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Jorge Moscat

Researcher at Cornell University

Publications -  200
Citations -  32258

Jorge Moscat is an academic researcher from Cornell University. The author has contributed to research in topics: Protein kinase C & Signal transduction. The author has an hindex of 79, co-authored 193 publications receiving 28031 citations. Previous affiliations of Jorge Moscat include Mayo Clinic & University of Cincinnati.

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The atypical protein kinase Cs. Functional specificity mediated by specific protein adapters.

TL;DR: The details of how these adapters serve to link the a PKCs to different receptor signaling pathways and substrates in response to specific stimuli are crucial not only for developing an understanding of the roles and functions of the aPKCs themselves, but also for more generally establishing a view of how specificity in signal transduction is achieved.
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p62: a versatile multitasker takes on cancer

TL;DR: The role of protein kinase C (PKC)-interacting protein p62 has emerged as a crucial molecule in a myriad of cellular functions, such as nutrient sensing, regulator and substrate of autophagy, inducer of oxidative detoxifying proteins, and modulator of mitotic transit and genomic stability as discussed by the authors.
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zeta PKC induces phosphorylation and inactivation of I kappa B-alpha in vitro.

TL;DR: It is shown here that zeta PKC associates with and activates MKK‐MAPK in vitro, suggesting that one of the mechanisms whereby overexpression of zETA PKC leads to deregulation of cell growth may be accounted for at least in part by activation of the MKK-MAPK complex.
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Evidence for the in vitro and in vivo interaction of Ras with protein kinase C zeta.

TL;DR: The zeta isoform of protein kinase C (zeta PKC) has been shown to be involved in the maturation of Xenopus oocytes and mitogenic signaling in fibroblasts, and it is shown here that the expression of a dominant negative mutant of Ras (Asn-17) severely impairs the activation of zetaPKC in mouse fibro Blasts.
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Evidence for involvement of protein kinase C (PKC)-zeta and noninvolvement of diacylglycerol-sensitive PKCs in insulin-stimulated glucose transport in L6 myotubes.

TL;DR: The findings suggest that, whereas PKC-zeta is a reasonable candidate to participate in insulin stimulation of glucose transport, DAG-sensitive PKCs are unlikely participants.