Evidence map›Paper›PMID 11258478›Full record

ReviewEMBO reports2000

The atypical protein kinase Cs. Functional specificity mediated by specific protein adapters.

J Moscat, M T Diaz-Meco

Open access · bronzeAbstract readReview
In one paragraph

Review in EMBO reports, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

75 citing papers in PubMed, 217 citations in OpenAlex.

  1. High Expression ofCancer genomics & proteomics · 2025
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15 more citing papers are in PubMed but not listed here.

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

2 authors at 2 institutions in 1 country.

J MoscatCentro de Biología Molecular Severo Ochoa, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Universidad Autónoma, Canto Blanco, Spain. jmoscat@cbm.uam.es
M T Diaz-Meco
Consejo Superior de Investigaciones Científicas · ESUniversidad Autónoma de Madrid · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Since its discovery more than 10 years ago, the atypical PKC (aPKC) subfamily has attracted great interest. A number of reports have shown that the kinases of this subfamily play critical roles in signaling pathways that control cell growth, differentiation and survival. Recently, several investigators have identified a number of aPKC-interacting proteins whose characterization is helping to unravel the mechanisms of action and functions of these kinases. These interactors include p62, Par-6, MEK5 and Par-4. The details of how these adapters serve to link the aPKCs to different receptor signaling pathways and substrates in response to specific stimuli are crucial not only for developing an understanding of the roles and functions of the aPKCs themselves, but also for more generally establishing a view of how specificity in signal transduction is achieved.

Indexed as

Intracellular Signaling Peptides and ProteinsAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsCarrier ProteinsHumansModels, BiologicalMolecular Sequence DataProtein BindingProtein Kinase CProtein Structure, TertiarySequence Homology, Amino AcidSignal TransductionApoptosis Regulatory ProteinsCarrier ProteinsIntracellular Signaling Peptides and Proteinsprostate apoptosis response-4 proteinProtein Kinase C

Identifiers

PMID11258478
PMCPMC1083770
OpenAlexW2100246616

What OpenQuestion 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 OpenQuestion graph.