Protein Kinase C Protocols

Detalles Bibliográficos
Autor Corporativo: SpringerLink (Online service)
Otros Autores: Newton, Alexandra C. (Editor )
Formato: eBook
Lenguaje:English
Publicado: Totowa, NJ : Humana Press : Imprint: Humana, 2003.
Edición:1st ed. 2003.
Colección:Methods in Molecular Biology, 233
Materias:
Acceso en línea:https://doi.org/10.1385/1592593976
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040 |a Sistema de Bibliotecas del Tecnológico de Costa Rica 
245 1 0 |a Protein Kinase C Protocols  |c edited by Alexandra C. Newton. 
250 |a 1st ed. 2003. 
260 # # |a Totowa, NJ :  |b Humana Press :  |b Imprint: Humana,  |c 2003. 
300 |a XVI, 584 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 Methods in Molecular Biology,  |v 233 
505 0 |a The Ins and Outs of Protein Kinase C -- Early Studies of Protein Kinase C -- Expression and Purification -- Expression and Purification of Protein Kinase C from Insect Cells -- Expression and Purification of Protein Kinase C? from Bacteria -- Measuring the Activity of Protein Kinase C -- Complexities in Protein Kinase C Activity Assays -- Enzyme Assays for Protein Kinase C Activity -- Subcellular Translocation of Protein Kinase C -- Measuring the Interaction of Protein Kinase C with Membranes -- Measuring the Interaction of Protein Kinase C with Membranes -- Fluorescence Imaging of Protein Kinase C Translocation in Living Cells -- Measuring the Binding of Protein Kinase C to Sucrose-Loaded Vesicles -- Use of Stopped-Flow Fluorescence Spectroscopy to Measure Rapid Membrane Binding by Protein Kinase C -- [3H]Phorbol 12,13-Dibutyrate Binding Assay for Protein Kinase C and Related Proteins -- Measuring the Phosphorylation of Protein Kinase C -- Protein Kinase C Phosphorylation -- Pulse-Chase Analysis of Protein Kinase C -- PDK-1 and Protein Kinase C Phosphorylation -- In Vitro Autophosphorylation of Protein Kinase C Isozymes -- Tyrosine Phosphorylation of Protein Kinase C -- Methods to Study Dephosphorylation of Protein Kinase C In Vivo -- Phosphopeptide-Specific Antibodies to Protein Kinase C -- Identifying Protein Kinase C Substrates -- Identifying Protein Kinase C Substrates -- A Chemical Genetic Approach for the Identification of Direct Substrates of Protein Kinases -- Studying the Optimal Peptide Substrate Motifs of Protein Kinase C Using Oriented Peptide Libraries -- Structural Analysis of Protein Kinase C -- Structural Analysis of Protein Kinase C -- Bacterial Expression and Purification of C1 and C2 Domains of Protein Kinase C Isoforms -- Crystallization of the Protein Kinase C? C1B Domain -- Methods for Detecting Binding Proteins -- Methods for Detecting Binding Proteins -- Detection of Protein Kinase-Binding Partners by the Yeast Two-Hybrid Analysis -- Glutathione S-Transferase Pull-Down Assay -- Overlay Method for Detecting Protein-Protein Interactions -- An Overlay Assay for Detecting Protein Kinase C-Binding Proteins and Substrates -- Functional Proteomic Analysis of the Protein Kinase C Signaling System -- Pharmacological Probes for Protein Kinase C -- Pharmacological Probes for Protein Kinase C -- Applications of Inhibitors for Protein Kinase C and Their Isoforms -- Phorbol Esters as Probes for the Study of Protein Kinase C Function -- Irreversible Inactivation of Protein Kinase C Isozymes by Thiol-Reactive Peptide Substrate Analogs -- Genetic Approaches to Studying Protein Kinase C -- Genetic Approaches to Studying Protein Kinase C -- Animal Models in the Study of Protein Kinase C Isozymes -- Genetic Manipulation of Protein Kinase C In Vivo -- Yeast as a Host to Screen for Modulators and Regulatory Regions of Mammalian Protein Kinase C Isoforms -- Protein Kinase C in Disease -- Protein Kinase C in Disease -- Characterization of the Role of Protein Kinase C Isozymes in Colon Carcinogenesis Using Transgenic Mouse Models -- Alcohol Addiction. 
650 0 |a Biochemistry. 
650 1 4 |a Biochemistry, general. 
700 1 |a Newton, Alexandra C.  |e editor. 
710 2 |a SpringerLink (Online service) 
773 0 |t Springer eBooks 
856 4 0 |u https://doi.org/10.1385/1592593976