S. Jakes

发表

Casein kinase II stimulates Xenopus laevis DNA topoisomerase I by physical association.

R. Benbow, G. Kordiyak, S. Jakes, 1994, Biochemistry.

Cloning and Characterization of Human Lnk, an Adaptor Protein with Pleckstrin Homology and Src Homology 2 Domains that Can Inhibit T Cell Activation1

J. Hayashi, S. Jakes, Y. Li, 2000, The Journal of Immunology.

Signaling and protein associations of a cell permeable CD40 complex in B cells.

M. Kehry, S. Jakes, S. Zoog, 2004, Molecular immunology.

Pharmacophoric pattern matching in files of 3d chemical structures: evaluation of search performance

David Bawden, S. E. Jakes, D. Bawden, 1987 .

Pim kinase substrate identification and specificity.

B. Werneburg, N. Morrice, A. Knebel, 2006, Journal of biochemistry.

Hit to lead account of the discovery of bisbenzamide and related ureidobenzamide inhibitors of Rho kinase.

C. Cywin, E. Hickey, M. Kashem, 2010, Journal of medicinal chemistry.

Identification of pharmacological inhibitors of the MEK5/ERK5 pathway.

M. Kashem, R. Snow, S. Jakes, 2008, Biochemical and Biophysical Research Communications - BBRC.

Chemical influences on the specificity of tyrosine phosphorylation.

D. Graves, S. Jakes, B. Martin, 1990, The Journal of biological chemistry.

Substituted 2H-isoquinolin-1-one as potent Rho-Kinase inhibitors. Part 1: Hit-to-lead account.

C. Cywin, E. Hickey, M. Kashem, 2010, Bioorganic & medicinal chemistry letters.

Regulation of rhodopsin dephosphorylation by arrestin.

K. Palczewski, P. Hargrave, S. Jakes, 1989, The Journal of biological chemistry.

Recombinant IkappaB kinases alpha and beta are direct kinases of Ikappa Balpha.

G. W. Peet, M. Kehry, J. Li, 1998, Journal of Biological Chemistry.

Cloning and Characterization of Human Lnk, an Adaptor Protein with Pleckstrin Homology and Src Homology 2 Domains that Can Inhibit T Cell Activation

J. Hayashi, S. Jakes, J. Schembri-King, 2000 .

Histone H1 phosphorylated by protein kinase C is a selective substrate for the assay of protein phosphatase 2A in the presence of phosphatase 1.

S. Jakes, K. K. Schlender, 1988, Biochimica et biophysica acta.

Acidic residues are involved in substrate recognition by two soluble protein tyrosine phosphatases, PTP-5 and rrbPTP-1.

B. Jena, S. Jakes, T. Ingebritsen, 1993, Biochemistry.

Discovery and SAR of novel Naphthyridines as potent inhibitors of spleen tyrosine kinase (SYK).

Renee L DesJarlais, Mark R Player, R. DesJarlais, 2003, Bioorganic & medicinal chemistry letters.

Discovery of 2-phenylamino-imidazo[4,5-h]isoquinolin-9-ones: a new class of inhibitors of lck kinase.

J. Peterson, N. Moss, S. Lukas, 2002, Journal of medicinal chemistry.

Optimization of 2-phenylaminoimidazo[4,5-h]isoquinolin-9-ones: orally active inhibitors of lck kinase.

J. Peterson, S. Pav, N. Moss, 2003, Journal of medicinal chemistry.

Three Mechanistically Distinct Kinase Assays Compared: Measurement of Intrinsic ATPase Activity Identified the Most Comprehensive Set of ITK Inhibitors

Mohammed A. Kashem, Richard M. Nelson, Carol Ann Homon, 2007, Journal of biomolecular screening.

Isolation and characterization of an inhibitor-sensitive and a polycation-stimulated protein phosphatase from rat liver nuclei.

S. Jakes, R. Mellgren, K. K. Schlender, 1986, Biochimica et biophysica acta.

Hit to lead account of the discovery of a new class of inhibitors of Pim kinases and crystallographic studies revealing an unusual kinase binding mode.

C. Homon, B. Farmer, K. Qian, 2009, Journal of medicinal chemistry.

The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 beta subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site

T. Springer, S. Stacker, M. Hibbs, 1991, The Journal of experimental medicine.

Identification of actin binding protein, ABP-280, as a binding partner of human Lnk adaptor protein.

Y. Li, J. Hayashi, S. Jakes, 2000, Molecular Immunology.

Crystal structures of the human p56lck SH2 domain in complex with two short phosphotyrosyl peptides at 1.0 A and 1.8 A resolution.

T C Warren, J. King, L. Tong, 1996, Journal of molecular biology.

Determination of receptor-ligand kinetic and equilibrium binding constants using surface plasmon resonance: application to the lck SH2 domain and phosphotyrosyl peptides.

S. Jakes, R. Ingraham, R H Ingraham, 1995, Journal of medicinal chemistry.

Recombinant IκB Kinases α and β Are Direct Kinases of IκBα*

G. W. Peet, M. Kehry, K. Marcu, 1998, The Journal of Biological Chemistry.

A rationale for the design of an inhibitor of tyrosyl kinase.

C. Yuan, D. Graves, S. Jakes, 1990, The Journal of biological chemistry.

Discovery and characterization of a substrate selective p38alpha inhibitor.

C. Pargellis, B. Werneburg, S. Lukas, 2004, Biochemistry.

Pharmacophoric pattern matching in files of 3-D chemical structures: election of interatomic distance screens

Peter Willett, S. E. Jakes, P. Willett, 1986 .

Evolution of the Thienopyridine Class of Inhibitors of IκB Kinase-β: Part I: Hit-to-Lead Strategies

C. Homon, C. Cywin, Jiang-Ping Wu, 2006 .

Carboxymethyl-phenylalanine as a Replacement for Phosphotyrosine in SH2 Domain Binding*

J. Proudfoot, L. Tong, S. Lukas, 1998, The Journal of Biological Chemistry.

Interaction between the SH2 domains of ZAP-70 and the tyrosine-based activation motif 1 sequence of the zeta subunit of the T-cell receptor.

S. Lukas, S. Jakes, R. Ingraham, 1997, Archives of biochemistry and biophysics.

Ligands for the tyrosine kinase p56lck SH2 domain: discovery of potent dipeptide derivatives with monocharged, nonhydrolyzable phosphate replacements.

J. Proudfoot, L. Tong, E. Hickey, 1999, Journal of medicinal chemistry.

Binding affinities of the SH2 domains of ZAP‐70, p56/ck and Shc to the chain ITAMs of the T‐cell receptor determined by surface plasmon resonance

S. Jakes, R. Ingraham, J. Schembri-King, 1996, Journal of leukocyte biology.

Identification of the phosphoserine residue in histone H1 phosphorylated by protein kinase C

E. Reimann, S. Jakes, T. Hastings, 1988, FEBS letters.