S S Taylor

发表

Dissecting cAMP binding domain A in the RIalpha subunit of cAMP-dependent protein kinase. Distinct subsites for recognition of cAMP and the catalytic subunit.

S. Taylor, L J Huang, S S Taylor, 1998, The Journal of biological chemistry.

Structural features that specify tyrosine kinase activity deduced from homology modeling of the epidermal growth factor receptor.

J. Zheng, D. Knighton, S. Taylor, 1993, Proceedings of the National Academy of Sciences of the United States of America.

The protein kinase resource.

P E Bourne, I N Shindyalov, M Gribskov, 1997, Trends in biochemical sciences.

Kinetic analyses of mutations in the glycine-rich loop of cAMP-dependent protein kinase.

S. Taylor, I. Tsigelny, J. Adams, 1998, Biochemistry.

Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinases in vivo and in vitro.

Jonathan A. Cooper, S. Taylor, T. Hunter, 1984, The Journal of biological chemistry.

Crystal structure of the potent natural product inhibitor balanol in complex with the catalytic subunit of cAMP-dependent protein kinase.

K C Nicolaou, N. Xuong, S. Taylor, 1999, Biochemistry.

Genetically encoded reporters of protein kinase A activity reveal impact of substrate tethering

R Y Tsien, R. Tsien, S. Taylor, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Determinants of ligand binding to cAMP-dependent protein kinase.

J A McCammon, S. Taylor, J. Mccammon, 1999, Biochemistry.

A binary complex of the catalytic subunit of cAMP-dependent protein kinase and adenosine further defines conformational flexibility.

N. Xuong, S. Taylor, L. T. Ten Eyck, 1997, Structure.

Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase.

S. Taylor, F. Herberg, W. Dostmann, 1996, Biochemistry.

cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes.

Susan S. Taylor, S. Taylor, J. Buechler, 1990, Annual review of biochemistry.

Dynamics of cAMP-dependent protein kinase.

S. Taylor, P. Akamine, E. Radzio-Andzelm, 2001, Chemical reviews.

Role of the Glycine Triad in the ATP-binding Site of cAMP-dependent Protein Kinase*

S. Taylor, I. Tsigelny, W. Hemmer, 1997, The Journal of Biological Chemistry.

Three protein kinase structures define a common motif.

Susan S. Taylor, S. Taylor, E. Radzio-Andzelm, 1994, Structure.

Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase.

J. Zheng, D. Knighton, N. Xuong, 1991, Science.

Phosphorylation and activation of cAMP-dependent protein kinase by phosphoinositide-dependent protein kinase.

S. Taylor, B. Hemmings, Xiaodong Cheng, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Conserved water molecules contribute to the extensive network of interactions at the active site of protein kinase A.

S. Taylor, S. Shaltiel, S. Cox, 1998, Proceedings of the National Academy of Sciences of the United States of America.

Molecular design and biological activity of potent and selective protein kinase inhibitors related to balanol.

K C Nicolaou, S. Taylor, M. Bunnage, 1995, Chemistry & biology.

PKA: a portrait of protein kinase dynamics.

Susan S. Taylor, S. Taylor, Jian Wu, 2004, Biochimica et biophysica acta.

Crystal structure of a polyhistidine-tagged recombinant catalytic subunit of cAMP-dependent protein kinase complexed with the peptide inhibitor PKI(5-24) and adenosine.

N. Xuong, S. Taylor, S. Shaltiel, 1997, Biochemistry.

Structural adaptations of lactate dehydrogenase isozymes.

M G Rossmann, S. Taylor, M. Rossmann, 1977, Proceedings of the National Academy of Sciences of the United States of America.

Crosstalk between domains in the regulatory subunit of cAMP-dependent protein kinase: influence of amino terminus on cAMP binding and holoenzyme formation.

S. Taylor, F. Herberg, W. Dostmann, 1994, Biochemistry.