Reversible Protein Phosphorylation in Cell Regulation - Khandelwal, R.L.; Wang, J.H.; SpringerLink (Online service) (New York, NY : Springer US : Imprint: Springer, 1993)
R.L. Khandelwal and J.H. Wang: Preface -- Protein Kinases -- Expression, purification, characterization, and deletion mutations of phosphorylase kinase ? subunit: identification of an inhibitory domain in the ? subunit -- Interaction sites on phosphorylase kinase for calmodulin -- Preparation and functional characterization of a catalytically active fragment of phosphorylase kinase -- Development and characterization of fluorescently-labeled myosin light chain kinase calmodulin-binding domain peptides -- Autophosphorylation: a salient feature of protein kinases -- Expression of cGMP-dependent protein kinase in Escherichia coli -- Chicken smooth muscle myosin light chain kinase is acetylated on its NH2-terminal methionine -- Calcium/calmodulin-dependent protein kinase II: role in learning and memory -- In vitro substrate specificity of protein tyrosine kinases -- Protein Phosphatases -- Mutagenesis of the catalytic subunit of rabbit muscle protein phosphatase- -- Serine phosphorylation of protein tyrosine phosphatase (PTP1B) in HeLa cells in response to analogues of cAMP or diacylglycerol plus okadaic acid -- Purification and characterization of the human protein tyrosine phosphatase, PTP ?, from a baculovirus expression system -- Protein tyrosine phosphatase activity in Leishmania donovani -- Protein Phosphorylation in Signal Transduction -- The phosphorylation of stathmin by MAP kinase -- Networking with mitogen-activated protein kinases -- Interleukin-8 activates microtubule-associated protein 2 kinase (ERK1) in human neutrophils -- Signal transduction through the cAMP-dependent protein kinase -- Casein kinase II in signal transduction and cell cycle regulation -- The MAP kinase cascade. Discovery of a new signal transduction pathway -- Does the insulin-mimetic action of vanadate involve insulin receptor kinase? -- Cellular Regulation by Reversible Phosphorylation -- Phosphorylation of vertebrate nonmuscle and smooth muscle myosin heavy chains and light chains -- Phosphorylation of myosin light chain kinase: a cellular mechanism for Ca2+ desensitization -- The role of protein phosphorylation in the regulation of cyclic nucleotide phosphodiesterases -- Reversible phosphorylation of eukaryotic initiation factor 2? in response to endoplasmic reticular signaling -- On the importance of protein phosphorylation in cell cycle control -- Evidence for an extra-cellular function for protein kinase A -- In situ regulation of cell-cell communication by the cAMP-dependent protein kinase and protein kinase C -- A-Kinase Anchoring Proteins: a key to selective activation of cAMP-responsive events?.
Keywords: Biochemistry; Oncology .; Biochemistry, general; Oncology