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Elucidating The Effect Of Myopathy-Causing Mutations And Second-Site Suppressors On Client Processing By J-Domain Proteins, Melanie Y. Pullen
Elucidating The Effect Of Myopathy-Causing Mutations And Second-Site Suppressors On Client Processing By J-Domain Proteins, Melanie Y. Pullen
Arts & Sciences Electronic Theses and Dissertations
Defects in protein quality control may lead to protein misfolding and aggregation often associated with protein conformational disorders such as Alzheimerճ Disease and Limb Girdle Muscular Dystrophy, among others. Molecular chaperones protect against protein misfolding and aggregation. A chaperone of interest is the ubiquitously expressed type II Hsp40 co-chaperone DNAJB6, which assists in protein folding and disaggregation. Mutations within the DNAJB6 G/F domain have been associated with the dominantly inherited disease Limb-Girdle Muscular Dystrophy type 1D (LGMD1D), now referred to as LGMDD1. Our collaborators recently discovered novel LGMDD1-associated mutations in the J-domain of DNAJB6. In the enclosed body of work, …