The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Isoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase C
Open accessAbstract
The protein kinase C (PKC) family of isoenzymes is believed to mediate a wide range of signal-transduction pathways in many different cell types. A series of bisindolylmaleimides have been evaluated as inhibitors of members of the conventional PKC family (PKCs-alpha, -beta, -gamma) and of a representative of the new, Ca(2+)-independent, PKC family, PKC-epsilon. In contrast with the indolocarbazole staurosporine, all the bisindolylmaleimides investigated showed slight selectivity for PKC-alpha over the other isoenzymes examined. In addition, bisindolylmaleimides bearing a conformationally restricted side-chain were less active as inhibitors of PKC-epsilon. Most noticeable of these was Ro 32-0432, which showed a 10-fold selectivity for PKC-alpha and a 4-fold selectivity for PKC-beta I over PKC-epsilon.
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Cites
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Potent selective inhibitors of protein kinase C
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Self-citationTissue and cellular distribution of the extended family of protein kinase C isoenzymes
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Self-citationProtein kinase C, calcium and phospholipid degradation
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Metadata
- Authors
- Wilkinson, S. E., Parker, P. J., & Nixon, J. S.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1993-09-01
- Volume
- 294
- Issue
- 2
- Pages
- 335-337
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1822066871
- Cited by
- 522
- References
- 15
- FWCI
- 6.25
- Type
- journal article
- Language
- en
- Open access
- bronze
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