D
David O. Morgan
Researcher at University of California, San Francisco
Publications - 158
Citations - 30459
David O. Morgan is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Cyclin-dependent kinase & Phosphorylation. The author has an hindex of 73, co-authored 153 publications receiving 29329 citations. Previous affiliations of David O. Morgan include Aaron Diamond AIDS Research Center & University of California, Berkeley.
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Journal ArticleDOI
Principles of CDK regulation
TL;DR: The activity of cyclin-dependent kinases is controlled by four highly conserved biochemical mechanisms, forming a web of regulatory pathways unmatched in its elegance and intricacy.
Journal ArticleDOI
Cyclin-dependent kinases: engines, clocks, and microprocessors.
TL;DR: This work has shown that Cdk activity is governed by a complex network of regulatory subunits and phosphorylation events whose precise effects on Cdk conformation have been revealed by recent crystallographic studies.
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Formation and activation of a cyclin E-cdk2 complex during the G1 phase of the human cell cycle
Andrew Koff,Antonio Giordano,D Desai,Yamashita K,J. W. Harper,Stephen J. Elledge,Takeharu Nishimoto,David O. Morgan,B. R. Franza,James M. Roberts +9 more
TL;DR: Results provide further evidence that in all eukaryotes assembly of a cyclin-Cdk complex is an important step in the biochemical pathway that controls cell proliferation during G1.
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A chemical switch for inhibitor-sensitive alleles of any protein kinase
Anthony C. Bishop,Jeffrey A. Ubersax,Dejah T. Petsch,Dina Matheos,Nathanael S. Gray,Justin D. Blethrow,Eiji Shimizu,Joe Z. Tsien,Peter G. Schultz,Mark D. Rose,John L. Wood,David O. Morgan,Kevan M. Shokat,Kevan M. Shokat +13 more
TL;DR: A chemical genetic strategy for sensitizing protein kinases to cell-permeable molecules that do not inhibit wild-type kinases is described, allowing for rapid functional characterization of members of this important gene family.
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Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose
TL;DR: It is shown that replacement of one or both of the twin tyrosines (residues 1162 and 1163) with phenylalanine results in a dramatic reduction in or loss of insulin-activated autophosphorylation and kinase activity in vitro.