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Le Peuch, C. J., Ballester, R., Rosen, O. M. (1983) Purified rat brain calcium- and phospholipid-dependent protein kinase phosphorylates ribosomal protein S6. Proceedings of the National Academy of Sciences, 80 (22) 6858-6862 doi:10.1073/pnas.80.22.6858

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Reference TypeJournal (article/letter/editorial)
TitlePurified rat brain calcium- and phospholipid-dependent protein kinase phosphorylates ribosomal protein S6.
JournalProceedings of the National Academy of Sciences
AuthorsLe Peuch, C. J.Author
Ballester, R.Author
Rosen, O. M.Author
Year1983 (November 1)Volume80
Issue22
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.80.22.6858Search in ResearchGate
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Mindat Ref. ID1431466Long-form Identifiermindat:1:5:1431466:7
GUID0
Full ReferenceLe Peuch, C. J., Ballester, R., Rosen, O. M. (1983) Purified rat brain calcium- and phospholipid-dependent protein kinase phosphorylates ribosomal protein S6. Proceedings of the National Academy of Sciences, 80 (22) 6858-6862 doi:10.1073/pnas.80.22.6858
Plain TextLe Peuch, C. J., Ballester, R., Rosen, O. M. (1983) Purified rat brain calcium- and phospholipid-dependent protein kinase phosphorylates ribosomal protein S6. Proceedings of the National Academy of Sciences, 80 (22) 6858-6862 doi:10.1073/pnas.80.22.6858
In(1983, November) Proceedings of the National Academy of Sciences Vol. 80 (22) Proceedings of the National Academy of Sciences

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Huganir, R. L., Greengard, P. (1983) cAMP-dependent protein kinase phosphorylates the nicotinic acetylcholine receptor. Proceedings of the National Academy of Sciences, 80 (4) 1130-1134 doi:10.1073/pnas.80.4.1130
Albert, K. A., Helmer-Matyjek, E., Nairn, A. C., Muller, T. H., Haycock, J. W., Greene, L. A., Goldstein, M., Greengard, P. (1984) Calcium/phospholipid-dependent protein kinase (protein kinase C) phosphorylates and activates tyrosine hydroxylase. Proceedings of the National Academy of Sciences, 81 (24) 7713-7717 doi:10.1073/pnas.81.24.7713
Huang, K. P., Nakabayashi, H., Huang, F. L. (1986) Isozymic forms of rat brain Ca2+-activated and phospholipid-dependent protein kinase. Proceedings of the National Academy of Sciences, 83 (22) 8535-8539 doi:10.1073/pnas.83.22.8535
Blenis, J., Erikson, R. L. (1985) Regulation of a ribosomal protein S6 kinase activity by the Rous sarcoma virus transforming protein, serum, or phorbol ester. Proceedings of the National Academy of Sciences, 82 (22) 7621-7625 doi:10.1073/pnas.82.22.7621
Erikson, E., Maller, J. L. (1985) A protein kinase from Xenopus eggs specific for ribosomal protein S6. Proceedings of the National Academy of Sciences, 82 (3) 742-746 doi:10.1073/pnas.82.3.742
Chen, R H, Abate, C, Blenis, J (1993) Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase. Proceedings of the National Academy of Sciences, 90 (23) 10952-10956 doi:10.1073/pnas.90.23.10952
Ouimet, C. C., McGuinness, T. L., Greengard, P. (1984) Immunocytochemical localization of calcium/calmodulin-dependent protein kinase II in rat brain. Proceedings of the National Academy of Sciences, 81 (17) 5604-5608 doi:10.1073/pnas.81.17.5604
Bollag, G. E., Roth, R. A., Beaudoin, J., Mochly-Rosen, D., Koshland, D. E. (1986) Protein kinase C directly phosphorylates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity. Proceedings of the National Academy of Sciences, 83 (16) 5822-5824 doi:10.1073/pnas.83.16.5822
Girard, P. R., Mazzei, G. J., Wood, J. G., Kuo, J. F. (1985) Polyclonal antibodies to phospholipid/Ca2+-dependent protein kinase and immunocytochemical localization of the enzyme in rat brain. Proceedings of the National Academy of Sciences, 82 (9) 3030-3034 doi:10.1073/pnas.82.9.3030
Smith, C. J., Rubin, C. S., Rosen, O. M. (1980) Insulin-treated 3T3-L1 adipocytes and cell-free extracts derived from them incorporate 32P into ribosomal protein S6. Proceedings of the National Academy of Sciences, 77 (5) 2641-2645 doi:10.1073/pnas.77.5.2641
Rosen, O. M., Herrera, R., Olowe, Y., Petruzzelli, L. M., Cobb, M. H. (1983) Phosphorylation activates the insulin receptor tyrosine protein kinase. Proceedings of the National Academy of Sciences, 80 (11) 3237-3240 doi:10.1073/pnas.80.11.3237
 
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