Disruption of Protein-Protein Interfaces [electronic resource] :In Search of New Inhibitors / edited by Stefano Mangani.
by Mangani, Stefano [editor.]; SpringerLink (Online service).
Material type:
Item type | Current location | Call number | Status | Date due | Barcode |
---|---|---|---|---|---|
MAIN LIBRARY | QD415-436 (Browse shelf) | Available |
Browsing MAIN LIBRARY Shelves Close shelf browser
R856-857 Ambient Assisted Living | QD95-96 Modern NMR Methodology | QA75.5-76.95 Semantic Technology | QD415-436 Disruption of Protein-Protein Interfaces | RC254-282 Advances in Nutrition and Cancer | QA564-609 Basic Algebraic Geometry 2 | TK7800-8360 Analog Filters in Nanometer CMOS |
Drug discovery by targeting protein-protein interactions -- Protein-Protein Interaction Inhibitors: case studies on small molecules and natural compounds -- Disrupting Protein-Protein Interfaces using GRID Molecular Interaction Fields -- NMR as a tool to target protein-protein interactions -- Protein-protein interactions in the solid state The troubles of crystallizing of protein- protein complexes -- Fluorescence observables and enzyme kinetics in the investigation of PPI modulation by small molecules Detection, mechanistic insight, functional consequences.
"Disruption of Protein-Protein Interfaces" reviews the latest developments and future perspectives in drug discovery at protein-protein interfaces, as well as including details of experimental and computational tools to tackle the subject, and highlighting the contribution of the Italian research community to the field. Evidence shows that blocking or modulating protein-protein interactions might lead to the development of useful new drugs. Consequently, in recent years great effort has been dedicated to unveiling the molecular details of protein-protein interfaces by structural techniques e.g. X-ray diffraction, NMR spectroscopy. This book, written and edited by leaders in the field, provides examples from the literature of successes and failures to develop drug-like molecules effective in interacting at protein-protein interfaces.
There are no comments for this item.