Evidence map›Paper›PMID 38515502›Full record

ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2023

Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in

Samuel F Haysom, Jonathan Machin, James M Whitehouse, Jim E Horne, Katherine Fenn, Yue Ma, Hassane El Mkami, Nils Böhringer, Till F Schäberle, Neil A Ranson and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.1field-weighted citation impact, top 16% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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

12 authors at 3 institutions in 2 countries.

Samuel F HaysomAstbury Centre for Structural Molecular Biology School of Molecular and Cellular Biology University of Leeds Leeds LS2 9JT UK.
Jonathan MachinAstbury Centre for Structural Molecular Biology School of Molecular and Cellular Biology University of Leeds Leeds LS2 9JT UK.
James M WhitehouseAstbury Centre for Structural Molecular Biology School of Molecular and Cellular Biology University of Leeds Leeds LS2 9JT UK.
Jim E HorneAstbury Centre for Structural Molecular Biology School of Molecular and Cellular Biology University of Leeds Leeds LS2 9JT UK.
Katherine FennAstbury Centre for Structural Molecular Biology School of Molecular and Cellular Biology University of Leeds Leeds LS2 9JT UK.
Yue MaAstbury Centre for Structural Molecular Biology School of Biomedical Sciences University of Leeds Leeds LS2 9JT UK.
Hassane El MkamiSchool of Physics and Astronomy University of St. Andrews St. Andrews KY16 9SS UK.
Nils BöhringerInstitute for Insect Biotechnology Natural Product Research Justus-Liebig-University Giessen Ohlebergsweg 12 35392 Giessen Germany.
Till F SchäberleInstitute for Insect Biotechnology Natural Product Research Justus-Liebig-University Giessen Ohlebergsweg 12 35392 Giessen Germany.
Neil A RansonAstbury Centre for Structural Molecular Biology School of Molecular and Cellular Biology University of Leeds Leeds LS2 9JT UK.
Sheena E RadfordAstbury Centre for Structural Molecular Biology School of Molecular and Cellular Biology University of Leeds Leeds LS2 9JT UK.ORCID 0000-0002-3079-8039
Christos PliotasAstbury Centre for Structural Molecular Biology School of Biomedical Sciences University of Leeds Leeds LS2 9JT UK.ORCID 0000-0002-4309-4858
University of Leeds · GBJustus-Liebig-Universität Gießen · DEUniversity of St Andrews · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

The β-barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram-negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane (OM). Here, we use Pulsed Electron-Electron Double Resonance (PELDOR, or DEER) spectroscopy distance measurements to interrogate the conformational ensemble of the BAM complex in

Indexed as

BAMCryoemDarobactinIn-Cell EPRPELDOR

Identifiers

PMID38515502
PMCPMC10952338
OpenAlexW4376141439

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.