Evidence map›Paper›PMID 18400864›Full record

ArticleJournal of virology2008

Systematic study of the functions for the residues around the nucleotide pocket in simian virus 40 AAA+ hexameric helicase.

William B Greenleaf, Jingping Shen, Dahai Gai, Xiaojiang S Chen

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Molecular switch-like regulation enables global subunit coordination in a viral ring ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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  8. Review
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  12. Insights into the MCM functional mechanism: lessons learned from the archaeal MCM complex.Critical reviews in biochemistry and molecular biology · 2010
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Simulating the electrostatic guidance of the vectorial translocations in hexameric helicases and translocases.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  18. 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

4 authors at 2 institutions in 1 country.

William B GreenleafDepartment of Molecular and Computational Biology, University of Southern California, Los Angeles, California 90089-1340, USA.
Jingping Shen
Dahai Gai
Xiaojiang S Chen
University of Southern California · USUniversity of Colorado Denver · US

Funding

SV40 T Antigen Structure and Helicase MechanismsR01AI055926 · NIAID · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, XIAOJIANG S · 2004 to 2013
$4.0M
VIRAL AND CHEMICAL CARCINOGENESIST32CA009320 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI JONES, PETER A · 1985 to 2012
$2.5M
NCI NIH HHS 5T32CA009320-22NCI NIH HHS T32 CA009320NIAID NIH HHS R01 AI055926NIAID NIH HHS R01AI055926
6 · The paper itself

Abstract

The high-resolution structural data for simian virus 40 large-T-antigen helicase revealed a set of nine residues bound to ATP/ADP directly or indirectly. The functional role of each of these residues in ATP hydrolysis and also the helicase function of this AAA+ (ATPases associated with various cellular activities) molecular motor are unclear. Here, we report our mutational analysis of each of these residues to examine their functionality in oligomerization, DNA binding, ATP hydrolysis, and double-stranded DNA (dsDNA) unwinding. All mutants were capable of oligomerization in the presence of ATP and could bind single-stranded DNA and dsDNA. ATP hydrolysis was substantially reduced for proteins with mutations of residues making direct contact with the gamma-phosphate of ATP or the apical water molecule. A potentially noncanonical "arginine finger" residue, K418, is critical for ATP hydrolysis and helicase function, suggesting a new type of arginine finger role by a lysine in the stabilization of the transition state during ATP hydrolysis. Interestingly, our mutational data suggest that the positive- and negative-charge interactions in the uniquely observed residue pairs, R498/D499 and R540/D502, in large-T-antigen helicase are critically involved in the transfer of energy of ATP binding/hydrolysis to DNA unwinding.

Indexed as

Models, MolecularAdenosine TriphosphatasesAlanineAmino Acid SubstitutionAntigens, Viral, TumorDNA HelicasesDNA, Single-StrandedHydrolysisKineticsMutagenesis, Site-DirectedNucleotidesPhosphorus RadioisotopesProtein Structure, TertiarySimian virus 40Adenosine TriphosphatasesAlanineAntigens, Viral, TumorDNA HelicasesDNA, Single-StrandedNucleotidesPhosphorus Radioisotopes

Identifiers

PMID18400864
PMCPMC2395154
OpenAlexW2164021415

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.