Evidence map›Paper›PMID 28693322›Full record

ArticleACS nano2017

Nanopore Sensing of Protein Folding.

Wei Si, Aleksei Aksimentiev

Abstract read
In one paragraph

Article in ACS nano, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing 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

45 citing papers in PubMed.

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  11. Nanopore analysis of cis-diols in fruits.Nature communications · 2024
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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

2 authors.

Wei SiDepartment of Physics, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.
Aleksei AksimentievDepartment of Physics, University of Illinois at Urbana-Champaign , Urbana, Illinois 61801, United States.ORCID 0000-0002-6042-8442

Funding

Plasmonic nanopores for trapping, controlled motion and sequencing of DNAR01HG007406 · NHGRI · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI AKSIMENTIEV, ALEKSEI · 2013 to 2016
$2.4M
NHGRI NIH HHS R01 HG007406
6 · The paper itself

Abstract

Single-molecule studies of protein folding hold keys to unveiling protein folding pathways and elusive intermediate folding states-attractive pharmaceutical targets. Although conventional single-molecule approaches can detect folding intermediates, they presently lack throughput and require elaborate labeling. Here, we theoretically show that measurements of ionic current through a nanopore containing a protein can report on the protein's folding state. Our all-atom molecular dynamics (MD) simulations show that the unfolding of a protein lowers the nanopore ionic current, an effect that originates from the reduction of ion mobility in proximity to a protein. Using a theoretical model, we show that the average change in ionic current produced by a folding-unfolding transition is detectable despite the orientational and conformational heterogeneity of the folded and unfolded states. By analyzing millisecond-long all-atom MD simulations of multiple protein transitions, we show that a nanopore ionic current recording can detect folding-unfolding transitions in real time and report on the structure of folding intermediates.

Indexed as

NanoporesProtein FoldingDatabases, ProteinIon TransportMolecular Dynamics SimulationProtein ConformationProteinsProtein UnfoldingProteinsfolding intermediatesionic currentmisfoldingmolecular dynamicsnanoporeprotein folding

Identifiers

PMID28693322
PMCPMC5564329

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Registered trials

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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.