G
Guri Tzivion
Researcher at University of Mississippi Medical Center
Publications - 33
Citations - 4844
Guri Tzivion is an academic researcher from University of Mississippi Medical Center. The author has contributed to research in topics: Phosphorylation & MAPK/ERK pathway. The author has an hindex of 25, co-authored 32 publications receiving 4526 citations. Previous affiliations of Guri Tzivion include Harvard University & Wayne State University.
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Journal ArticleDOI
FoxO transcription factors; Regulation by AKT and 14-3-3 proteins.
TL;DR: The present review summarizes the current knowledge of FoxO regulation by AKT and 14-3-3 proteins, focusing on its mechanistic and structural aspects and discusses its crosstalk with the other FoxO regulatory mechanisms.
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14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation.
Guri Tzivion,Joseph Avruch +1 more
TL;DR: This review seeks to summarize the features of the 14-3-3 proteins critical to the phosphoserine/phosphothreonine binding function and to illustrate through specific examples several ways in which a stereotyped binding function is deployed to regulate diverse biologic functions and signal transduction pathways.
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A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
TL;DR: It is proposed that dimeric 14-3-3 is needed both to maintain Raf in an inactive state in the absence of GTP-bound Ras and to stabilize an active conformation of Raf produced during activation in vivo.
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Ras activation of the Raf kinase: tyrosine kinase recruitment of the MAP kinase cascade.
Joseph Avruch,Khokhlatchev A,John M. Kyriakis,Zhijun Luo,Guri Tzivion,Demetrios G. Vavvas,Zhang Xf +6 more
TL;DR: The way in which work from this and other laboratories on insulin signaling led to the discovery of the mammalian MAP kinase cascade and, in turn, to the identification of unique role of the Raf kinases in RTK activation of this protein (Ser/Thr) kinases cascade is summarized.
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14-3-3 proteins; bringing new definitions to scaffolding.
TL;DR: The 14-3-3 proteins are a part of an emerging family of proteins and protein domains that bind to serine/threonine-phosphorylated residues in a context specific manner, analogous to the Src homology 2 (SH2) and phospho-tyrosine binding (PTB) domains.