J
James E. Ferrell
Researcher at Stanford University
Publications - 146
Citations - 21933
James E. Ferrell is an academic researcher from Stanford University. The author has contributed to research in topics: Xenopus & Phosphorylation. The author has an hindex of 61, co-authored 139 publications receiving 20550 citations. Previous affiliations of James E. Ferrell include University of California, Berkeley & SRI International.
Papers
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Journal ArticleDOI
STIM Is a Ca2+ Sensor Essential for Ca2+-Store-Depletion-Triggered Ca2+ Influx
Jen Liou,Man Lyang Kim,Won Do Heo,Joshua T. Jones,Jason W. Myers,James E. Ferrell,Tobias Meyer +6 more
TL;DR: This study suggests that STIM proteins function as Ca(2+) store sensors in the signaling pathway connecting Ca(1+)-store-depletion-mediated Ca( 2+) influx, and suggests that this mutant failed to respond to store depletion.
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Mechanisms of specificity in protein phosphorylation
TL;DR: A typical protein kinase must recognize between one and a few hundred bona fide phosphorylation sites in a background of ∼700,000 potentially phosphorylatable residues.
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Ultrasensitivity in the mitogen-activated protein kinase cascade
TL;DR: It is demonstrated that the cascade arrangement has unexpected consequences for the dynamics of MAPK signaling, and MAPK is predicted to behave like a highly cooperative enzyme, even though it was not assumed that any of the enzymes in the cascade were regulated cooperatively.
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Self-perpetuating states in signal transduction: positive feedback, double-negative feedback and bistability.
TL;DR: The basic properties of bistable circuits, the requirements for construction of a satisfactorybistable switch, and the recent progress towards constructing and analysing bistables signaling systems are reviewed.
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The Biochemical Basis of an All-or-None Cell Fate Switch in Xenopus Oocytes
TL;DR: Analysis of individual oocytes showed that the response of MAPK to progesterone or Mos was equivalent to that of a cooperative enzyme with a Hill coefficient of at least 35, more than 10 times the Hill coefficient for the binding of oxygen to hemoglobin.