Classification of Protein Kinases and Phosphorylation Site Sequences: T. Hunter, Protein Kinase Classification. S.K. Hanks and A.M. Quinn, Protein Kinase Catalytic Domain Sequence Database: Identification of Conserved Features of Primary Structure and Classification of Family Members. R.B. Pearson and B.E. Kemp, Protein Kinase Phosphorylation Site Sequences and Consensus Specificity Motifs: Tabulations. Assays of Protein Kinases: C.V.C. Glover and C.D. Allis, Enzyme Activity Dot Blots for Assaying Protein Kinases. S.-L. Li, D. Sahal, and Y. Fujita-Yamaguchi, Solid-Phase Protein-Tyrosine Kinase Assays. G. Rijksen, B.A. van Oirschit, and G.E.J. Staal, Nonradioactive Assays of Protein-Tyrosine Kinase Activity Using Antiphosphotyrosine Antibodies. E. Racker, Use of Synthetic Amino Acid Polymers for Assay of Protein-Tyrosine and Protein-Serine Kinases. E. Racker and P.C. Sen, Assay of Phosphorylation of Small Substrates and of Synthetic Random Polymers That Interact Chemically with Adenosine 5prime-Triphosphate. J.E. Casnellie, Assay of Protein Kinases Using Peptides with Basic Residues for Phosphocellulose Binding. B.E. Kemp and R.B. Pearson, Design and Use of Peptide Substrates for Protein Kinases. D.R. Marshak and D. Carroll, Synthetic Peptide Substrates for Casein Kinase II. Purification of Protein Kinases: General Methods: S. Ferrari and G. Thomas, Micro and Macro Purification Methods for Protein Kinases. J.R. Woodgett, Use of Synthetic Peptides Mimicking Phosphorylation Sites for Affinity Purification of Protein-Serine Kinases. P. Jeno and G. Thomas, Affinity Purification of Protein Kinases Using Adenosine 5prime-Triphosphate, Amino Acid, and Peptide Analogs. Bacterial Protein Kinases: J.F. Hess, R.B. Bourret, and M.I. Simon, Phosphorylation Assays for Proteins of Two-Component Regulatory System Controlling Chemotaxis in Escherichia coli. K.A. Borkovich and M.I. Simon, Coupling of Receptor Function to Phosphate-Transfer Reactions in Bacterial Chemotaxis. J.-C. Cortay, D. Naaegre, and A.J. Cozzone, Analyzing Protein Phosphorylation in Prokaryotes. Protein-Serine Kinases: K. Ogita, Y. Ono, U. Kikkawa, and Y. Nishizuka, Expression, Separation, and Assay of Protein Kinase C Subspecies. P.J. Parker and R.M. Marais, Purification of Protein Kinase C Isotypes from7078v, cont. Bovine Brain: K.-P. Huang and F.L. Huang, Purification and Analysis of Protein Kinase C Isozymes. E. Erikson, J.L. Maller, and R.L. Erikson, Xenopus Ribosomal Protein S6 Kinase II. H.A. Lane and G. Thomas, Purification and Properties of Mitogen-Activated S6 Kinase from Rat Liver and 3T3 Cells. J.-C. Labbe, J.-C. Cavadore, and M. Doreaae, M-Phase-Specific CDC2 Kinase: Preparation from Starfish Oocytes and Properties. L.J. Cisek and J.L. Corden, Purification of Protein Kinases That Phosphorylate Repetitive Carboxyl-Terminal Domain of Eukaryotic RNA Polymerase II. T.C. Chambers and T.A. Langan, Purification and Properties of Growth-Associated H1 Histone Kinase. S.H. Francis, L. Wolfe, and J.D. Corbin, Purification of Type Iga and Type Igb Isozymes and Proteolyzed Type Igb Monomeric Enzyme of Guanosine Cyclic Monophosphate-Dependent Protein Kinase from Bovine Aorta. T.W. Sturgill, L.B. Ray, N.G. Anderson, and A.K. Erickson, Purification of Mitogen-Activated Protein Kinase from Epidermal Growth Factor-Treated 3T3-L1 Fibroblasts. J.L. Benovic, Purification and Characterization of ~gb-Adrenergic Receptor Kinase. D. Carling, P.R. Clarke, and D.G. Hardie, Adenosine Monophosphate-Activated Protein Kinase: Hydroxymethylylutaryl-CoA Reductase Kinase. Protein-Tyrosine Kinases: L. Radonnstrand and C.-H. Heldin, Purification of Platelet-Derived Growth Factor ~gb-Receptor from Porcine Uterus. J. Hsuan and P. Yaish, Affinity Purification of Active Epidermal Growth Factor Receptor Using Monoclonal Antibodies. Protein-Histidine Kinases: Y.-F. Wei and H.R. Matthews, Identification of Phosphohistidine in Proteins and Purification of Protein Histidine Kinases. Renaturation of Protein Kinases: J.E. Hutchcroft, M. Anostario, Jr., M.L. Harrison, and R.L. Geahlen, Renaturation and Assay of Protein Kinases after Electrophoresis in Sodium Dodecyl Sulfate-Polyacrylamide Gels. J.L. Celenza and M. Carlson, Renaturation of Protein Kinase Activity on Protein Blots. J.E. Ferrell, Jr., and G.S. Martin, Assessing Activities of Blotted Protein Kinases. S.M. Kee, C.-J. Yuan, and D.J. Graves, High-Performance Liquid Chromatographic Separation and Renaturation of Protein Kinase Subunits: Application to Catalytic Subunit of Phosphorylase Kinase. Antibodies against Protein Kinases: A. Kishimoto, N. Saito, K. Ogita, and U. Kikkawa, Preparation and Use of Protein Kinase C Subspecies-Specific Antipeptide Antibodies for Immunostaining. F.L. Huang, Y. Yoshida, and K.-P. Huang, Preparation, Characterization, and Use of Isozyme-Specific Antiprotein Kinase C Antibodies. G.M. Clinton and N.A. Brown, Generation and Use of Antipeptide Antibodies Directed against Catalytic Domain of Protein Kinases. Affinity Labeling, Chemical Probing, and Crystallization of Protein Kinases: B.E. Haley, Nucleotide Photoaffinity Labeling of Protein Kinase Subunits. J.A. Buechler, J. Toner-Webb, and S.S. Taylor, Carbodiimides as Probes for Protein Kinase Structure and Function. W.T. Miller, Peptide-Based Affinity Labeling of Adenosine Cyclic Monophosphate-Dependent Protein Kinase. J. Zheng, D.R. Knighton, J. Parello, S.S. Taylor, and J.M. Sowadski, Crystallization of Catalytic Subunit Adenosine Cyclic Monophosphate-Dependent Protein Kinase. Cloning of Genes Encoding Protein Kinases: S.K. Hanks and R.A. Lindberg, Use of Degenerate Oligonucleotide Probes to Identify Clones That Encode Protein Kinases. A.F. Wilks, Cloning Members of Protein Tyrosine Kinase Family Using Polymerase Chain Reaction. M.H. Kraus and S.A. Aaronson, Detection and Isolation of Protein-Tyrosine Kinase Genes Employing Reduced Stringency Hybridization. R.A. Lindberg and E.B. Pasquale, Isolation of cDNA Clones That Encode Active Protein-Tyrosine Kinases Using Antibodies against Phosphotyrosine. J.R. Woodgett, cDNA Cloning and Properties of Glycogen Synthase Kinase-3. Expression and Analysis of Protein Kinases Using cDNA Clones: W. Yonemoto, M.M. McGlone, L.W. Slice, and S.S. Taylor, Prokaryotic Expression of Catalytic Subunit of Adenosine Cyclic Monophosphate-Dependent7078v, cont. Protein Kinase: S.I. Rayter, Expression and Purification of Active abl Protein-Tyrosine Kinase in Escherichia coli. M.J. Zoller, K.E. Johnson, W. Yonemoto, and L. Levin, Functional Expression of Mammalian Adenosine Cyclic Monophosphate-Dependent Protein Kinase in Saccharomyces cerevisiae. M.D. Waterfield and C. Greenfield, Expression and Properties of Epidermal Growth Factor Receptor Expressed from Baculovirus Vectors. D.O. Morgan, J.M. Kaplan, J.M. Bishop, and H.E. Varmus, Production of p60c-src by Baculovirus Expression and Immunoaffinity Purification. L. Ellis and B.A. Levine, Use of Recombinant Baculoviruses and 1H NMR to Study Tyrosine Phosphorylation by Insulin Receptor Protein-Tyrosine Kinase. S. Stabel, D. Schaap, and P.J. Parker, Expression of Protein Kinase C Isotypes Using Baculovirus Vectors. J.C. Stone, M. Moran, and T. Pawson, Construction and Expression of Linker Insertion and Site-Directed Mutants of v-fps Protein-Tyrosine Kinase. Index.
This volume provides a compilation of recent methods for studying protein phosphorylation.
Biochemists, cell biologists, molecular biologists, developmental biologists, geneticists, and biophysicists.
- No. of pages:
- © Academic Press 1991
- 28th July 1991
- Academic Press
- Hardcover ISBN:
- eBook ISBN:
@from:Praise for the Series @qu:"The Methods in Enzymology series represents the gold-standard." @source:--NEUROSCIENCE @qu:"Incomparably useful." @source:--ANALYTICAL BIOCHEMISTRY @qu:"It is a true 'methods' series, including almost every detail from basic theory to sources of equipment and reagents, with timely documentation provided on each page." @source:--BIO/TECHNOLOGY @qu:"The series has been following the growing, changing and creation of new areas of science. It should be on the shelves of all libraries in the world as a whole collection." @source:--CHEMISTRY IN INDUSTRY @qu:"The appearance of another volume in that excellent series, Methods in Enzymology, is always a cause for appreciation for those who wish to successfully carry out a particular technique or prepare an enzyme or metabolic intermediate without the tiresome prospect of searching through unfamiliar literature and perhaps selecting an unproven method which is not easily reproduced." @source:--AMERICAN SOCIETY OF MICROBIOLOGY NEWS @qu:"If we had some way to find the work most often consulted in the laboratory, it could well be the multi-volume series Methods in Enzymology...a great work." @source:--ENZYMOLOGIA @qu:"A series that has established itself as a definitive reference for biochemists." @source:--JOURNAL OF CHROMATOGRAPHY
California Institute of Technology, Division of Biology, Pasadena, U.S.A.
The Salk Institute, La Jolla, CA, USA
Tony Hunter received his Ph.D. in 1969 from the University of Cambridge, England. He joined the Salk Institute in 1975 as an assistant professor and has been a professor since 1982. His current interests are the protein-tyrosine kinases of the Src and growth factor receptor families and the protein-tyrosine phosphatases that remove the phosphates added by protein-tyrosine kinases. He was elected as a Fellow of the Royal Society of London in 1987, a Fellow of the American Academy of Arts and Sciences in 1992, and as an Associate Member of the European Molecular Biology Organization in 1992.
The Salk Institute, La Jolla, California, USA
The Salk Institute, San Diego, California, U.S.A.
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