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Neurodegenerative diseases result from damage to neuronal cells in the brain essential for cognition, coordination, mobility, and strength and affect millions of people worldwide. A rare but fatal example of these detrimental disorders includes amyotrophic lateral sclerosis (ALS), which is characterized by the degeneration of motor neurons in the brain. The true underlying cause of ALS is unknown, but it has been linked to the accumulation of TAR DNA-binding protein 43 (TDP-43) aggregates in neurons. Previous research has discovered a protein capable of suppressing these aggregates known as DnaJB. Because of the disaggregation abilities of DnaJ proteins, they present large therapeutic potential for the future treatment of ALS. There are 66 J-proteins that feature a large degree of sequence and structural divergence. However, which isoforms of DnaJB best bind to and interact with ALS disease protein aggregates is not known. Therefore, our research intends to understand which protein interactions involving DnaJB isoforms best suppress the aggregation of TDP-43. Our results could unveil further information about DnaJB binding affinity and intensity with TDP-43 in neurons. Ultimately, understanding these interactions could direct the design of a more effective, chaperone-based treatment for ALS.
Owens, Rileigh, "A Study of DnaJB6 Isoform Interactions with ALS Disease Protein TDP-43" (2023). Biology Summer Fellows. 105.
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