The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Protein kinase C in transmembrane signalling
Open accessAbstract
Protein kinase C functions as the transducer of a second messenger, diacylglycerol, and is the major receptor for tumour‐promoting phorbol esters. The enzyme is a family of proteins with closely but distinct structures and individual enzymological properties. Members of the family are differently distributed in particular cell types and limited intracellular locations from lower organisms to mammalian tissues. The enzyme appears to interact with many signalling pathways, and display functions in the processing and modulation of cellular responses to external stimuli. Presumably, each member of the family plays discrete roles in the control of a variety of membrane functions and activation of gene transcription.
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Citations
Cites
Castagna, M., Takai, Y., Kaibuchi, K., Sano, K., Kikkawa, U., & Nishizuka, Y. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34459-4 · Cited by 4,725
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Control of aldosterone secretion: a model for convergence in cellular signaling pathways
SPÄT, A., & HUNYADY, L. (2004) · Physiological Reviews · doi:10.1152/physrev.00030.2003 · Cited by 494
Metadata
- Authors
- Farago, A., & Nishizuka, Y.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1990-08
- Volume
- 268
- Issue
- 2
- Pages
- 350-354
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2047347345
- Cited by
- 195
- References
- 1
- FWCI
- 12.70
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Farago, A., & Nishizuka, Y. (1990). Protein kinase C in transmembrane signalling. FEBS Letters. https://doi.org/10.1016/0014-5793(90)81284-u
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
