Anthony M. Pepio - Publications
Affiliations: | 2001 | McGill University, Montreal, QC, Canada |
Year | Citation | Score | |||
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2003 | Pepio AM, Sossin WS. In vitro autophosphorylation of protein kinase C isozymes. Methods in Molecular Biology (Clifton, N.J.). 233: 191-205. PMID 12840508 DOI: 10.1385/1-59259-397-6:191 | 0.701 | |||
2002 | Pepio AM, Thibault GL, Sossin WS. Phosphoinositide-dependent kinase phosphorylation of protein kinase C Apl II increases during intermediate facilitation in aplysia. The Journal of Biological Chemistry. 277: 37116-23. PMID 12140280 DOI: 10.1074/jbc.M202264200 | 0.733 | |||
2001 | Khan A, Pepio AM, Sossin WS. Serotonin activates S6 kinase in a rapamycin-sensitive manner in Aplysia synaptosomes. The Journal of Neuroscience : the Official Journal of the Society For Neuroscience. 21: 382-91. PMID 11160419 DOI: 10.1523/Jneurosci.21-02-00382.2001 | 0.661 | |||
2001 | Pepio AM, Sossin WS. Membrane translocation of novel protein kinase Cs is regulated by phosphorylation of the C2 domain. The Journal of Biological Chemistry. 276: 3846-55. PMID 11073945 DOI: 10.1074/jbc.M006339200 | 0.715 | |||
1999 | Nakhost A, Dyer JR, Pepio AM, Fan X, Sossin WS. Protein kinase C phosphorylated at a conserved threonine is retained in the cytoplasm. The Journal of Biological Chemistry. 274: 28944-9. PMID 10506140 DOI: 10.1074/jbc.274.41.28944 | 0.701 | |||
1998 | Dyer JR, Pepio AM, Yanow SK, Sossin WS. Phosphorylation of eIF4E at a conserved serine in Aplysia. The Journal of Biological Chemistry. 273: 29469-74. PMID 9792652 DOI: 10.1074/jbc.273.45.29469 | 0.701 | |||
1998 | Pepio AM, Fan X, Sossin WS. The role of C2 domains in Ca2+-activated and Ca2+-independent protein kinase Cs in aplysia. The Journal of Biological Chemistry. 273: 19040-8. PMID 9668085 DOI: 10.1074/jbc.273.30.19040 | 0.703 | |||
1998 | Pepio AM, Sossin WS. The C2 domain of the Ca(2+)-independent protein kinase C Apl II inhibits phorbol ester binding to the C1 domain in a phosphatidic acid-sensitive manner. Biochemistry. 37: 1256-63. PMID 9477951 DOI: 10.1021/bi971841u | 0.677 | |||
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