Evidence map›Paper›PMID 38100320›Full record

ArticleThe Biochemical journal2023

Into the fold: advances in understanding aPKC membrane dynamics.

Mathias Cobbaut, Peter J Parker, Neil Q McDonald

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2023. 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, top 67% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

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 at 2 institutions in 1 country.

Mathias CobbautSignalling and Structural Biology Laboratory, The Francis Crick Institute, NW1 1AT London, U.K.ORCID 0000-0003-0279-0336
Peter J ParkerProtein Phosphorylation Laboratory, The Francis Crick Institute, NW1 1AT London, U.K.ORCID 0000-0001-5907-6980
Neil Q McDonaldSignalling and Structural Biology Laboratory, The Francis Crick Institute, NW1 1AT London, U.K.ORCID 0000-0003-0975-6325
The Francis Crick Institute · GBKing's College London · GB

Funding

Medical Research CouncilWellcome Trust CC2068Wellcome Trust CC2140
6 · The paper itself

Abstract

Atypical protein kinase Cs (aPKCs) are part of the PKC family of protein kinases and are atypical because they don't respond to the canonical PKC activators diacylglycerol (DAG) and Ca2+. They are central to the organization of polarized cells and are deregulated in several cancers. aPKC recruitment to the plasma membrane compartment is crucial to their encounter with substrates associated with polarizing functions. However, in contrast with other PKCs, the mechanism by which atypical PKCs are recruited there has remained elusive until recently. Here, we bring aPKC into the fold, summarizing recent reports on the direct recruitment of aPKC to membranes, providing insight into seemingly discrepant findings and integrating them with existing literature.

Indexed as

Protein Kinase CCell MembraneProtein Kinase Capkcatypical pkccell polarityphospholipidsprotein kinase c

Identifiers

PMID38100320
PMCPMC10754278
OpenAlexW4389781567

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.