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Cited by 217

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

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

Open access
Moscat, Jorge, Diaz‐Meco, María T·2000·EMBO reports

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.

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Metadata

Authors
Moscat, J., & Diaz‐Meco, M. T.
Venue
EMBO reports
Published
2000-11
Volume
1
Issue
5
Pages
399-403
ISSN
  • 1469-221X (ISSN-L)
  • 1469-3178
OpenAlex
W2100246616
Cited by
217
References
2
FWCI
6.08
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: The atypical protein kinase Cs: Functional specificity mediated by specific protein adapters. https://app.cochat.ai/papers/10.1093/embo-reports/kvd098
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Moscat, J., & Diaz‐Meco, M. T. (2000). The atypical protein kinase Cs: Functional specificity mediated by specific protein adapters. EMBO reports. https://doi.org/10.1093/embo-reports/kvd098

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.