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The Role of AAA+ Proteins in Protein Repair and Degradation
ATPases Associated with diverse cellular Activities (AAA+) comprise a superfamily of proteins that are defined by the presence of the AAA+ domain containing canonical Walker A and B motifs required for ATP binding and hydrolysis. Members of this superfamily act on other proteins, DNA, RNA, or multicomponent complexes to affect their conformation or their assembly. There have been substantial advances in understanding the structure and mechanism of function of a large number of AAA+ proteins. In this Research Topic, review articles and original research papers discuss new aspects as well as provide a detailed overview of several AAA+ proteins, namely: ClpXP, Lon, ClpB, Hsp104, p97, AAA+ proteins of the proteasome, Rubisco activases, Torsin, Pontin, and Reptin.
Pathologic Conditions of the Human Nervous and Muscular Systems Associated with Mutant Chaperones: Molecular and Mechanistic Aspects
This eBook presents illustrative examples of genetic chaperonopathies affecting primarily nerves and muscles and discusses molecular mechanisms and treatment targeting chaperones, i.e., chaperonotherapy.
Molecular Chaperones in the Cell
Interest in molecular chaperones has grown exponentially over the last decade. Molecular Chaperones recognise nascet and unfolded polypeptide chains and are often essential for their folding, proteolytic processing, intracellular targeting, and secretion. They are vital for cell growth, with key roles in processes as diverse as signal transduction and stress survival. Much work has already been done in understanding the structure and function of the major molecular chaperones, and more recently the emphasis in research has shifted towrd exploring their precise roles in many different processes with which they are involved inside the cell. This aspect of molecular chaperone biology is the foc...
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