amino acid residues (617 to 632; the R peptide) deleted from its C terminus to match the proteolytically cleaved Env produced during viral budding-resulted in high levels of fusion. Env 601*, lacking the entire cytoplasmic tail (CT) (identified by hydrophobicity), also led to fusion. Truncation of an additional six residues (Env 595*) abolished fusion. The kinetics of forming fusion pores did not depend on whether cells were first prebound at 4 degrees C and the time until fusion measured after the temperature was raised to 37 degrees C or whether cells were first brought into contact at 37 degrees C and the time until fusion immediately measured. This similarity in kinetics indicates that binding is accomplished quickly compared to subsequent steps in fusion. The fusion pores formed by Env 601* and Env 616* had the same initial size and enlarged in similar manners. Thus, once the R peptide is removed, the CT is not needed for fusion and does not affect formed pores. However, residues 595 to 601 are required for fusion. It is suggested here that the ectodomain and membrane-spanning domain of Env are directly responsible for fusion and that the R peptide affects their configurations at some point during the fusion process, thereby indirectly controlling fusion.

Indexed as

Cell Fusion3T3 CellsAnimalsCell LineCytoplasmGene Products, envHumansMiceMoloney murine leukemia virusGene Products, env

Identifiers

PMID10590134
PMCPMC111556
OpenAlexW2006041366

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.