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Cited by 477

The DOI matches its Crossref record; 70 of the 70 references it cites were found in a registry or an index.

Assembly of allosteric macromolecular switches: lessons from PKA

Open access
Taylor, Susan S., Ilouz, Ronit, Zhang, Ping, Kornev, Alexandr P.·2012·Nature Reviews Molecular Cell Biology

Abstract

Protein kinases are dynamic molecular switches that have evolved to be only transiently activated. Kinase activity is embedded within a conserved kinase core, which is typically regulated by associated domains, linkers and interacting proteins. Moreover, protein kinases are often tethered to large macromolecular complexes to provide tighter spatiotemporal control. Thus, structural characterization of kinase domains alone is insufficient to explain protein kinase function and regulation in vivo. Recent progress in structural characterization of cyclic AMP-dependent protein kinase (PKA) exemplifies how our knowledge of kinase signalling has evolved by shifting the focus of structural studies from single kinase subunits to macromolecular complexes.

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Crossref · 10.1038/nrm3432

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Metadata

Authors
Taylor, S. S., Ilouz, R., Zhang, P., & Kornev, A. P.
Venue
Nature Reviews Molecular Cell Biology
Published
2012-09-20
Volume
13
Issue
10
Pages
646-658
ISSN
  • 1471-0072 (ISSN-L)
  • 1471-0080
OpenAlex
W2061684132
Cited by
477
References
70
FWCI
2.22
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Assembly of allosteric macromolecular switches: lessons from PKA. https://app.cochat.ai/papers/10.1038/nrm3432
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Taylor, S. S., Ilouz, R., Zhang, P., & Kornev, A. P. (2012). Assembly of allosteric macromolecular switches: lessons from PKA. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/nrm3432

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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.