Reversible Protein Phosphorylation in Cell Regulation

Detalles Bibliográficos
Autor Corporativo: SpringerLink (Online service)
Otros Autores: Khandelwal, R.L. (Editor ), Wang, J.H. (Editor )
Formato: eBook
Lenguaje:English
Publicado: New York, NY : Springer US : Imprint: Springer, 1993.
Edición:1st ed. 1993.
Colección:Developments in Molecular and Cellular Biochemistry ; 11
Materias:
Acceso en línea:https://doi.org/10.1007/978-1-4615-2600-1
LEADER 03754nam a22003255i 4500
001 978-1-4615-2600-1
005 20190619073642.0
007 cr nn 008mamaa
008 121227s1993 xxu| s |||| 0|eng d
020 |a 9781461526001 
024 7 |a 10.1007/978-1-4615-2600-1  |2 doi 
040 |a Sistema de Bibliotecas del Tecnológico de Costa Rica 
245 1 0 |a Reversible Protein Phosphorylation in Cell Regulation  |c edited by R.L. Khandelwal, J.H. Wang. 
250 |a 1st ed. 1993. 
260 # # |a New York, NY :  |b Springer US :  |b Imprint: Springer,  |c 1993. 
300 |a VI, 324 p.  |b online resource. 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
338 |a online resource  |b cr  |2 rdacarrier 
490 1 |a Developments in Molecular and Cellular Biochemistry ;  |v 11 
505 0 |a 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?. 
650 0 |a Biochemistry. 
650 0 |a Oncology  . 
650 1 4 |a Biochemistry, general. 
650 2 4 |a Oncology. 
700 1 |a Khandelwal, R.L.  |e editor. 
700 1 |a Wang, J.H.  |e editor. 
710 2 |a SpringerLink (Online service) 
773 0 |t Springer eBooks 
856 4 0 |u https://doi.org/10.1007/978-1-4615-2600-1