Evidence map›Paper›PMID 11932388›Full record

ArticleJournal of virology2002

Ty1 defect in proteolysis at high temperature.

Joseph F Lawler, Daniel P Haeusser, Angie Dull, Jef D Boeke, Jill B Keeney

Abstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-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

25 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
  2. Article
  3. Elimination of virus-like particles reduces protein aggregation and extends replicative lifespan inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Active transposition in genomes.Annual review of genetics · 2012
    Review
  19. Retrotransposition is associated with genome instability during chronological aging.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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.

Joseph F LawlerDepartment of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Daniel P Haeusser
Angie Dull
Jef D Boeke
Jill B Keeney
Juniata College · USJohns Hopkins Medicine · US

Funding

TRANSPOSITION MECHANISMSR01GM036481 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 1986 to 2011
$5.6M
NOVEL HOST GENES AFFECTING TRANSPOSITIONR15GM054291 · NIGMS · JUNIATA COLLEGE · PI KEENEY, JILL B · 1996 to 1998
–
NIGMS NIH HHS GM36481NIGMS NIH HHS GM54291-02NIGMS NIH HHS R01 GM036481
6 · The paper itself

Abstract

Retrotransposition of the Ty1 element of Saccharomyces cerevisiae is temperature sensitive. Transposition activity of Ty1 is abolished at temperatures above 34 degrees C. In this report, we show that the major block to transposition at high temperature is the inhibition of processing of the Gag-Pol-p199 polyprotein and the concomitant reduction of reverse transcriptase (RT) activity. Expression of a Ty1 protease construct in Escherichia coli shows that protease enzymatic activity is inherently temperature sensitive. In yeast, Gag processing is only partially inhibited at high temperature, while cleavage of the Gag-Pol polyprotein is completely inhibited. Sites of proteolytic processing are differentially susceptible to cleavage during growth at high temperature. Overall levels of the Gag-Pol polyprotein are reduced at high temperature, although the efficiency of the requisite +1 frameshifting event appears to be increased. RT activity is inherently relatively temperature resistant, yet no cDNA is made at high temperature and the amount of RT activity is greatly reduced in virus-like particles formed at high temperature. Taken together, these results suggest that alterations in Ty1 proteins that occur at high temperature affect both protease activity and RT activity, such that Ty1 transposition is abolished.

Indexed as

Hot TemperatureDNA, ComplementaryEndopeptidasesFusion Proteins, gag-polPlasmidsRetroelementsRNA-Directed DNA PolymeraseRNA, MessengerSaccharomyces cerevisiaeVirionDNA, ComplementaryEndopeptidasesFusion Proteins, gag-polRetroelementsRNA-Directed DNA PolymeraseRNA, Messenger

Identifiers

PMID11932388
PMCPMC155059
OpenAlexW2007998870

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.