Evidence map›Paper›PMID 36523158›Full record

ArticleBiophysical journal2023

Length matters: Functional flip of the short TatA transmembrane helix.

Eva R Stockwald, Lena M E Steger, Stefanie Vollmer, Christina Gottselig, Stephan L Grage, Jochen Bürck, Sergii Afonin, Julia Fröbel, Anne-Sophie Blümmel, Julia Setzler and 3 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

7 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. The Evolution of Lipids from Solvents to Substrates.Annual review of biophysics · 2026
    Review
  3. Review
  4. The mechanism of Tat-dependent protein translocation.Microbial cell (Graz, Austria) · 2026
    Article
  5. Article
  6. Article
  7. Membranes in focus.Biophysical journal · 2023
    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

13 authors at 2 institutions in 1 country.

Eva R StockwaldKarlsruhe Institute of Technology (KIT), Institute of Organic Chemistry, Karlsruhe, Germany.
Lena M E StegerKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), Karlsruhe, Germany.
Stefanie VollmerKarlsruhe Institute of Technology (KIT), Institute of Organic Chemistry, Karlsruhe, Germany.
Christina GottseligKarlsruhe Institute of Technology (KIT), Institute of Organic Chemistry, Karlsruhe, Germany.
Stephan L GrageKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), Karlsruhe, Germany.
Jochen BürckKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), Karlsruhe, Germany.
Sergii AfoninKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), Karlsruhe, Germany.
Julia FröbelUniversity of Freiburg, Institute of Biochemistry and Molecular Biology, Freiburg, Germany.
Anne-Sophie BlümmelUniversity of Freiburg, Institute of Biochemistry and Molecular Biology, Freiburg, Germany.
Julia SetzlerKarlsruhe Institute of Technology (KIT), Institute of Nanotechnology, Karlsruhe, Germany.
Wolfgang WenzelKarlsruhe Institute of Technology (KIT), Institute of Nanotechnology, Karlsruhe, Germany.
Torsten H WaltherKarlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), Karlsruhe, Germany. Electronic address: torsten.walther@kit.edu.
Anne S UlrichKarlsruhe Institute of Technology (KIT), Institute of Organic Chemistry, Karlsruhe, Germany; Karlsruhe Institute of Technology (KIT), Institute of Biological Interfaces (IBG-2), Karlsruhe, Germany. Electronic address: anne.ulrich@kit.edu.
Karlsruhe Institute of Technology · DEUniversity of Freiburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The twin arginine translocase (Tat) exports folded proteins across bacterial membranes. The putative pore-forming or membrane-weakening component (TatA

Indexed as

Escherichia coli ProteinsMembrane Transport ProteinsLipid BilayersMagnetic Resonance SpectroscopyEscherichia coli ProteinsLipid BilayersMembrane Transport Proteins

Identifiers

PMID36523158
PMCPMC10257086
OpenAlexW4311511740

What OpenQuestion holds

Textmetadata
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.