Evidence map›Paper›PMID 41007321›Full record

ReviewBiology2025

Structural Insights into Arginine Kinase and Phosphagen Kinase Homologs: Mechanisms of Catalysis, Regulation, and Evolution.

Sung-Min Kang

Abstract readReview
In one paragraph

Review in Biology, 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

1 author.

Sung-Min KangCollege of Pharmacy, Duksung Women's University, Seoul 01369, Republic of Korea.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Phosphagen kinases are vital for energy buffering and ATP regeneration in cells with high or fluctuating energy demands. Phosphagens are small, high-energy phosphate-storage molecules, such as arginine phosphate or creatine phosphate, that serve as immediate phosphate donors for rapid ATP production. Among them, arginine kinase plays a central role in invertebrates, while creatine kinase is predominant in vertebrates. This review presents a comprehensive structural analysis of arginine kinases and their homologs across diverse species, ranging from invertebrates like

Indexed as

arginine kinasecatalytic mechanismphosphagen kinaseprotein structure

Identifiers

PMID41007321
PMCPMC12467219

What Socratic holds

Textmetadata
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 Socratic graph.