Evidence map›Paper›PMID 25752954›Full record

ArticleArchives of biochemistry and biophysics2015

The conserved core enzymatic activities and the distinct dynamics of polyomavirus large T antigens.

Ping An, Jeffrey L Brodsky, James M Pipas

Open access · greenAbstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.7field-weighted citation impact, top 27% 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

9 citing papers in PubMed, 13 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Viruses in colorectal cancer.Molecular oncology · 2022
    Review
  5. Article
  6. Article
  7. The Biology and Clinical Features of Cutaneous Polyomaviruses.The Journal of investigative dermatology · 2019
    Review
  8. Review
  9. 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

3 authors at 1 institution in 1 country.

Ping AnDepartment of Biological Sciences, University of Pittsburgh, 4249 Fifth Avenue, Pittsburgh, PA 15260, USA.
Jeffrey L BrodskyDepartment of Biological Sciences, University of Pittsburgh, 4249 Fifth Avenue, Pittsburgh, PA 15260, USA.
James M PipasDepartment of Biological Sciences, University of Pittsburgh, 4249 Fifth Avenue, Pittsburgh, PA 15260, USA. Electronic address: pipas@pitt.edu.
University of Pittsburgh · US

Funding

University of Pittsburgh Clinical and Translational Science InstituteUL1TR000005 · NCATS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI REIS, STEVEN E · 2012 to 2015
$50.8M
Single Nephron and MetabolomicsP30DK079307 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2008 to 2022
$13.4M
ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
Regulation of Transcription and Translation by Human PolyomavirusesR21AI109339 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI PIPAS, JAMES M · 2014 to 2015
$404k
NCATS NIH HHS UL1 TR000005NIAID NIH HHS R21 AI109339NIDDK NIH HHS DK79307NIDDK NIH HHS P30 DK079307NIGMS NIH HHS GM75061NIGMS NIH HHS R01 GM075061
6 · The paper itself

Abstract

Several human polyomaviruses including JCV, BKV and TSV are associated with diseases, particularly in immunosuppressed patients. While the large T antigen (LT) encoded by the monkey polyomavirus SV40 is well studied, and possesses intrinsic ATPase and DNA helicase activities, the LTs of the human polyomaviruses are relatively uncharacterized. In order to evaluate whether these enzymatic activities, which are required for viral DNA replication, are conserved between polyomaviruses, we performed a comparative study using the LTs from JCV, TSV and SV40. The ATPase and DNA helicase activities and the interaction with the cellular tumor suppressor p53 were assayed for the purified Zn-ATPase domains of the three LTs. We found that all Zn-ATPases were active ATPases. The Zn-ATPase domains also functioned as DNA helicases, although the measured kinetic constants differed among the three proteins. In addition, when tested against four small molecule ATPase inhibitors, the Zn-ATPase domains of TSV was more resistant than that of SV40 and JCV. Our results show that, while LTs from JCV and TSV share the core ATPase and DNA helicase activities, they possess important functional differences that might translate into their respective abilities to infect and replicate in hosts.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAntigens, Viral, TumorDNA HelicasesJC VirusModels, MolecularMolecular Sequence DataPolyomavirusProtein Structure, TertiarySimian virus 40Adenosine TriphosphatasesAntigens, Viral, TumorDNA HelicasesATPaseDNA helicasep53PolyomavirusProtein–protein interaction

Identifiers

PMID25752954
PMCPMC4865250
OpenAlexW2038714566

What OpenQuestion holds

Textmetadata
LicenceTDM
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.