Evidence map›Paper›PMID 26795032›Full record

ArticleJournal of the American Chemical Society2016

Ligand Induced Conformational Changes of a Membrane Transporter in E. coli Cells Observed with DEER/PELDOR.

Benesh Joseph, Arthur Sikora, David S Cafiso

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
14.6field-weighted citation impact, top 1% 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

38 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Article
  3. Rapid Analysis of DEER Signals Including Short Distances.The journal of physical chemistry letters · 2025
    Article
  4. Endogenous Cu(II) Labeling for Distance Measurements on Proteins by EPR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  5. Article
  6. Article
  7. Modeling of Cu(II)-based protein spin labels using rotamer libraries.Physical chemistry chemical physics : PCCP · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Cucurbit[7]uril Enhances Distance Measurements of Spin-Labeled Proteins.Journal of the American Chemical Society · 2023
    Article
  12. iScience · 2023
    Article
  13. Article
  14. Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Chemical communications (Cambridge, England) · 2021
    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

3 authors at 2 institutions in 2 countries.

Benesh JosephInstitute of Physical and Theoretical Chemistry and Center for Biomolecular Magnetic Resonance, University of Frankfurt , Max-von-Laue-Strasse 7, 60438 Frankfurt am Main, Germany.
Arthur SikoraDepartment of Chemistry and Center for Membrane Biology, University of Virginia , McCormick Road, Charlottesville, Virginia 22904-4319, United States.
David S CafisoDepartment of Chemistry and Center for Membrane Biology, University of Virginia , McCormick Road, Charlottesville, Virginia 22904-4319, United States.
University of Virginia · USGoethe University Frankfurt · DE

Funding

MOLECULAR MECHANISMS OF MEMBRANE TRANSPORTR01GM035215 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI DAVID S CAFISO · 1985 to 2026
$7.3M
NIGMS NIH HHS GM035215NIGMS NIH HHS R01 GM035215
6 · The paper itself

Abstract

An unrealized goal in structural biology is the determination of structure and conformational change at high resolution for membrane proteins within the cellular environment. Pulsed electron-electron double resonance (PELDOR) is a well-established technique to follow conformational changes in purified membrane protein complexes. Here we demonstrate the first proof of concept for the use of PELDOR to observe conformational changes in a membrane protein in intact cells. We exploit the fact that outer membrane proteins usually lack reactive cysteines and that paramagnetic spin labels entering the periplasm are selectively reduced to achieve specific labeling of the cobalamin transporter BtuB in Escherichia coli. We characterize conformational changes in the second extracellular loop of BtuB upon ligand binding and compare the PELDOR data with high-resolution crystal structures. Our approach avoids detergent extraction, purification, and reconstitution usually required for these systems. With this approach, structure, function, conformational changes, and molecular interactions of outer membrane proteins can be studied at high resolution in the cellular environment.

Indexed as

Electron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsLigandsMembrane Transport ProteinsProtein ConformationEscherichia coli ProteinsLigandsMembrane Transport Proteins

Identifiers

PMID26795032
PMCPMC4837646
OpenAlexW2262846858

What OpenQuestion holds

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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.