Evidence map›Paper›PMID 22171253›Full record

ArticleJournal of virology2012

The G-patch domain of Mason-Pfizer monkey virus is a part of reverse transcriptase.

Ivana Křízová, Romana Hadravová, Jitka Štokrová, Jana Günterová, Michal Doležal, Tomáš Ruml, Michaela Rumlová, Iva Pichová

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.5field-weighted citation impact, top 43% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Protease-mediated maturation of M-PMV reverse transcriptase into a functional heterodimer.Protein science : a publication of the Protein Society · 2026
    Article
  2. Review
  3. Unveiling the DHX15-G-patch interplay in retroviral RNA packaging.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Journal of virology · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Regulation of DEAH/RHA helicases by G-patch proteins.BioMed research international · 2015
    Review
  14. Article
  15. 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

8 authors at 2 institutions in 1 country.

Ivana KřízováInstitute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, vvi, IOCB & Gilead Research Center, Prague, Czech Republic.
Romana Hadravová
Jitka Štokrová
Jana Günterová
Michal Doležal
Tomáš Ruml
Michaela Rumlová
Iva Pichová
Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry · CZUniversity of Chemistry and Technology, Prague · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mason-Pfizer monkey virus (M-PMV), like some other betaretroviruses, encodes a G-patch domain (GPD). This glycine-rich domain, which has been predicted to be an RNA binding module, is invariably localized at the 3' end of the pro gene upstream of the pro-pol ribosomal frameshift sequence of genomic RNAs of betaretroviruses. Following two ribosomal frameshift events and the translation of viral mRNA, the GPD is present in both Gag-Pro and Gag-Pro-Pol polyproteins. During the maturation of the Gag-Pro polyprotein, the GPD transiently remains a C-terminal part of the protease (PR), from which it is then detached by PR itself. The destiny of the Gag-Pro-Pol-encoded GPD remains to be determined. The function of the GPD in the retroviral life cycle is unknown. To elucidate the role of the GPD in the M-PMV replication cycle, alanine-scanning mutational analysis of its most highly conserved residues was performed. A series of individual mutations as well as the deletion of the entire GPD had no effect on M-PMV assembly, polyprotein processing, and RNA incorporation. However, a reduction of the reverse transcriptase (RT) activity, resulting in a drop in M-PMV infectivity, was determined for all GPD mutants. Immunoprecipitation experiments suggested that the GPD is a part of RT and participates in its function. These data indicate that the M-PMV GPD functions as a part of reverse transcriptase rather than protease.

Indexed as

AnimalsCell LineHumansMason-Pfizer monkey virusPolyproteinsProtein Structure, TertiaryRNA-Directed DNA PolymeraseViral ProteinsPolyproteinsRNA-Directed DNA PolymeraseViral Proteins

Identifiers

PMID22171253
PMCPMC3302395
OpenAlexW2032290993

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.