Evidence map›Paper›PMID 27793283›Full record

ArticleMethods in enzymology2016

Single-Molecule FRET to Measure Conformational Dynamics of DNA Mismatch Repair Proteins.

J W Gauer, S LeBlanc, P Hao, R Qiu, B C Case, M Sakato, M M Hingorani, D A Erie, K R Weninger

Abstract read
In one paragraph

Article in Methods in enzymology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing 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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Recurrent mismatch binding by MutS mobile clamps on DNA localizes repair complexes nearby.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Live-Cell FRET Imaging of Phosphorylation-Dependent Caveolin-1 Switch.Methods in molecular biology (Clifton, N.J.) · 2020
    Article
  13. Homologous Recombination under the Single-Molecule Fluorescence Microscope.International journal of molecular sciences · 2019
    Review
  14. Combining TIR and FRET in Molecular Test Systems.International journal of molecular sciences · 2019
    Article
  15. Article
  16. 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

9 authors.

J W GauerUniversity of North Carolina at Chapel Hill, Chapel Hill, NC, United States.
S LeBlancUniversity of North Carolina at Chapel Hill, Chapel Hill, NC, United States.
P HaoNorth Carolina State University, Raleigh, NC, United States.
R QiuNorth Carolina State University, Raleigh, NC, United States.
B C CaseWesleyan University, Middletown, CT, United States.
M SakatoWesleyan University, Middletown, CT, United States.
M M HingoraniWesleyan University, Middletown, CT, United States.
D A ErieUniversity of North Carolina at Chapel Hill, Chapel Hill, NC, United States. Electronic address: derie@email.unc.edu.
K R WeningerNorth Carolina State University, Raleigh, NC, United States. Electronic address: krwening@ncsu.edu.

Funding

Structure Function Studies of DNA Mismatch RepairR01GM079480 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ERIE, DOROTHY A · 2007 to 2017
$2.7M
Quantitative analysis of transient DNA repair processes in vivoR01GM109832 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BRUSTAD, ERIC MICHAEL, ERIE, DOROTHY A · 2014 to 2017
$1.0M
Mechanistic studies of DNA repair and damage responseR01GM080294 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ERIE, DOROTHY A · 2009 to 2010
$565k
Investigation of defective allosteric signaling as a basis for DNA mismatch repair malfunction in Lynch cancer syndromeR15GM114743 · NIGMS · WESLEYAN UNIVERSITY · PI HINGORANI, MANJU M · 2015 to 2015
$409k
NIGMS NIH HHS R01 GM079480NIGMS NIH HHS R01 GM080294NIGMS NIH HHS R01 GM109832NIGMS NIH HHS R15 GM114743
6 · The paper itself

Abstract

Single-molecule FRET measurements have a unique sensitivity to protein conformational dynamics. The FRET signals can either be interpreted quantitatively to provide estimates of absolute distance in a molecule configuration or can be qualitatively interpreted as distinct states, from which quantitative kinetic schemes for conformational transitions can be deduced. Here we describe methods utilizing single-molecule FRET to reveal the conformational dynamics of the proteins responsible for DNA mismatch repair. Experimental details about the proteins, DNA substrates, fluorescent labeling, and data analysis are included. The complementarity of single molecule and ensemble kinetic methods is discussed as well.

Indexed as

DNADNA Mismatch RepairFluorescence Resonance Energy TransferNucleic Acid ConformationProtein ConformationProteinsSingle Molecule ImagingDNAProteinsATPaseDNA mismatch repairEnzyme kineticsFRETSingle-molecule fluorescencesmFRETTIRF microscopyTransient kinetics

Identifiers

PMID27793283
PMCPMC5423442

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Registered trials

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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.