Evidence map›Paper›PMID 41017145›Full record

ArticleBiophysical journal2025

Selective detection of a key region in chemotaxis signaling protein complexes by solid-state NMR.

Jessica J Allen, Songlin Wang, Chad M Rienstra, Lynmarie K Thompson

Abstract read
In one paragraph

Article in Biophysical journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Jessica J AllenDepartment of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts.
Songlin WangNational Magnetic Resonance Facility at Madison (NMRFAM), University of Wisconsin-Madison, Madison, Wisconsin.
Chad M RienstraNational Magnetic Resonance Facility at Madison (NMRFAM), University of Wisconsin-Madison, Madison, Wisconsin; Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin; Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin; Morgridge Institute for Research, Madison, Wisconsin. Electronic address: crienstra@wisc.edu.
Lynmarie K ThompsonDepartment of Chemistry, University of Massachusetts Amherst, Amherst, Massachusetts. Electronic address: thompson@chem.umass.edu.

Funding

Technologies for Solid-State NMR Data CollectionP41GM136463 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI WESTLER, WILLIAM MILO · 2021 to 2025
$6.4M
NMR User Program at NMRFAMR24GM141526 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Katherine Anne Henzler-Wildman · 2021 to 2026
$6.4M
Chemistry-Biology Interface Predoctoral Training GrantT32GM139789 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI ERIC Robert STRIETER · 2021 to 2026
$3.4M
Assembly and Function of Bacterial Chemotaxis Receptor Signaling ComplexesR01GM120195 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI THOMPSON, LYNMARIE K. · 2017 to 2023
$2.1M
Acquisition of Bruker 900 MHz NEO console and probesS10OD034243 · OD · UNIVERSITY OF WISCONSIN-MADISON · PI HENZLER-WILDMAN, KATHERINE ANNE · 2023 to 2023
$1.5M
NIGMS NIH HHS P41 GM136463NIGMS NIH HHS R01 GM120195NIGMS NIH HHS R24 GM141526NIGMS NIH HHS T32 GM139789NIH HHS S10 OD034243
6 · The paper itself

Abstract

Understanding how large protein complexes function requires tools that can resolve both structure and dynamics in their native assembly states. Here, we apply solid-state nuclear magnetic resonance (SSNMR) to selectively detect rigid regions of a receptor protein fragment in the context of the >500-kDa chemoreceptor signaling complex found in chemotactic bacteria. These complexes assemble into hexagonal arrays that network multiple active units together. The cytoplasmic fragment of the E. coli aspartate chemoreceptor exhibits dynamics on multiple timescales across different regions of the protein, and these dynamics differ between signaling states. We apply

Indexed as

ChemotaxisEscherichia coli ProteinsNuclear Magnetic Resonance, BiomolecularSignal TransductionEscherichia coliEscherichia coli Proteins

Identifiers

PMID41017145
PMCPMC12532373

What OpenQuestion holds

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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.