Evidence map›Paper›PMID 25826642›Full record

ArticleAngewandte Chemie (International ed. in English)2015

Distance Measurement on an Endogenous Membrane Transporter in E. coli Cells and Native Membranes Using EPR Spectroscopy.

Benesh Joseph, Arthur Sikora, Enrica Bordignon, Gunnar Jeschke, David S Cafiso, Thomas F Prisner

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
12.9field-weighted citation impact, top 2% 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

41 citing papers in PubMed, 103 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  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. Article
  8. Article
  9. Article
  10. Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex inAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  11. Review
  12. GdJournal of the American Chemical Society · 2023
    Article
  13. Pulse dipolar EPR for determining nanomolar binding affinities.Chemical communications (Cambridge, England) · 2022
    Article
  14. Article
  15. Chemical communications (Cambridge, England) · 2021
    Article
  16. Article
  17. Article
  18. Nanomolar Pulse Dipolar EPR Spectroscopy in Proteins: CuThe journal of physical chemistry. B · 2021
    Article
  19. Article
  20. Orientation and dynamics of CuPhysical chemistry chemical physics : PCCP · 2020
    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

6 authors at 4 institutions in 3 countries.

Benesh JosephInstitut für physikalische und theoretische Chemie und Biomolekulares Magnetresonanz Zentrum, Universität Frankfurt, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main (Germany) http://www.prisner.de.
Arthur SikoraDepartment of Chemistry, University of Virginia, McCormick Road, Charlottesville VA22904-4319 (USA).
Enrica BordignonDepartment of Physics, Free University of Berlin, Arnimallee 14, 14195 Berlin (Germany).
Gunnar JeschkeLaboratory for Physical Chemistry, ETH Zurich, Vladimir-Prelog-Weg 2, 8093 Zürich (Switzerland).
David S CafisoDepartment of Chemistry, University of Virginia, McCormick Road, Charlottesville VA22904-4319 (USA). cafiso@virginia.edu.
Thomas F PrisnerInstitut für physikalische und theoretische Chemie und Biomolekulares Magnetresonanz Zentrum, Universität Frankfurt, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main (Germany) http://www.prisner.de. prisner@prisner.de.
ETH Zurich · CHFreie Universität Berlin · DEGoethe University Frankfurt · DEUniversity of Virginia · US

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

Membrane proteins may be influenced by the environment, and they may be unstable in detergents or fail to crystallize. As a result, approaches to characterize structures in a native environment are highly desirable. Here, we report a novel general strategy for precise distance measurements on outer membrane proteins in whole Escherichia coli cells and isolated outer membranes. The cobalamin transporter BtuB was overexpressed and spin-labeled in whole cells and outer membranes and interspin distances were measured to a spin-labeled cobalamin using pulse EPR spectroscopy. A comparative analysis of the data reveals a similar interspin distance between whole cells, outer membranes, and synthetic vesicles. This approach provides an elegant way to study conformational changes or protein-protein/ligand interactions at surface-exposed sites of membrane protein complexes in whole cells and native membranes, and provides a method to validate outer membrane protein structures in their native environment.

Indexed as

Electron Spin Resonance SpectroscopyBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularBacterial Outer Membrane ProteinsBtuB protein, E coliEscherichia coli ProteinsMembrane Transport ProteinsEPR spectroscopyin-cell spectroscopymembrane proteinsspin labelingvitamin B12 transporter

Identifiers

PMID25826642
PMCPMC4426067
OpenAlexW2157382945

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.