Evidence map›Paper›PMID 21339604›Full record

ArticleJournal of physics. Condensed matter : an Institute of Physics journal2010

Facilitated translocation of polypeptides through a single nanopore.

Robert Bikwemu, Aaron J Wolfe, Xiangjun Xing, Liviu Movileanu

Abstract read
In one paragraph

Article in Journal of physics. Condensed matter : an Institute of Physics journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

34 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Insertion state of modular protein nanopores into a membrane.Biochimica et biophysica acta. Biomembranes · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Detergent Desorption of Membrane Proteins Exhibits Two Kinetic Phases.The journal of physical chemistry letters · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016
    Article
  18. Article
  19. Article
  20. 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

4 authors at 2 institutions in 2 countries.

Robert BikwemuDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, NY 13244-1130, USA.
Aaron J Wolfe
Xiangjun Xing
Liviu Movileanu
Syracuse University · USShanghai Jiao Tong University · CN

Funding

Engineered Nanopores for Single-Molecule Stochastic SensingR01GM088403 · NIGMS · SYRACUSE UNIVERSITY · PI MOVILEANU, LIVIU · 2009 to 2022
$3.8M
NIGMS NIH HHS R01 GM088403
6 · The paper itself

Abstract

The transport of polypeptides through nanopores is a key process in biology and medical biotechnology. Despite its critical importance, the underlying kinetics of polypeptide translocation through protein nanopores is not yet comprehensively understood. Here, we present a simple two-barrier, one-well kinetic model for the translocation of short positively charged polypeptides through a single transmembrane protein nanopore that is equipped with negatively charged rings, simply called traps. We demonstrate that the presence of these traps within the interior of the nanopore dramatically alters the free energy landscape for the partitioning of the polypeptide into the nanopore interior, as revealed by significant modifications in the activation free energies required for the transitions of the polypeptide from one state to the other. Our kinetic model permits the calculation of the relative and absolute exit frequencies of the short cationic polypeptides through either opening of the nanopore. Moreover, this approach enabled quantitative assessment of the kinetics of translocation of the polypeptides through a protein nanopore, which is strongly dependent on several factors, including the nature of the translocating polypeptide, the position of the traps, the strength of the polypeptide-attractive trap interactions and the applied transmembrane voltage.

Indexed as

Models, ChemicalModels, MolecularProtein TransportComputer SimulationDiffusionNanostructuresPeptidesPorosityPeptides

Identifiers

PMID21339604
PMCPMC3108026
OpenAlexW2094274729

What OpenQuestion holds

Textmetadata
LicenceTDM
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.