Evidence map›Paper›PMID 23271514›Full record

ArticleEuropean biophysics journal : EBJ2013

Peptide translocation through the mesoscopic channel: binding kinetics at the single molecule level.

Usha Lamichhane, Tuhidul Islam, Sonal Prasad, Helge Weingart, Kozhinjampara R Mahendran, Mathias Winterhalter

Abstract read
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In one paragraph

Article in European biophysics journal : EBJ, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Lysenin Channels as Sensors for Ions and Molecules.Sensors (Basel, Switzerland) · 2020
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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.

Usha LamichhaneSchool of Engineering and Science, Jacobs University Bremen, Campus Ring 1, 28759, Bremen, Germany.
Tuhidul Islam
Sonal Prasad
Helge Weingart
Kozhinjampara R Mahendran
Mathias Winterhalter

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single channel electrophysiological studies have been carried out to elucidate the underlying interactions during the translocation of polypeptides through protein channels. For this we used OmpF from the outer cell membrane of E. coli and arginine-based peptides of different charges, lengths and covalently linked polyethylene glycol as a model system. In order to reveal the fast kinetics of peptide binding, we performed a temperature scan. Together with the voltage-dependent single-channel conductance, we quantify peptide binding and translocation.

Indexed as

Models, MolecularCell MembraneElectrophysiological PhenomenaEscherichia coliKineticsPeptidesPolyethylene GlycolsPorinsProtein ConformationProtein TransportTemperatureThermodynamicsOmpF proteinPeptidesPolyethylene GlycolsPorins

Identifiers

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.