Evidence map›Paper›PMID 40953491›Full record

ArticleJournal of the American Chemical Society2025

Quantification of Membrane Protein Conformational Free Energy from Mutations and a Single Atom.

Belen Ramirez-Cordero, Nathaniel J Traaseth

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

2 authors.

Belen Ramirez-CorderoDepartment of Chemistry, New York University, New York, New York 10003, United States.ORCID 0000-0003-0037-4777
Nathaniel J TraasethDepartment of Chemistry, New York University, New York, New York 10003, United States.ORCID 0000-0002-1185-6088

Funding

Mechanisms of Allostery and Molecular Recognition in the Small Multidrug Resistance FamilyR01AI108889 · NIAID · NEW YORK UNIVERSITY · PI Nathaniel J. Traaseth · 2014 to 2026
$5.4M
Transport Mechanisms and Inhibition of Efflux Pumps in Pathogenic OrganismsR01AI165782 · NIAID · NEW YORK UNIVERSITY · PI SHOHEI KOIDE, Nathaniel J. Traaseth · 2022 to 2026
$4.0M
NIAID NIH HHS R01 AI108889NIAID NIH HHS R01 AI165782
6 · The paper itself

Abstract

Secondary active transporters are membrane proteins involved in moving substrates across the cellular membrane. Conformational dynamics underlie this process, allowing the transporter to sample at least two conformations, nominally grouped into inward- and outward-facing states. While studies of structure and dynamics have revealed atomistic insight into transport mechanisms and transport rates, the relative free energy differences among conformations remain underexplored. In this work, we quantified free energy differences between inward- and outward-facing conformations of the multidrug

Indexed as

AntiportersEscherichia coli ProteinsEscherichia coliModels, MolecularMutationNuclear Magnetic Resonance, BiomolecularProtein ConformationThermodynamicsAntiportersEmrE protein, E coliEscherichia coli Proteins

Identifiers

PMID40953491
PMCPMC12464994

What OpenQuestion holds

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LicenceCC BY
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.