Evidence map›Paper›PMID 11069998›Full record

ArticleJournal of virology2000

The carboxy-terminal fragment of nucleolin interacts with the nucleocapsid domain of retroviral gag proteins and inhibits virion assembly.

E Bacharach, J Gonsky, K Alin, M Orlova, S P Goff

Open access · greenAbstract 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 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.8field-weighted citation impact, top 14% 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

29 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Identification of a novel RNA virus lethal to tilapia.Journal of clinical microbiology · 2014
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Profile of Stephen P. Goff. Interview by Greg Williams.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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  18. Review
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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 4 institutions in 3 countries.

E BacharachHoward Hughes Medical Institute, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.
J Gonsky
K Alin
M Orlova
S P Goff
Howard Hughes Medical Institute · USCellular Therapeutics (United Kingdom) · GBColumbia University · USInstitute of Molecular Biology and Biophysics · RU

Funding

Mechanisms of Silencing of Retroviral DNAs in Embryonic Cell LinesR01CA030488 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI GOFF, STEPHEN PAINE · 1985 to 2024
$4.3M
CONSTRUCTION AND ANALYSIS OF RETROVIRUS MUTANTSR37CA030488 · NCI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI GOFF, STEPHEN PAINE · 1990 to 2013
$2.2M
NCI NIH HHS CA 30488NCI NIH HHS R01 CA030488NCI NIH HHS R37 CA030488
6 · The paper itself

Abstract

A yeast two-hybrid screen for cellular proteins that interact with the murine leukemia virus (MuLV) Gag protein resulted in the identification of nucleolin, a host protein known to function in ribosome assembly. The interacting fusions contained the carboxy-terminal 212 amino acids of nucleolin [Nuc(212)]. The nucleocapsid (NC) portion of Gag was necessary and sufficient to mediate the binding to Nuc(212). The interaction of Gag with Nuc(212) could be demonstrated in vitro and was manifested in vivo by the NC-dependent incorporation of Nuc(212) inside MuLV virions. Overexpression of Nuc(212), but not full-length nucleolin, potently and specifically blocked MuLV virion assembly and/or release. A mutant of MuLV, selected to specifically disrupt the binding to Nuc(212), was found to be severely defective for virion assembly. This mutant harbors a single point mutation in capsid (CA) adjacent to the CA-NC junction, suggesting a role for this region in Moloney MuLV assembly. These experiments demonstrate that selection for proteins that bind assembly domain(s) can yield potent inhibitors of virion assembly. These experiments also raise the possibility that a nucleolin-Gag interaction may be involved in virion assembly.

Indexed as

Virus AssemblyAnimalsCOS CellsGene Products, gagNucleocapsidNucleolinPhosphoproteinsRetroviridaeRNA-Binding ProteinsVirionGene Products, gagNucleolinPhosphoproteinsRNA-Binding Proteins

Identifiers

PMID11069998
PMCPMC113183
OpenAlexW2142913486

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.