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Full-Text Articles in Life Sciences
Validating A New In Vivo Model To Study Als, Izabela J. Cimachowska
Validating A New In Vivo Model To Study Als, Izabela J. Cimachowska
Student Theses and Dissertations
Buildup of oxidative stress and mitochondrial dysfunction are well known characteristics of both sporadic and hereditary amyotrophic lateral sclerosis (ALS). While both forms of the disease seem to arise from common cellular dysfunction, the genetic disease is studied to a much greater extent. Engineering novel animal models of the sporadic form of the disease is crucial for development of druggable targets to treat ALS and understand the underlying mechanisms. Interestingly, accumulation of oxidative stress by exacerbated emission of reactive oxygen species (ROS) from presynaptic mitochondria is a hallmark of both hereditary and sporadic ALS. Previous work by our laboratory showed …
Diseases At Work, Alice Liu '19, Nicholas Opiola '19, Gunnar Bergmann '19, Femi Durodola '20, Suraj Sunkara '19
Diseases At Work, Alice Liu '19, Nicholas Opiola '19, Gunnar Bergmann '19, Femi Durodola '20, Suraj Sunkara '19
Human Diseases Graphic Novels
No abstract provided.
Hsp90 And Its Co-Chaperones Modify Tdp-43 Localization, Aggregation, And Toxicity, Lilian T. Lin
Hsp90 And Its Co-Chaperones Modify Tdp-43 Localization, Aggregation, And Toxicity, Lilian T. Lin
Electronic Thesis and Dissertation Repository
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease associated with protein misfolding and protein aggregation. In particular, the TAR DNA-binding protein (TDP-43) is often found in the pathological inclusions in neurons of ALS patient brains and spinal cords. This phenomenon is known as TDP-43 proteinopathy, the mislocalization of TDP-43 from the cell nucleus and the formation of aggregates in the cytoplasm. Numerous mutations in the gene encoding TDP-43 have also been linked to familial cases of ALS (fALS) and cause TDP-43 proteinopathy. This study attempts to decipher how the molecular chaperone Hsp90 and its co-chaperones, Aha1, Sti1, and Cdc37, modulate …