Evidence map›Paper›PMID 40806479›Full record

ArticleInternational journal of molecular sciences2025

LIMK2-1 Is a Phosphorylation-Dependent Inhibitor of Protein Phosphatase-1 Catalytic Subunit and Myosin Phosphatase Holoenzyme.

Andrea Kiss, Emese Tóth, Zsófia Bodogán, Mohamad Mahfood, Zoltán Kónya, Ferenc Erdődi

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

6 authors.

Andrea KissDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary.ORCID 0000-0002-0664-5235
Emese TóthDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary.ORCID 0000-0003-4519-6134
Zsófia BodogánDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary.
Mohamad MahfoodDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary.
Zoltán KónyaDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary.
Ferenc ErdődiDepartment of Medical Chemistry, Faculty of Medicine, University of Debrecen, H-4032 Debrecen, Hungary.ORCID 0000-0002-5277-3668

Funding

Coordinating Center for International Education, University of Debrecen, Debrecen, Hungary naNational Research, Development and Innovation Office of Hungary K129104University of Debrecen Bridging Fund (1G3D BKJ0 BFKA 247)
6 · The paper itself

Abstract

The C-kinase-activated protein phosphatase-1 (PP1) inhibitor of 17 kDa (CPI-17) is a specific inhibitor of the PP1 catalytic subunit (PP1c) and the myosin phosphatase (MP) holoenzyme. CPI-17 requires the phosphorylation of Thr38 in the peptide segment

Indexed as

Lim KinasesMyosin-Light-Chain PhosphataseProtein Phosphatase 1Catalytic DomainHeLa CellsHoloenzymesHumansMarine ToxinsMCF-7 CellsOxazolesPhosphorylationcalyculin AHoloenzymesLim KinasesMarine ToxinsMyosin-Light-Chain PhosphataseOxazolesProtein Phosphatase 1calyculin A (CLA)C-kinase-activated protein phosphatase-1 (PP1) inhibitor of 17 kDa (CPI-17)LIMK2 isoform 1 (LIMK2-1)LIM kinase 2 (LIMK2)myosin phosphatase holoenzyme (MP)protein phosphatase-1 (PP1)

Identifiers

PMID40806479
PMCPMC12347249

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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.