Evidence map›Paper›PMID 40601812›Full record

ArticleThe FEBS journal2025

Protein kinase A: a quirky prototype.

Matthew G Gold

Abstract read
In one paragraph

Article in The FEBS journal, 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.

Matthew G GoldDepartment of Neuroscience, Physiology & Pharmacology, University College London, UK.ORCID https://orcid.org/0000-0002-1281-0815

Funding

Biotechnology and Biological Sciences Research Council BB/X008215/1
6 · The paper itself

Abstract

Protein kinase A (PKA) has served as a prototype for establishing kinase fundamentals, including sequence, structure and catalytic mechanism. However, PKA is quirky in some respects. Its regulatory elements are expressed separately, including type I (RI) regulatory subunits that contain unusual disulphide-linked dimerization and docking domains. Benjamin-Zukerman and colleagues report on the RIβ mutation L50R that disrupts this domain to cause neuronal loss and parkinsonism driven by a PKA mutation. They show that PKA catalytic subunits are released more easily from RIβ subunits containing the L50R mutation, adding depth to our understanding of this neurodevelopmental disorder.

Indexed as

Cyclic AMP-Dependent Protein KinasesAnimalsCatalytic DomainHumansMutationCyclic AMP-Dependent Protein KinasescAMPdimerneurodevelopmental disorderprotein kinase A

Identifiers

PMID40601812
PMCPMC12443464

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.