Modular Protein Domains
1. Edition October 2004
XXII, 502 Pages, Hardcover
129 Pictures (50 Colored Figures)
This unique reference covers all relevant protein domains, including SH2, SH3, PDZ, WW, PTB, EH, PH and PX. Its user-oriented concept combines broad coverage with easy retrieval of essential information, and includes a special section on Web-based tools and databases.
Essential for the study of protein-protein interactions in vivo or in silico, and for successful functional proteomics studies.
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Since the full functionality of any given protein can only be understood in terms of its interaction with other, often regulatory proteins, this unique reference source covers all relevant protein domains, including SH2, SH3, PDZ, WW, PTB, EH, PH and PX. Its user-oriented concept combines broad coverage with easy retrieval of essential information, and includes a special section on Web-based tools and databases covering protein modules and functional peptide motifs.
Essential for the study of protein-protein interactions in vivo or in silico, and a prerequisite for successful functional proteomics studies.
With a prologue by Sir Tom Blundell.
An overview of protein to protein interactions and protein modules
SH2 domain as a paradigm of protein modules
PROTEIN BINDING DOMAINS THAT INTERACT WITH PROLINE LIGANDS
PROTEIN BINDING DOMAINS AND THEIR REGULATION BY PHOSPHORYLATION
14-3-3 proteins and phospho-serine/theronine binding modules
Protein kinase domains as important catalytic domains functionally linked to protein binding domains
PROTEIN DOMAINS REGULATING CHROMATIN FUNCTION
Chromo & Shadow-Chromo domains
PROTEIN DOMAINS RECOGNIZING SHORT PEPTIDE CORES IN THEIR LIGANDS
EXAMPLES OF FUNCTIONAL DIVERSITY AMONG PROTEIN DOMAINS: UBIQUITIN AND ACTIN BINDING DOMAINS
PHOSPHO-INOSITIDE BINDING PROTEIN DOMAINS
VHS and ENTH domains
DISSECTING DOMAINS AND LIGANDS WITH PEPTIDE CHEMISTRY AND COMPUTERS
Peptide and protein repertoires for global analysis of modules
Computational analysis of modular protein domains
Nomenclatures for protein modules and their cognate motifs
EPILOGUE: Future perspectives
Nature Cell Biology, July 2005
Mario Gimona is laboratory head at the Consorzio Mario Negri Sud in Santa Maria Imbaro (Italy) and reader for molecular cell biology at the University of Salzburg (Austria). He was born in Salzburg where he also received his degrees in genetics and biochemistry, after completing his Ph.D. work in the lab of Vic Small at the Austrian Academy of Sciences. Following his post-doctoral time at the CSHL, New York (USA) with David Helfman he set up his own laboratory in Salzburg at the OeAW in 1996. His research interests revolve around the linguistic variation of functional protein modules and their role in the regulation of the actin cytoskeleton.
Marius Sudol has been an Associate Professor at the Mount Sinai School of Medicine in New York since 1995. He was instrumental in the delineation and characterization of one of the smallest protein modules, the WW domain. His work also implicated the WW domain in signaling pathways underlying several human diseases including Alzheimer's disease, hypertension and cancer. He earned a Ph.D. at The Rockefeller University in New York in 1983 and stayed at his Alma Mater as a postdoctoral fellow and faculty member until his move to Mount Sinai. Dr.Sudol has published 95 research articles and is credited as inventor on two biotechnology patents.
Michael B. Yaffe is Associate Professor of Biology at the Center for Cancer Research, Massachusetts Institute of Technology. He earned his MD and PhD degrees at Case Western Reserve University, and did residency training in general surgery, trauma and critical care medicine at Harvard Medical School. He was a post-doctoral fellow in Cell Biology at Harvard under Lewis C. Cantley, where he remained as junior faculty until moving to MIT in 2000. He is interested in signal transduction, protein phosphorylation, and phosphopeptide-binding domains, with a focus on cell cycle control, DNA damage responses, and inflammation.
All editors are members of the "Protein Module Consortium", a world-wide organization to support researchers interested in protein modules.