Evidence map›Paper›PMID 23891547›Full record

ArticleMethods (San Diego, Calif.)2014

Analyzing conformational dynamics of single P-glycoprotein transporters by Förster resonance energy transfer using hidden Markov models.

Nawid Zarrabi, Stefan Ernst, Brandy Verhalen, Stephan Wilkens, Michael Börsch

Abstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

12 citing papers in PubMed, 35 citations in OpenAlex.

  1. Gold Ion Beam Milled Gold Zero-Mode Waveguides.Nanomaterials (Basel, Switzerland) · 2022
    Article
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  11. Regulatory conformational changes of the ε subunit in single FRET-labeled FProceedings of SPIE--the International Society for Optical Engineering · 2014
    Article
  12. Towards monitoring conformational changes of the GPCR neurotensin receptor 1 by single-molecule FRET.Proceedings of SPIE--the International Society for Optical Engineering
    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

5 authors at 3 institutions in 2 countries.

Nawid ZarrabiSingle-Molecule Microscopy Group, Jena University Hospital, Friedrich Schiller University Jena, 07743 Jena, Germany; 3rd Institute of Physics, University of Stuttgart, 70550 Stuttgart, Germany.
Stefan ErnstSingle-Molecule Microscopy Group, Jena University Hospital, Friedrich Schiller University Jena, 07743 Jena, Germany.
Brandy VerhalenDepartment of Biochemistry & Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Stephan WilkensDepartment of Biochemistry & Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Michael BörschSingle-Molecule Microscopy Group, Jena University Hospital, Friedrich Schiller University Jena, 07743 Jena, Germany; 3rd Institute of Physics, University of Stuttgart, 70550 Stuttgart, Germany. Electronic address: michael.boersch@med.uni-jena.de.
SUNY Upstate Medical University · USUniversity of Stuttgart · DEJena University Hospital · DE

Funding

STRUCTURE OF THE VACUOLAR ATPASE BY ELECTRON MICROSCOPYR01GM058600 · NIGMS · UPSTATE MEDICAL UNIVERSITY · PI WILKENS, STEPHAN · 1999 to 2020
$4.8M
STRUCTURE OF P-GLYCOPROTEIN BY ELECTRON MICROSCOPYR01CA100246 · NCI · UPSTATE MEDICAL UNIVERSITY · PI WILKENS, STEPHAN · 2004 to 2008
$843k
NCI NIH HHS CA100246NCI NIH HHS R01 CA100246NIGMS NIH HHS GM058600NIGMS NIH HHS R01 GM058600
6 · The paper itself

Abstract

Single-molecule Förster resonance energy (smFRET) transfer has become a powerful tool for observing conformational dynamics of biological macromolecules. Analyzing smFRET time trajectories allows to identify the state transitions occuring on reaction pathways of molecular machines. Previously, we have developed a smFRET approach to monitor movements of the two nucleotide binding domains (NBDs) of P-glycoprotein (Pgp) during ATP hydrolysis driven drug transport in solution. One limitation of this initial work was that single-molecule photon bursts were analyzed by visual inspection with manual assignment of individual FRET levels. Here a fully automated analysis of Pgp smFRET data using hidden Markov models (HMM) for transitions up to 9 conformational states is applied. We propose new estimators for HMMs to integrate the information of fluctuating intensities in confocal smFRET measurements of freely diffusing lipid bilayer bound membrane proteins in solution. HMM analysis strongly supports that under conditions of steady state turnover, conformational states with short NBD distances and short dwell times are more populated compared to conditions without nucleotide or transport substrate present.

Indexed as

AlgorithmsAnimalsATP Binding Cassette Transporter, Subfamily BBiological TransportFluorescence Resonance Energy TransferHumansLiposomesMarkov ChainsMicroscopy, ConfocalModels, MolecularProtein ConformationSolutionsATP Binding Cassette Transporter, Subfamily BLiposomesSolutionsHidden Markov modelP-glycoproteinProtein dynamicsSingle-molecule FRET

Identifiers

PMID23891547
PMCPMC3900600
OpenAlexW2008037560

What OpenQuestion holds

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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.