Evidence map›Paper›PMID 20227373›Full record

ArticleMolecular cell2010

Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins.

Neil M Kad, Hong Wang, Guy G Kennedy, David M Warshaw, Bennett Van Houten

Abstract read
In one paragraph

Article in Molecular cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
–field-weighted citation impact
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

100 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

40 more citing papers are in PubMed but not listed here.

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.

Neil M KadDepartment of Biological Sciences, University of Essex, Colchester, Essex CO4 3SQ, UK. nkad@essex.ac.uk
Hong Wang
Guy G Kennedy
David M Warshaw
Bennett Van Houten

Funding

Ventricular and Cardiac Fiber Characterization and Integration CoreP01HL059408 · NHLBI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI PALMER, BRADLEY M · 1999 to 2014
$26.4M
Smooth Muscle Myosin: Molecular Mechanics and Intramolecular CommunicationR01HL085489 · NHLBI · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI WARSHAW, DAVID M · 2006 to 2009
$1.5M
DNA damage induced structural and dynamic changes at telomeresR00ES016758 · NIEHS · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI WANG, HONG · 2012 to 2014
$733k
DNA damage induced structural and dynamic changes at telomeresK99ES016758 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI WANG, HONG · 2009 to 2010
$165k
Intramural NIH HHSNHLBI NIH HHS HL059408NHLBI NIH HHS HL085489NHLBI NIH HHS P01 HL059408NHLBI NIH HHS R01 HL085489NIEHS NIH HHS K99 ES016758NIEHS NIH HHS K99ES016758-01NIEHS NIH HHS R00 ES016758
6 · The paper itself

Abstract

How DNA repair proteins sort through a genome for damage is one of the fundamental unanswered questions in this field. To address this problem, we uniquely labeled bacterial UvrA and UvrB with differently colored quantum dots and visualized how they interacted with DNA individually or together using oblique-angle fluorescence microscopy. UvrA was observed to utilize a three-dimensional search mechanism, binding transiently to the DNA for short periods (7 s). UvrA also was observed jumping from one DNA molecule to another over approximately 1 microm distances. Two UvrBs can bind to a UvrA dimer and collapse the search dimensionality of UvrA from three to one dimension by inducing a substantial number of UvrAB complexes to slide along the DNA. Three types of sliding motion were characterized: random diffusion, paused motion, and directed motion. This UvrB-induced change in mode of searching permits more rapid and efficient scanning of the genome for damage.

Indexed as

DNA RepairMicroscopy, Atomic ForceMicroscopy, FluorescenceQuantum DotsAdenosine TriphosphatasesAdenosine TriphosphateBinding SitesDNADNA-Binding ProteinsDNA HelicasesElectrophoretic Mobility Shift AssayEscherichia coli ProteinsKineticsModels, MolecularNucleic Acid ConformationProtein BindingAdenosine TriphosphatasesAdenosine TriphosphateDNADNA-Binding ProteinsDNA HelicasesEscherichia coli ProteinsUvrA protein, E coliUvrB protein, E coli

Identifiers

PMID20227373
PMCPMC3986923

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.