Evidence map›Paper›PMID 36528790›Full record

ArticleBiophysical journal2023

Insights into autoregulation of a membrane protein complex by its cytoplasmic domains.

Vanessa Leone, Richard T Bradshaw, Caroline Koshy, Paul Suhwan Lee, Cristina Fenollar-Ferrer, Veronika Heinz, Christine Ziegler, Lucy R Forrest

Open access · greenAbstract read
In one paragraph

Article in Biophysical journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.1field-weighted citation impact, top 56% 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

2 citing papers in PubMed, 1 citations in OpenAlex.

  1. Adaptive microevolution in CC17Frontiers in cellular and infection microbiology · 2026
    Article
  2. 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

8 authors at 3 institutions in 2 countries.

Vanessa LeoneComputational Structural Biology Section, National Institutes of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland. Electronic address: vanessa.leone@nih.gov.
Richard T BradshawComputational Structural Biology Section, National Institutes of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland.
Caroline KoshyComputational Structural Biology Section, National Institutes of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland.
Paul Suhwan LeeComputational Structural Biology Section, National Institutes of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland.
Cristina Fenollar-FerrerComputational Structural Biology Section, National Institutes of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland.
Veronika HeinzDepartment of Structural Biology/Biophysics II, University of Regensburg, Regensburg, Germany.
Christine ZieglerDepartment of Structural Biology/Biophysics II, University of Regensburg, Regensburg, Germany.
Lucy R ForrestComputational Structural Biology Section, National Institutes of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland. Electronic address: lucy.forrest@nih.gov.
National Institute of Neurological Disorders and Stroke · USNational Institutes of Health · USUniversity of Regensburg · DE

Funding

Computational Studies of Membrane Transport ProteinsZIANS003139 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI FORREST, LUCY · 2014 to 2025
$13.7M
Breakthrough Molecular Dynamics Research via an Anton2 SupercomputerR01GM116961 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI BLOOD, PHILIP D. · 2016 to 2023
$3.0M
Intramural NIH HHS ZIA NS003139NIGMS NIH HHS R01 GM116961
6 · The paper itself

Abstract

Membrane transporters mediate the passage of molecules across membranes and are essential for cellular function. While the transmembrane region of these proteins is responsible for substrate transport, often the cytoplasmic regions are required for modulating their activity. However, it can be difficult to obtain atomic-resolution descriptions of these autoregulatory domains by classical structural biology techniques, especially if they lack a single, defined structure. The betaine permease, BetP, a homotrimer, is a prominent and well-studied example of a membrane protein whose autoregulation depends on cytoplasmic N- and C-terminal segments. These domains sense and transduce changes in K

Indexed as

SymportersBacterial ProteinsHomeostasisMembrane ProteinsModels, MolecularProtein SubunitsBacterial ProteinsMembrane ProteinsProtein SubunitsSymporters

Identifiers

PMID36528790
PMCPMC9941749
OpenAlexW4311860137

What OpenQuestion holds

Textmetadata
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.