Record Display for the EPA National Library Catalog

RECORD NUMBER: 462 OF 611

Main Title Protein-Protein Interactions as New Drug Targets [electronic resource] /
Type EBOOK
Author Klussmann, Enno.
Other Authors
Author Title of a Work
Scott, John.
Publisher Springer Berlin Heidelberg,
Year Published 2008
Call Number RM1-950
ISBN 9783540728436
Subjects Medicine ; Toxicology ; Biochemistry ; Cytology
Internet Access
Description Access URL
http://dx.doi.org/10.1007/978-3-540-72843-6
Collation XV, 512 p. online resource.
Notes
Due to license restrictions, this resource is available to EPA employees and authorized contractors only
Contents Notes
Organization of Scaffolds -- A-Kinase Anchoring Proteins as the Basis for cAMP Signaling -- Arrestins as Multi-Functional Signaling Adaptors -- Role of Ena/VASP Proteins in Homeostasis and Disease -- Scaffold/Matrix Attachment Regions (S/MARs): Relevance for Disease and Therapy -- Clathrin/AP-2-Dependent Endocytosis: A Novel Playground for the Pharmacological Toolbox? -- Scaffolding Proteins and Cellular Signalling -- PDE4 Associates with Different Scaffolding Proteins: Modulating Interactions as Treatment for Certain Diseases -- G-Protein-Coupled Receptor-Signaling Components in Membrane Raft and Caveolae Microdomains -- Protein Scaffolds, Lipid Domains and Substrate Recognition in Protein Kinase C Function: Implications for Rational Drug Design -- Compartmentalised MAPK Pathways -- Dynamic Protein Complexes Regulate NF-?B Signaling -- An Oncogenic Hub: ?-Catenin as a Molecular Target for Cancer Therapeutics -- A Toolkit for Real-Time Detection of cAMP: Insights into Compartmentalized Signaling -- Cell Type-Specific Anchoring -- Scaffolding Proteins in Cardiac Myocytes -- Molecular Architecture of Signal Complexes Regulating Immune Cell Function -- Scaffolding Proteins at the Postsynaptic Density: Shank as the Architectural Framework -- Interference with Protein-Protein Interaction Sites as a New Pharmacological Concept -- Domains Mediate Protein-Protein Interactions and Nucleate Protein Assemblies -- Proline-Rich Sequence Recognition Domains (PRD): Ligands, Function and Inhibition -- Chemical Inhibition Through Conformational Stabilization of Rho GTPase Effectors -- Pharmacological Interference with Protein-Protein Interactions Mediated by Coiled-Coil Motifs -- Direct AKAP-Mediated Protein-Protein Interactions as Potential Drug Targets. Disease-relevant intracellular protein-protein interactions occurring at defined cellular sites possess great potential as drug targets. They permit highly specific pharmacological interference with defined cellular functions. Drugs targeting such interactions are likely to act with fewer side effects than conventional medication influencing whole cell functions. This book discusses therapeutically relevant protein-protein interactions with a major focus on scaffolding proteins tethering signal transduction processes to defined cellular compartments by direct protein-protein interactions. Recent advances in the development of pharmacological agents interfering with protein-protein interactions are highlighted.