Evidence map›Paper›PMID 25204359›Full record

ArticleNano letters2014

Direct correlation of DNA binding and single protein domain motion via dual illumination fluorescence microscopy.

Mohamed Ghoneim, Maria Spies

Abstract read
In one paragraph

Article in Nano letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
7.1field-weighted citation impact, top 3% 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

22 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
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  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Formation and Recognition of UV-Induced DNA Damage within Genome Complexity.International journal of molecular sciences · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Single-molecule sorting of DNA helicases.Methods (San Diego, Calif.) · 2016
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

2 authors at 2 institutions in 1 country.

Mohamed GhoneimCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
Maria Spies
University of Illinois Urbana-Champaign · USUniversity of Iowa · US

Funding

Human DNA Replication Machines: Structure-Function of Polymerase Alpha-PrimaseR01GM101167 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI TAHIROV, TAHIR H · 2013 to 2017
$1.9M
Regulation of unwinding and remodeling activities in FeS-DNA helicasesR01GM108617 · NIGMS · UNIVERSITY OF IOWA · PI SPIES, MARIA · 2014 to 2018
$1.6M
Howard Hughes Medical InstituteNIGMS NIH HHS 1R01 GM108617NIGMS NIH HHS R01 GM101167NIGMS NIH HHS R01 GM108617
6 · The paper itself

Abstract

We report a dual illumination, single-molecule imaging strategy to dissect directly and in real-time the correlation between nanometer-scale domain motion of a DNA repair protein and its interaction with individual DNA substrates. The strategy was applied to XPD, an FeS cluster-containing DNA repair helicase. Conformational dynamics was assessed via FeS-mediated quenching of a fluorophore site-specifically incorporated into XPD. Simultaneously, binding of DNA molecules labeled with a spectrally distinct fluorophore was detected by colocalization of the DNA- and protein-derived signals. We show that XPD undergoes thermally driven conformational transitions that manifest in spatial separation of its two auxiliary domains. DNA binding does not strictly enforce a specific conformation. Interaction with a cognate DNA damage, however, stabilizes the compact conformation of XPD by increasing the weighted average lifetime of this state by 140% relative to an undamaged DNA. Our imaging strategy will be a valuable tool to study other FeS-containing nucleic acid processing enzymes.

Indexed as

ArchaeaArchaeal ProteinsBinding SitesDNA, ArchaealDNA HelicasesDNA RepairEquipment DesignMicroscopy, FluorescenceProtein BindingProtein Structure, TertiaryArchaeal ProteinsDNA, ArchaealDNA HelicasesDNA damage recognitionDNA repairmulticolor single-molecule detectionprotein domain motiontotal-internal reflection fluorescence microscopyXPD helicase

Identifiers

PMID25204359
PMCPMC4189620
OpenAlexW2316750555

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.