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 accessAbstract
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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Cites
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Self-citationIntrinsically Disordered Proteins
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Cited by
Li, L., Li, C., Zhang, Z., & Alexov, E. (2013) · Journal of Chemical Theory and Computation · doi:10.1021/ct400065j · Cited by 543
Constitutive activation of PKA catalytic subunit in adrenal Cushing’s syndrome
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Activation of PKA leads to mesenchymal-to-epithelial transition and loss of tumor-initiating ability
Pattabiraman, D. R., Bierie, B., Kober, K. I., Thiru, P., Krall, J. A., Zill, C., Reinhardt, F., Tam, W. L., & Weinberg, R. A. (2016) · Science · doi:10.1126/science.aad3680 · Cited by 332
Activating hotspot L205R mutation in PRKACA and adrenal Cushing’s syndrome
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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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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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