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Charcot Marie Tooth disease (CMT) and distal hereditary motor neuropathy (dHMN) are two heterogeneous and clinically overlapping diseases of the peripheral nervous system. Pathogenic mutations in various proteins including the small heat shock protein 27 (Hsp27, HSPB1) are associated with CMT and dHMN; however the molecular mechanisms underlying disease progression are not understood. Hsp27 is a ubiquitously expressed and highly conserved molecular chaperone that is involved in cytoprotective functions including protein homeostasis (proteostasis), redox modulation, inhibition of apoptosis, stabilisation of the cytoskeleton, and axonal transport. The mechanisms by which Hsp27 impacts these processes are largely unknown, as are the effects of disease-related mutations on the molecular structure and function of the protein. In an effort to better understand the roles of Hsp27 mutations in the development of CMT and dHMN, this thesis explores the effects of disease-causing mutations on the ....
The effects of the climate change including an increase in the average global temperatures, and abnormal weather events such as frequent and severe heatwaves are emerging as a worldwide ecological concern due to their impacts on plant vegetation and crop productivity. In this review, the molecular processes of plants in response to heat stress from the sensing of heat stress, the subsequent molecular cascades associated with the activation of heat shock factors and their primary targets (heat shock proteins), to the cellular responses have been summarized with an emphasis on the classification and functions of heat shock proteins. Vegetables contain many essential vitamins, minerals, antioxidants, and fibers that provide many critical health benefits to humans. The adverse effects of heat stress on vegetable growth can be alleviated by developing vegetable crops with enhanced thermotolerance with the aid of various genetic tools. To achieve this goal, a solid understanding of the molec ....
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The maintenance of cellular protein homeostasis, or proteostasis, is dependent upon a complex network of molecular chaperones, degradation machinery and other regulatory factors, which together act to keep the proteome soluble and functional. Disturbances to proteostasis can lead to protein aggregation and inclusion formation, processes associated with a variety of neurodegenerative disorders. The heat shock proteins (Hsps) are a superfamily of molecular chaperones that are dramatically upregulated in response to cellular stress. The Hsps can bind aggregation-prone proteins and either refold or traffic them for degradation. One class of Hsps, the DNAJBs, act as co-factors of the Hsp70 machine and have been previously identified as potent suppressors of disease-related protein aggregation. This has raised the potential of targeting DNAJB chaperone action in the context of protein aggregation associated with disease. In the work described in this thesis, a destabilised isoform of the ....