Evidence map›Paper›PMID 31383358›Full record

ArticleBiophysical journal2019

Identification of Multiple Kinetic Populations of DNA-Binding Proteins in Live Cells.

Han N Ho, Daniel Zalami, Jürgen Köhler, Antoine M van Oijen, Harshad Ghodke

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Replication stalling activates SSB for recruitment of DNA damage tolerance factors.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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 at 3 institutions in 2 countries.

Han N HoMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, Australia; Illawarra Health and Medical Research Institute, Wollongong, Australia.
Daniel ZalamiSpectroscopy of Soft Matter, University of Bayreuth, Bayreuth, Germany.
Jürgen KöhlerSpectroscopy of Soft Matter, University of Bayreuth, Bayreuth, Germany; Bavarian Polymer Institute, Bayreuth, Germany; Bayreuth Institute of Macromolecular Research, University of Bayreuth, Bayreuth, Germany.
Antoine M van OijenMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, Australia; Illawarra Health and Medical Research Institute, Wollongong, Australia. Electronic address: vanoijen@uow.edu.au.
Harshad GhodkeMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, Wollongong, Australia; Illawarra Health and Medical Research Institute, Wollongong, Australia. Electronic address: harshad@uow.edu.au.
University of Wollongong · AUBavarian Polymer Institute · DEUniversity of Bayreuth · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding how multiprotein complexes function in cells requires detailed quantitative understanding of their association and dissociation kinetics. Analysis of the heterogeneity of binding lifetimes enables the interrogation of the various intermediate states formed during the reaction. Single-molecule fluorescence imaging permits the measurement of reaction kinetics inside living organisms with minimal perturbation. However, poor photophysical properties of fluorescent probes limit the dynamic range and accuracy of measurements of off rates in live cells. Time-lapse single-molecule fluorescence imaging can partially overcome the limits of photobleaching; however, limitations of this technique remain uncharacterized. Here, we present a structured analysis of which timescales are most accessible using the time-lapse imaging approach and explore uncertainties in determining kinetic subpopulations. We demonstrate the effect of shot noise on the precision of the measurements as well as the resolution and dynamic range limits that are inherent to the method. Our work provides a convenient implementation to determine theoretical errors from measurements and to support interpretation of experimental data.

Indexed as

Cell SurvivalDNA-Binding ProteinsEscherichia coliKineticsPhotobleachingProtein BindingDNA-Binding Proteins

Identifiers

PMID31383358
PMCPMC6731377
OpenAlexW2964087535

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.