Evidence map›Paper›PMID 41123309›Full record

ArticleACS sensors2025

Modulating Chromophore Flexibility in GEVIs through Threonine-Based Molecular Switches Reveals an Influence of Membrane Curvature on Protein Activity.

Lee Min Leong, Sang Chul Shin, Nazarii Frankiv, Jun Kyu Rhee, Heejung Kim, Jihye Seong, Junhyuk Woo, Kyungreem Han, Douglas A Storace, Bradley J Baker

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ACS sensors, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. 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

10 authors.

Lee Min LeongBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.ORCID 0009-0005-2169-0084
Sang Chul ShinTechnological Convergence Center, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.
Nazarii FrankivBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.
Jun Kyu RheeBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.
Heejung KimDepartment of Converging Science and Technology, Kyung Hee University, Seoul 02447, Republic of Korea.
Jihye SeongDepartment of Biomedical Sciences and Pharmacology, Seoul National University College of Medicine, Seoul 03080, Republic of Korea.
Junhyuk WooBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.
Kyungreem HanBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.
Douglas A StoraceDepartment of Biological Science, Florida State University, Tallahassee, Florida 32306, United States.
Bradley J BakerBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.ORCID 0000-0003-4652-5585

Funding

Understanding functional transformations carried out by the bulbR01DC020519 · NIDCD · FLORIDA STATE UNIVERSITY · PI Douglas Anthony Storace · 2022 to 2026
$1.9M
NIDCD NIH HHS R01 DC020519
6 · The paper itself

Abstract

Many genetically encoded voltage indicators (GEVIs) rely on fluorescent protein (FP) domains to report changes in membrane potential. Rapid and reversible disruption of steady-state fluorescence during voltage sensor activation revealed transient conformational changes near the chromophore in the FP domain, implicating chromophore flexibility as a potential mechanism of signal modulation. Substitution of a bulky phenylalanine near the chromophore with threonine (F165T) introduced a distinct secondary component in the fluorescence response, consistent with increased chromophore mobility. This effect was tunable: an external, directionally polarized offset (164

Indexed as

Cell MembraneGreen Fluorescent ProteinsLuminescent ProteinsThreonineMembrane PotentialsGreen Fluorescent ProteinsLuminescent ProteinsThreoninechromophore flexibilityfluorescent protein biosensorsgenetically encoded voltage indicators (GEVIs)membrane curvature sensingthreonine molecular switch

Identifiers

PMID41123309
PMCPMC13048449

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.