Evidence map›Paper›PMID 9371647›Full record

ArticleJournal of virology1997

Antiviral determinants of rat Mx GTPases map to the carboxy-terminal half.

L Johannes, R Kambadur, H Lee-Hellmich, C A Hodgkinson, H Arnheiter, E Meier

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.7field-weighted citation impact, top 29% 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

10 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. [Identification of dynamic co-expression networks in peripheral blood of rats after middle cerebral artery occlusion].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2019
    Article
  3. Mx proteins: antiviral gatekeepers that restrain the uninvited.Microbiology and molecular biology reviews : MMBR · 2013
    Review
  4. Review
  5. Review
  6. Mx gene diversity and influenza association among five wild dabbling duck species (Anas spp.) in Alaska.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2010
    Article
  7. Review
  8. Article
  9. Article
  10. Interferon-induced human MxA GTPase blocks nuclear import of Thogoto virus nucleocapsids.Proceedings of the National Academy of Sciences of the United States of America · 1999
    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

6 authors at 1 institution in 1 country.

L JohannesLaboratory of Developmental Neurogenetics, National Institute of Neurological Disorders and Stroke, Bethesda, Maryland 20892, USA.
R Kambadur
H Lee-Hellmich
C A Hodgkinson
H Arnheiter
E Meier
National Institute of Neurological Disorders and Stroke · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Rat Mx2 and rat Mx3 are two alpha/beta interferon-inducible cytoplasmic GTPases that differ in three residues in the amino-terminal third, which also contains the tripartite GTP-binding domain, and that differ in five residues in the carboxy-terminal quarter, which also contains a dimerization domain. While Mx2 is active against vesicular stomatitis virus (VSV), Mx3 lacks antiviral activity. We mapped the functional difference between Mx2 and Mx3 protein to two critical residues in the carboxy-terminal parts of the molecules. An exchange of either residue 588 or 630 of Mx2 with the corresponding residues of Mx3 abolished anti-VSV activity, and the introduction of the two Mx2 residues on an Mx3 background partially restored anti-VSV activity. These results are consistent with the facts that Mx2 and Mx3 have similar intrinsic GTPase activities and that the GTPase domain of Mx3 can fully substitute for the GTPase domain of Mx2. Nevertheless, the amino-terminal third containing the GTP-binding domain is necessary for antiviral activity, since an amino-terminally truncated Mx2 protein is devoid of anti-VSV activity. Furthermore, Fab fragments of a monoclonal antibody known to neutralize antiviral activity block GTPase activity by binding an epitope in the carboxy-terminal half of Mx2 or Mx3 protein. The results are consistent with a two-domain model in which both the conserved amino-terminal half and the less-well-conserved carboxy-terminal half of Mx proteins carry functionally important domains.

Indexed as

GTP-Binding Proteins3T3 CellsAnimalsAntiviral AgentsEpitopesGTP PhosphohydrolasesMiceMyxovirus Resistance ProteinsProteinsRatsRecombinant Fusion ProteinsVesicular stomatitis Indiana virusAntiviral AgentsEpitopesGTP-Binding ProteinsGTP PhosphohydrolasesMx1 protein, mouseMx2 protein, mouseMx2 protein, ratMyxovirus Resistance ProteinsProteinsRecombinant Fusion Proteins

Identifiers

PMID9371647
PMCPMC230291
OpenAlexW2118972963

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.