D
Dennis J. Templeton
Researcher at University of Virginia
Publications - 57
Citations - 7612
Dennis J. Templeton is an academic researcher from University of Virginia. The author has contributed to research in topics: Kinase & MAP kinase kinase kinase. The author has an hindex of 41, co-authored 57 publications receiving 7325 citations. Previous affiliations of Dennis J. Templeton include Case Western Reserve University & Baylor College of Medicine.
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Keap1 is a redox-regulated substrate adaptor protein for a Cul3-dependent ubiquitin ligase complex.
TL;DR: The results suggest that the ability of Keap1 to assemble into a functional E3 ubiquitin ligase complex is the critical determinant that controls steady-state levels of Nrf2 in response to cancer-preventive compounds and oxidative stress.
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The role of c-Jun N-terminal kinase (JNK) in apoptosis induced by ultraviolet C and gamma radiation. Duration of JNK activation may determine cell death and proliferation.
TL;DR: The data revealed the requirement of the JNK pathway in radiation-induced apoptosis and implicated the importance of the duration of JNK activation in determining the cell fates.
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Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
Mlnhong Yan,Tianang Dai,Joseph C. Deak,John M. Kyriakis,Leonard I. Zon,James R. Woodgett,Dennis J. Templeton +6 more
TL;DR: Induction of MEKK does not result in the activation of MAPK, but instead stimulates the stress-activated protein kinases (SAPKs)6–8 which are identical to a Jun amino-terminal kinase9,10 which in turn phosphorylates and activates SAPK.
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Activation of SAPK/JNK by TNF Receptor 1 Through a Noncytotoxic TRAF2-Dependent Pathway
Gioacchino Natoli,Antonio Costanzo,Angelo Ianni,Dennis J. Templeton,James R. Woodgett,Clara Balsano,Massimo Levrero +6 more
TL;DR: TNF-induced activation of the stress-activated protein kinase (SAPK) was shown to occur through a noncytotoxic TRAF2-dependent pathway, which means SAPK activation occurs through a pathway that is not required for TNF-R1-induced apoptosis.
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Amino acid-induced translation of TOP mRNAs is fully dependent on phosphatidylinositol 3-kinase-mediated signaling, is partially inhibited by rapamycin, and is independent of S6K1 and rpS6 phosphorylation.
Hua Tang,Eran Hornstein,Miri Stolovich,Galit Levy,Mark Livingstone,Dennis J. Templeton,Joseph Avruch,Oded Meyuhas +7 more
TL;DR: It appears that translational regulation of TOP mRNAs, at least by amino acids, is fully dependent on PI3-kinase, is partially sensitive to rapamycin, and requires neither S6K1 activity nor rpS6 phosphorylation.