Folding for the Synapse [Hardcover]

Folding for the Synapse addresses the current view on how protein folding and misfolding, controlled by molecular chaperones, contribute to synapse function and dysfunction. Molecular chaperones have been studied in relation to de novo protein folding, but there is increasing awareness that chaperone function is required for the regulation of protein dynamics when functioning physiologically as an isolated moiety or part of a protein complex. This book will introduce both important concepts of folding machineries and give examples of the biological relevance of further chaperone functions.

This book addresses the current view on how protein folding and misfolding, controlled by molecular chaperones, contribute to synapse function and dysfunction. Examples of the biological relevance of further chaperone functions are included.

Introduction,- Protein Folding and Molecular Chaperones.- Transport of Proteins and Vesicles to the Synapse.- Protein Synthesis, Folding and Degradation in the Synaptic Compartment.- Synaptic Protein Interactions/Reguatlion by Molecular Chaperones.- Folding/Misfolding and Synaptic Dysfunction During Chronic Neurodegeration.

Folding for the Synapse addresses the current view on how protein folding/misfolding and its regulation by molecular chaperones contribute to synapse function and dysfunction. Molecular chaperones control de novo protein folding. However, there is increasing awareness that chaperones physiologically function to regulate protein-protein interaction cascades. This book will introduce the concept of folding machineries and also give examples of the biological relevance of further chaperone modality. Chaperones prevent misfolded proteins from accumulating into toxic intra-or extracellular aggregates in Alzheimers, Parkinsons, Huntingtons, prion, and motor neuron diseases (proteinopathies). The various disease-defining protein aggregates in these proteinopathies are indicative of ovl£(