Evidence map›Paper›PMID 34762087›Full record

ArticlePhysical chemistry chemical physics : PCCP2021

Structural determinants of a permeation barrier of the SecYEG translocon in the active state.

Ekaterina Sobakinskaya, Heinrich Krobath, Thomas Renger, Frank Müh

Open access · hybridAbstract read
In one paragraph

Article in Physical chemistry chemical physics : PCCP, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.7field-weighted citation impact, top 25% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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

4 authors at 1 institution in 1 country.

Ekaterina SobakinskayaInstitute for Theoretical Physics, Johannes Kepler University Linz, Altenberger Strasse 69, A-4040 Linz, Austria. ekaterina.sobakinskaya@jku.at.ORCID http://orcid.org/0000-0002-2177-6698
Heinrich KrobathInstitute for Theoretical Physics, Johannes Kepler University Linz, Altenberger Strasse 69, A-4040 Linz, Austria. ekaterina.sobakinskaya@jku.at.ORCID http://orcid.org/0000-0001-6473-8109
Thomas RengerInstitute for Theoretical Physics, Johannes Kepler University Linz, Altenberger Strasse 69, A-4040 Linz, Austria. ekaterina.sobakinskaya@jku.at.ORCID http://orcid.org/0000-0001-9245-3805
Frank MühInstitute for Theoretical Physics, Johannes Kepler University Linz, Altenberger Strasse 69, A-4040 Linz, Austria. ekaterina.sobakinskaya@jku.at.ORCID http://orcid.org/0000-0002-8818-2616
Johannes Kepler University of Linz · AT

Funding

Austrian Science Fund FWF P 33154
6 · The paper itself

Abstract

The SecYEG translocon is a channel in bacteria, which provides a passage for secretory proteins across as well as integration of membrane proteins into the plasma membrane. The molecular mechanism, by which SecYEG manages protein transport while preventing water and ion leakage through the membrane, is still controversial. We employed molecular dynamics simulations to assess the contribution of the major structural elements - the plug and the pore ring (PR) - to the sealing of SecYEG in the active state,

Indexed as

Molecular Dynamics SimulationProtein ConformationSEC Translocation ChannelsThermus thermophilusSEC Translocation Channels

Identifiers

PMID34762087
PMCPMC8612361
OpenAlexW3208142599

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.