The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
The Complete Primary Structure of Protein Kinase C—the Major Phorbol Ester Receptor
Abstract
Protein kinase C, the major phorbol ester receptor, was purified from bovine brain and through the use of oligonucleotide probes based on partial amino acid sequence, complementary DNA clones were derived from bovine brain complementary DNA libraries. Thus, the complete amino acid sequence of bovine protein kinase C was determined, revealing a domain structure. At the amino terminal is a cysteine-rich domain with an internal duplication; a putative calcium-binding domain follows, and there is at the carboxyl terminal a domain that shows substantial homology, but not identity, to sequences of other protein kinase.
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Cites
The role of protein kinase C in cell surface signal transduction and tumour promotion
Nishizuka, Y. (1984) · Nature · doi:10.1038/308693a0 · Cited by 7,454
Inositol Trisphosphate, a Novel Second Messenger in Cellular Signal Transduction
Berridge, M. J., & Irvine, R. F. (1984) · Nature · doi:10.1038/312315a0 · Cited by 6,086
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
Lehrach, H., Diamond, D., Wozney, J. M., & Boedtker, H. (1977) · Biochemistry · doi:10.1021/bi00640a033 · Cited by 3,415
Ullrich, A., Coussens, L., Hayflick, J. S., Dull, T. J., Gray, A., Tam, A. W., Lee, J., Yarden, Y., Libermann, T. A., Schlessinger, J., et al. (1984) · Nature · doi:10.1038/309418a0 · Cited by 2,752
Self-citationA system for shotgun DNA sequencing
Messing, J., Crea, R., & Seeburg, P. H. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.2.309 · Cited by 2,619
Streb, H., Irvine, R. F., Berridge, M. J., & Schulz, I. (1983) · Nature · doi:10.1038/306067a0 · Cited by 2,593
Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences
Downward, J., Yarden, Y., Mayes, E., Scrace, G., Totty, N., Stockwell, P., Ullrich, A., Schlessinger, J., & Waterfield, M. D. (1984) · Nature · doi:10.1038/307521a0 · Cited by 2,516
Self-citationHunter, T., & Cooper, J. A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.004341 · Cited by 2,107
Waterfield, M. D., Scrace, G. T., Whittle, N., Stroobant, P., Johnsson, A., Wasteson, Å., Westermark, B., Heldin, C.-H., Huang, J. S., & Deuel, T. F. (1983) · Nature · doi:10.1038/304035a0 · Cited by 1,616
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The extended protein kinase C superfamily
MELLOR, H., & PARKER, P. J. (1998) · Biochemical Journal · doi:10.1042/bj3320281 · Cited by 1,538
Self-citationSelbie, L. A., Schmitz-Peiffer, C., Sheng, Y., & Biden, T. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80525-0 · Cited by 349
KSR modulates signal propagation within the MAPK cascade.
Therrien, M., Michaud, N. R., Rubin, G. M., & Morrison, D. K. (1996) · Genes & Development · doi:10.1101/gad.10.21.2684 · Cited by 257
Enzastaurin: A lesson in drug development
Bourhill, T., Narendran, A., & Johnston, R. N. (2017) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2017.02.003 · Cited by 55
Protein Kinase C as a Therapeutic Target in Non-Small Cell Lung Cancer
Sadeghi, M. M., Salama, M. F., & Hannun, Y. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115527 · Cited by 31
Metadata
- Authors
- Parker, P. J., Coussens, L., Totty, N., Rhee, L., Young, S., Chen, E., Stabel, S., Waterfield, M. D., & Ullrich, A.
- Venue
- Science
- Published
- 1986-08-22
- Volume
- 233
- Issue
- 4766
- Pages
- 853-859
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2009856702
- Cited by
- 854
- References
- 38
- FWCI
- 45.87
- Type
- journal article
- Language
- en
- Open access
- closed
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- Parker, P. J., Coussens, L., Totty, N., Rhee, L., Young, S., Chen, E., Stabel, S., Waterfield, M. D., & Ullrich, A. (1986). The Complete Primary Structure of Protein Kinase C—the Major Phorbol Ester Receptor. Science. https://doi.org/10.1126/science.3755547
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