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Small Heat Shock Protein 27 And Its Role In Human Disease, Bianka Andrea Holguin
Small Heat Shock Protein 27 And Its Role In Human Disease, Bianka Andrea Holguin
Open Access Theses & Dissertations
Small heat shock protein 27 (Hsp27) is a ubiquitously expressed molecular chaperone with roles in many physiological processes. As an ATP-independent molecular chaperone, Hsp27 protects substrates from irreversible aggregation and holds them in a folding competent state for later recycling into the proteome. Hsp27 proteins form dimers that are assembled into large oligomeric complexes. Phosphorylation of Hsp27 dissembles the oligomers into chaperone active dimers. Several missense mutations of Hsp27 are causative for the neurodegenerative disorders Charcot-Marie-Tooth disease 2F and distal Hereditary Motor Neuropathy IIB. Here I show that the oligomerization and chaperoning ability of Hsp27 are altered by the Hsp27 …
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 …