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.<br> Essential for the study of protein-protein interactions in vivo or in silico, and a prerequisite for successful functional proteomics studies.<br> With a prologue by Sir Tom Blundell.
INTRODUCTION<br> An overview of protein to protein interactions and protein modules<br> SH2 domain as a paradigm of protein modules<br> PROTEIN BINDING DOMAINS THAT INTERACT WITH PROLINE LIGANDS<br> SH3 domain<br> WW domain<br> EVH1 domain<br> GYF domain<br> PROTEIN BINDING DOMAINS AND THEIR REGULATION BY PHOSPHORYLATION<br> PTB domain<br> FHA domains<br> 14-3-3 proteins and phospho-serine/theronine binding modules<br> Protein kinase domains as important catalytic domains functionally linked to protein binding domains<br> PROTEIN DOMAINS REGULATING CHROMATIN FUNCTION<br> SET domains<br> Bromo domain<br> Chromo & Shadow-Chromo domains<br> PROTEIN DOMAINS RECOGNIZING SHORT PEPTIDE CORES IN THEIR LIGANDS<br> PDZ domain<br> EH domain<br> EXAMPLES OF FUNCTIONAL DIVERSITY AMONG PROTEIN DOMAINS: UBIQUITIN AND ACTIN BINDING DOMAINS<br> Ubiquitin-Binding Domains<br> CH domain<br> PHOSPHO-INOSITIDE BINDING PROTEIN DOMAINS<br> PH domain<br> VHS and ENTH domains<br> PX domain<br> DISSECTING DOMAINS AND LIGANDS WITH PEPTIDE CHEMISTRY AND COMPUTERS<br> Peptide and protein repertoires for global analysis of modules<br> Computational analysis of modular protein domains<br> Nomenclatures for protein modules and their cognate motifs<br> EPILOGUE: Future perspectives<br>
"... the book is well written and provides clear, concise and informative reviews on some of the most common domains involved in protein-peptide interactions."<br> <br> Nature Cell Biology, July 2005<br> <br> <br>
Gianni Cesareni is a Full Professor of Genetics at the University of Rome Tor Vergata (Italy). After obtaining a degree in physics at the University of Rome La Sapienza he spent three years in Cambridge in the laboratory of Sidney Brenner. He then moved to the EMBL in Heidelberg where he led a group working on the mechanisms controlling plasmid DNA replication. Since 1989 he teaches and works in Rome. He is interested in the interplay between specificity and promiscuity in the protein interaction network mediated by protein recognition modules.<br> <br> 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.<br> <br> 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.<br> <br> 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.<br> <br> All editors are members of the "Protein Module Consortium", a world-wide organization to support researchers interested in protein modules.
The definitive reference on protein modules covers all relevant modular domains mediating protein-protein interactions:<br> <br> - SH2, SH3, WW domains<br> - EVH1 and GYF domains<br> - PTB and FHA domains<br> - Protein kinase domains<br> - SET, Bromo and Chromo domains<br> - PDZ and EH domains<br> - Ubiquitin- and actin-binding domains<br> - Phosphoinositide-binding domains<br> <br> Structure, function and interaction partners of the domains are systematically treated, a general section covers methods to study protein-protein interactions on a proteome-wide scale.<br> <br>
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