Evidence map›Paper›PMID 22700977›Full record

ArticleThe Journal of biological chemistry2012

Structural basis for the interaction of a hexameric replicative helicase with the regulatory subunit of human DNA polymerase α-primase.

Bo Zhou, Diana R Arnett, Xian Yu, Aaron Brewster, Gregory A Sowd, Charlies L Xie, Stefan Vila, Dahai Gai, Ellen Fanning, Xiaojiang S Chen

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.1field-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

31 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. SV40 T-antigen uses a DNA shearing mechanism to initiate origin unwinding.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. The Biology and Clinical Features of Cutaneous Polyomaviruses.The Journal of investigative dermatology · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  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

10 authors at 3 institutions in 1 country.

Bo ZhouDepartment of Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089, USA.
Diana R Arnett
Xian Yu
Aaron Brewster
Gregory A Sowd
Charlies L Xie
Stefan Vila
Dahai Gai
Ellen Fanning
Xiaojiang S Chen
University of Southern California · USVanderbilt University · USVanderbilt-Ingram Cancer Center

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI STACIE B DUSETZINA · 1995 to 2026
$172.8M
CONTROL OF SIMIAN VIRUS 40 AND CELLULAR DNA REPLICATIONR01GM052948 · NIGMS · VANDERBILT UNIVERSITY · PI FRIEDMAN, KATHERINE LOUISE · 1995 to 2013
$6.1M
SV40 T Antigen Structure and Helicase MechanismsR01AI055926 · NIAID · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, XIAOJIANG S · 2004 to 2013
$4.0M
Structural Studies of MCM ComplexR01GM080338 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, XIAOJIANG S · 2009 to 2012
$1.4M
Virology Training ProgramT32AI089554 · NIAID · VANDERBILT UNIVERSITY · PI CROWE, JAMES E · 2010 to 2014
$816k
NCI NIH HHS P30 CA068485NIAID NIH HHS AI055926NIAID NIH HHS R01 AI055926NIAID NIH HHS T32-AI089554NIGMS NIH HHS GM080338NIGMS NIH HHS GM52948NIGMS NIH HHS R01 GM052948NIGMS NIH HHS R01 GM080338
6 · The paper itself

Abstract

DNA polymerase α-primase (Pol-prim) plays an essential role in eukaryotic DNA replication, initiating synthesis of the leading strand and of each Okazaki fragment on the lagging strand. Pol-prim is composed of a primase heterodimer that synthesizes an RNA primer, a DNA polymerase subunit that extends the primer, and a regulatory B-subunit (p68) without apparent enzymatic activity. Pol-prim is thought to interact with eukaryotic replicative helicases, forming a dynamic multiprotein assembly that displays primosome activity. At least three subunits of Pol-prim interact physically with the hexameric replicative helicase SV40 large T antigen, constituting a simple primosome that is active in vitro. However, structural understanding of these interactions and their role in viral chromatin replication in vivo remains incomplete. Here, we report the detailed large T antigen-p68 interface, as revealed in a co-crystal structure and validated by site-directed mutagenesis, and we demonstrate its functional importance in activating the SV40 primosome in cell-free reactions with purified Pol-prim, as well as in monkey cells in vivo.

Indexed as

Base SequenceBlotting, SouthernDNA Polymerase IDNA PrimaseDNA PrimersDNA ReplicationHumansModels, MolecularMolecular Sequence DataSimian virus 40DNA polymerase alpha-primaseDNA Polymerase IDNA PrimaseDNA Primers

Identifiers

PMID22700977
PMCPMC3411022
OpenAlexW2017551066

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.