Evidence map›Paper›PMID 36680342›Full record

ArticleBiophysical journal2023

Role of K364 next to the active site cysteine in voltage-dependent phosphatase activity of Ci-VSP.

Ian Costa Paixao, Natsuki Mizutani, Makoto Matsuda, Rizki Tsari Andriani, Takafumi Kawai, Atsushi Nakagawa, Yoshifumi Okochi, Yasushi Okamura

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Voltage clamp fluorometry inBio-protocol · 2025
    Article
  2. Article
  3. Article
  4. Membranes in focus.Biophysical journal · 2023
    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

8 authors at 3 institutions in 1 country.

Ian Costa PaixaoDepartment of Physiology, Graduate School of Medicine, Osaka University, Suita, Japan; Graduate School of Frontier Biosciences, Osaka University, Suita, Japan.
Natsuki MizutaniDepartment of Physiology, Graduate School of Medicine, Osaka University, Suita, Japan.
Makoto MatsudaDepartment Oncogene Research, Research Institute for Microbial Diseases, Osaka University, Suita, Japan; Laboratory for Supramolecular Crystallography, Institute for Protein Research, Osaka University, Suita, Japan.
Rizki Tsari AndrianiDepartment of Physiology, Graduate School of Medicine, Osaka University, Suita, Japan; Graduate School of Medicine, Osaka University JSPS International Research Fellow, Suita, Japan.
Takafumi KawaiDepartment of Physiology, Graduate School of Medicine, Osaka University, Suita, Japan.
Atsushi NakagawaLaboratory for Supramolecular Crystallography, Institute for Protein Research, Osaka University, Suita, Japan.
Yoshifumi OkochiDepartment of Physiology, Graduate School of Medicine, Osaka University, Suita, Japan. Electronic address: okochyo@phys2.med.osaka-u.ac.jp.
Yasushi OkamuraDepartment of Physiology, Graduate School of Medicine, Osaka University, Suita, Japan; Graduate School of Frontier Biosciences, Osaka University, Suita, Japan. Electronic address: yokamura@phys2.med.osaka-u.ac.jp.
The University of Osaka · JPOsaka Gakuin University · JPProtein Research Foundation · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage-sensing phosphatase (VSP) consists of the voltage sensor domain (VSD) similar to that of voltage-gated ion channels and the cytoplasmic phosphatase region with remarkable similarity to the phosphatase and tensin homolog deleted on chromosome 10 (PTEN). Membrane depolarization activates VSD, leading to dephosphorylation of three species of phosphoinositides (phosphatidylinositol phosphates (PIPs)), PI(3,4,5)P

Indexed as

CysteineLysineAmino AcidsAnimalsCatalytic DomainMammalsPhosphatidylinositol PhosphatesPhosphoric Monoester HydrolasesZebrafishAmino AcidsCysteineLysinePhosphatidylinositol PhosphatesPhosphoric Monoester Hydrolases

Identifiers

PMID36680342
PMCPMC10257114
OpenAlexW4317681244

What Socratic 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 Socratic graph.