T
Teri G. Boulton
Researcher at University of Texas Southwestern Medical Center
Publications - 23
Citations - 7651
Teri G. Boulton is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Receptor tyrosine kinase & Glycoprotein 130. The author has an hindex of 21, co-authored 23 publications receiving 7504 citations. Previous affiliations of Teri G. Boulton include Regeneron.
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Journal ArticleDOI
ERKs: A family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
Teri G. Boulton,Steven H. Nye,David J. Robbins,Nancy Y. Ip,Elizabeth Radzlejewska,Sharon D. Morgenbesser,Ronald A. DePinho,Nikos Panayotatos,Melanie H. Cobb,George D. Yancopoulos +9 more
TL;DR: Cl cloning and characterization of two ERK1-related kinases, ERK2 and ERK3, are described and evidence suggesting that there are additional ERK family members is provided, which may serve as intermediates that depend on tyrosine phosphorylation to activate serine/threonineosphorylation cascades.
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Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors
Neil Stahl,Thomas Farruggella,Teri G. Boulton,Zhong Zhong,James E. Darnell,George D. Yancopoulos +5 more
TL;DR: Selecting particular substrates that characterize responses to the ciliary neurotrophic factor-interleukin-6 cytokine family depended not on which Jak was activated, but was instead determined by specific tyrosine-based motifs in the receptor components--gp130 and LIFR--shared by these cytokines.
Journal ArticleDOI
Association and activation of Jak-Tyk kinases by CNTF-LIF-OSM-IL-6 beta receptor components.
Neil Stahl,Teri G. Boulton,Thomas Farruggella,Nancy Y. Ip,S. Davis,Bruce A. Witthuhn,Frederick W. Quelle,Olli Silvennoinen,Giovanna Barbieri,Sandra Pellegrini,James N. Ihle,George D. Yancopoulos +11 more
TL;DR: Unlike other cytokine receptors studied to date, the receptors for the CNTF cytokine family utilize all known members of the Jak-Tyk family, but induce distinct patterns of Jak- Tyk phosphorylation in different cell lines.
Journal ArticleDOI
An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control
Teri G. Boulton,George D. Yancopoulos,Jill S. Gregory,Clive A. Slaughter,Carolyn R. Moomaw,Joan Hsu,Melanie H. Cobb +6 more
TL;DR: A protein kinase characterized by its ability to phosphorylate microtubule-associated protein-2 (MAP2), is thought to be an early intermediate in an insulin-stimulated phosphorylation cascade and in a variety of other mammalian cell responses to extracellular signals.