Evidence map›Paper›PMID 32400834›Full record

ArticleNanoscale2020

Effect of a post-translational modification mimic on protein translocation through a nanopore.

David P Hoogerheide, Philip A Gurnev, Tatiana K Rostovtseva, Sergey M Bezrukov

Open access · greenAbstract read
In one paragraph

Article in Nanoscale, 2020. 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
1.7field-weighted citation impact, top 17% 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

14 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  12. Capturing single molecules by nanopores: measured times and thermodynamics.Physical chemistry chemical physics : PCCP · 2021
    Article
  13. Article
  14. PPDiffuse: A Quantitative Prediction Tool for Diffusion of Charged Polymers in a Nanopore.Journal of research of the National Institute of Standards and Technology · 2020
    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 2 institutions in 4 countries.

David P HoogerheideCenter for Neutron Research, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA. david.hoogerheide@nist.gov.ORCID http://orcid.org/0000-0003-2918-1469
Philip A GurnevSection on Molecular Transport, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.ORCID http://orcid.org/0000-0001-9247-5027
Tatiana K RostovtsevaSection on Molecular Transport, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.ORCID http://orcid.org/0000-0001-7299-7362
Sergey M BezrukovSection on Molecular Transport, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.ORCID http://orcid.org/0000-0002-8209-8050
National Institutes of Health · USNational Institute of Standards and Technology · US

Funding

Biophysics of Large Membrane ChannelsZIAHD000072 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI BEZRUKOV, SERGEY M · 2009 to 2025
$22.8M
Intramural NIH HHS ZIA HD000072Intramural NIST DOC 9999-NIST
6 · The paper itself

Abstract

Post-translational modifications (PTMs) of proteins are recognized as crucial components of cell signaling pathways through modulating folding, altering stability, changing interactions with ligands, and, therefore, serving multiple regulatory functions. PTMs occur as covalent modifications of the protein's amino acid side chains or the length and composition of their termini. Here we study the functional consequences of PTMs for α-synuclein (αSyn) interactions with the nanopore of the voltage-dependent anion channel (VDAC) of the outer mitochondrial membrane. PTMs were mimicked by a divalent Alexa Fluor 488 sidechain attached separately at two positions on the αSyn C-terminus. Using single-channel reconstitution into planar lipid membranes, we find that such modifications change interactions drastically in both efficiency of VDAC inhibition by αSyn and its translocation through the VDAC nanopore. Analysis of the on/off kinetics in terms of an interaction "quasipotential" allows the positions of the C-terminal modifications to be determined with an accuracy of about three residues. Moreover, our results uncover a previously unobserved mechanism by which cytosolic proteins control β-barrel channels and thus a new regulatory function for PTMs.

Indexed as

alpha-SynucleinMitochondria, LiverMitochondrial MembranesNanoporesProtein Processing, Post-TranslationalAnimalsProtein TransportRatsalpha-SynucleinSnca protein, rat

Identifiers

PMID32400834
PMCPMC7350168
OpenAlexW3019720946

What OpenQuestion holds

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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.