Evidence map›Paper›PMID 26302243›Full record

ArticleACS nano2015

Dynamics and Energy Contributions for Transport of Unfolded Pertactin through a Protein Nanopore.

Benjamin Cressiot, Esther Braselmann, Abdelghani Oukhaled, Adrian H Elcock, Juan Pelta, Patricia L Clark

Open access · greenAbstract read
In one paragraph

Article in ACS nano, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

28 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Blobs form during the single-file transport of proteins across nanopores.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. From current trace to the understanding of confined media.The European physical journal. E, Soft matter · 2018
    Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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 at 4 institutions in 2 countries.

Benjamin CressiotDepartment of Chemistry & Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Esther BraselmannDepartment of Chemistry & Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
Abdelghani OukhaledLAMBE UMR 8587 CNRS, University of Cergy-Pontoise , Cergy-Pontoise, France.
Adrian H ElcockDepartment of Biochemistry, University of Iowa , Iowa City, Iowa 52242, United States.
Juan PeltaLAMBE UMR 8587 CNRS, University of Évry-Val-d'Essonne , Évry, France.
Patricia L ClarkDepartment of Chemistry & Biochemistry, University of Notre Dame , Notre Dame, Indiana 46556, United States.
University of Notre Dame · USCentre National de la Recherche Scientifique · FRLaboratoire Analyse et Modélisation pour la Biologie et l'Environnement · FRUniversity of Iowa · US

Funding

Chemistry-Biochemistry-Biology Training Program at Notre DameT32GM075762 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CHANG, MAYLAND F, MOBASHERY, SHAHRIAR · 2007 to 2021
$3.7M
Interactions Regulating Translation and Protein Biogenesis in VivoU54GM105816 · NIGMS · UNIVERSITY OF NOTRE DAME · PI BUSKIRK, ALLEN ROWDON, CLARK, PATRICIA LOUISE · 2013 to 2017
$3.7M
OUTER MEMBRANE SECRETION MECHANISM FOR AUTOTRANSPORTER PROTEINSR01GM097573 · NIGMS · UNIVERSITY OF NOTRE DAME · PI CLARK, PATRICIA LOUISE · 2011 to 2014
$1.1M
NIGMS NIH HHS R01 GM097573NIGMS NIH HHS T32 GM075762NIGMS NIH HHS U54 GM105816
6 · The paper itself

Abstract

To evaluate the physical parameters governing translocation of an unfolded protein across a lipid bilayer, we studied protein transport through aerolysin, a passive protein channel, at the single-molecule level. The protein model used was the passenger domain of pertactin, an autotransporter virulence protein. Transport of pertactin through the aerolysin nanopore was detected as transient partial current blockades as the unfolded protein partially occluded the aerolysin channel. We compared the dynamics of entry and transport for unfolded pertactin and a covalent end-to-end dimer of the same protein. For both the monomer and the dimer, the event frequency of current blockades increased exponentially with the applied voltage, while the duration of each event decreased exponentially as a function of the electrical potential. The blockade time was twice as long for the dimer as for the monomer. The calculated activation free energy includes a main enthalpic component that we attribute to electrostatic interactions between pertactin and the aerolysin nanopore (despite the low Debye length), plus an entropic component due to confinement of the unfolded chain within the narrow pore. Comparing our experimental results to previous studies and theory suggests that unfolded proteins cross the membrane by passing through the nanopore in a somewhat compact conformation according to the "blob" model of Daoud and de Gennes.

Indexed as

NanoporesProtein TransportProtein UnfoldingBacterial Outer Membrane ProteinsLipid BilayersNanotechnologyProtein DenaturationVirulence Factors, BordetellaBacterial Outer Membrane ProteinsLipid BilayerspertactinVirulence Factors, Bordetellaautotransporterselectrical detectionprotein nanoporesecretionsingle moleculetranslocationunfolded protein

Identifiers

PMID26302243
PMCPMC4835817
OpenAlexW2418788167

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.