Evidence map›Paper›PMID 36982314›Full record

ArticleInternational journal of molecular sciences2023

Unfolding Individual Domains of BmrA, a Bacterial ABC Transporter Involved in Multidrug Resistance.

Kristin Oepen, Veronika Mater, Dirk Schneider

Open access · goldFull text read
In one paragraph

Article in International journal of molecular sciences, 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
1.2field-weighted citation impact, top 19% 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, 5 citations in OpenAlex.

  1. The Antidepressant Drug Clomipramine Inhibits the ABC Transporter BmrA.Chembiochem : a European journal of chemical biology · 2026
    Article
  2. Article
  3. 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 1 institution in 1 country.

Kristin OepenDepartment of Chemistry-Biochemistry, Johannes Gutenberg University Mainz, Hanns-Dieter-Hüsch-Weg 17, 55128 Mainz, Germany.
Veronika MaterDepartment of Chemistry-Biochemistry, Johannes Gutenberg University Mainz, Hanns-Dieter-Hüsch-Weg 17, 55128 Mainz, Germany.
Dirk SchneiderDepartment of Chemistry-Biochemistry, Johannes Gutenberg University Mainz, Hanns-Dieter-Hüsch-Weg 17, 55128 Mainz, Germany.ORCID 0000-0003-4517-6387
Johannes Gutenberg University Mainz · DE

Funding

DynaMem (State of Rhineland-Palatinate) N/A
6 · The paper itself

Abstract

The folding and stability of proteins are often studied via unfolding (and refolding) a protein with urea. Yet, in the case of membrane integral protein domains, which are shielded by a membrane or a membrane mimetic, urea generally does not induce unfolding. However, the unfolding of α-helical membrane proteins may be induced by the addition of sodium dodecyl sulfate (SDS). When protein unfolding is followed via monitoring changes in Trp fluorescence characteristics, the contributions of individual Trp residues often cannot be disentangled, and, consequently, the folding and stability of the individual domains of a multi-domain membrane protein cannot be studied. In this study, the unfolding of the homodimeric bacterial ATP-binding cassette (ABC) transporter

Indexed as

ATP-Binding Cassette TransportersBacillusDrug Resistance, Multiple, BacterialProtein UnfoldingAdenosine TriphosphateProtein FoldingUreaAdenosine TriphosphateATP-Binding Cassette TransportersUreaABC transporterBmrAmembrane proteinmulti-domain proteinprotein foldingprotein stabilityTrp fluorescence spectroscopy

Identifiers

PMID36982314
PMCPMC10049088
OpenAlexW4323664115

What OpenQuestion holds

Textfull text, public
LicenceCC BY
measurements read44
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.