Evidence map›Paper›PMID 41303446›Full record

ArticleInternational journal of molecular sciences2025

From Plankton to Primates: How VSP Sequence Diversity Shapes Voltage Sensing.

Lee Min Leong, Youna Kim, Bradley J Baker

Abstract read
In one paragraph

Article in International journal of molecular sciences, 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

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

3 authors.

Lee Min LeongBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.ORCID 0009-0005-2169-0084
Youna KimBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.
Bradley J BakerBrain Science Institute, Korea Institute of Science and Technology, Seoul 02792, Republic of Korea.ORCID 0000-0003-4652-5585

Funding

Korea Institute of Science and Technology 2e31523
6 · The paper itself

Abstract

Voltage-sensing phosphatases (VSPs) provide a conserved framework for dissecting the mechanics of voltage sensing and for engineering genetically encoded voltage indicators (GEVIs). To evaluate how natural sequence diversity shapes function, we compared VSP voltage-sensing domains (VSDs) from multiple species by replacing the phosphatase domain with a fluorescent protein to enable optical detection of VSD responses. Every construct that reached the plasma membrane produced a voltage-dependent optical signal, underscoring the deep conservation of voltage sensing across VSP orthologs. Yet lineage-specific substitutions generated strikingly different phenotypes. A plankton VSP ortholog from

Indexed as

Phosphoric Monoester HydrolasesPlanktonAmino Acid SequenceAnimalsAplysiaCell MembraneCricetulusHumansPrimatesPhosphoric Monoester Hydrolasesgenetically encoded voltage indicator (GEVI)voltage-sensing domain (VSD)voltage-sensing phosphatase (VSP)

Identifiers

PMID41303446
PMCPMC12652588

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.