Evidence map›Paper›PMID 37569469›Full record

ReviewInternational journal of molecular sciences2023

Gating of β-Barrel Protein Pores, Porins, and Channels: An Old Problem with New Facets.

Lauren A Mayse, Liviu Movileanu

Abstract readReview
In one paragraph

Review in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Article
  2. Solute flux through a fluctuating membrane channel.Physical chemistry chemical physics : PCCP · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Exploring the Terra incognita of AI-based domain classifications.Protein science : a publication of the Protein Society · 2025
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. 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

2 authors.

Lauren A MayseDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, NY 13244, USA.
Liviu MovileanuDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, NY 13244, USA.ORCID 0000-0002-2525-3341

Funding

Engineered Nanopores for Single-Molecule Stochastic SensingR01GM088403 · NIGMS · SYRACUSE UNIVERSITY · PI MOVILEANU, LIVIU · 2009 to 2022
$3.8M
Development of Modular Synthetic Sensors for Protein Biomarker DetectionR01EB033412 · NIBIB · SYRACUSE UNIVERSITY · PI LIVIU MOVILEANU · 2023 to 2026
$1.4M
NIBIB NIH HHS R01 EB033412NIGMS NIH HHS R01 GM088403NIH HHS R01 GM088403 (to L.M.) and R01 EB033412 (to L.M.).
6 · The paper itself

Abstract

β barrels are ubiquitous proteins in the outer membranes of mitochondria, chloroplasts, and Gram-negative bacteria. These transmembrane proteins (TMPs) execute a wide variety of tasks. For example, they can serve as transporters, receptors, membrane-bound enzymes, as well as adhesion, structural, and signaling elements. In addition, multimeric β barrels are common structural scaffolds among many pore-forming toxins. Significant progress has been made in understanding the functional, structural, biochemical, and biophysical features of these robust and versatile proteins. One frequently encountered fundamental trait of all β barrels is their voltage-dependent gating. This process consists of reversible or permanent conformational transitions between a large-conductance, highly permeable open state and a low-conductance, solute-restrictive closed state. Several intrinsic molecular mechanisms and environmental factors modulate this universal property of β barrels. This review article outlines the typical signatures of voltage-dependent gating. Moreover, we discuss recent developments leading to a better qualitative understanding of the closure dynamics of these TMPs.

Indexed as

Membrane Transport ProteinsPorinsBacterial Outer Membrane ProteinsBiophysicsMolecular ConformationBacterial Outer Membrane ProteinsMembrane Transport ProteinsPorinsconformational transitionselectrophysiologymembrane proteinsprotein foldingsingle-molecule dynamics

Identifiers

PMID37569469
PMCPMC10418385

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.