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Full-Text Articles in Biochemistry
Biochemical Characterization Of Wild-Type Hsp27 And Point Mutation S135f That Leads To Neurodegenerative Disease, Janelly Villalobos
Biochemical Characterization Of Wild-Type Hsp27 And Point Mutation S135f That Leads To Neurodegenerative Disease, Janelly Villalobos
Open Access Theses & Dissertations
HSPB1, also classified as heat shock protein 27 (Hsp27), is a small chaperone that is active in cells during stressful conditions. The chaperone can stabilize target proteins in a non-aggregated folding state and might be involved in regulation of folding and assembly of neurofilaments. There are five mutations in the genome of Hsp27 that are involved in Charcot Marie Tooth Disease (CMT). This neurodegenerative disease is characterized by the first decades of life where it slowly progresses to weakness of muscles followed by sensory loss and skeletal deformities. CMT is the most common hereditary neuromuscular disease, with an estimated rate …
The Human Mitochondrial Chaperonin: It Takes Two Single-Rings To Tango, Adrian Sergio Enriquez
The Human Mitochondrial Chaperonin: It Takes Two Single-Rings To Tango, Adrian Sergio Enriquez
Open Access Theses & Dissertations
The human mitochondrial chaperonin is a macromolecular machine that catalyzes the proper folding and assembly of newly imported mitochondrial proteins into their biologically active state. It is composed of two proteins from the highly conserved heat shock protein family, hsp10 and hsp60, that assemble into large oligomeric complexes responsible for mediating the folding of non-native polypeptides in an ATP dependent manner. In addition to its innate role in protein folding, human mitochondrial hsp60 has been implicated in numerous moonlighting cellular activities that have been linked to diseases conditions such as cancer and neurodegeneracy. In light of its cellular importance, the …