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dc.contributor.authorSim, Dynnen_US
dc.identifier.citationSim, D. (2022). Roles of TDP-43 domains in RNA-free phase separation. Final Year Project (FYP), Nanyang Technological University, Singapore.
dc.description.abstractTAR-DNA-binding protein (TDP-43) has remained the central focus of research into Amyotrophic Lateral Sclerosis (ALS) since its discovery as the primary component of pathological inclusions in ALS patients. RNA-deficient TDP-43 was shown to demix into spherical shell-like condensates, which was suggested to be the precursor of the cytoplasmic aggregates. In this study, I investigated how each TDP-43 domain contributes to the formation of TDP-43 spherical shells. In particular, the role of the RNA recognition motifs (RRMs) during the shell-like phase separation was thoroughly examined. Self-association of TDP-43 via NTD (N-terminal domain) appeared to be crucial for the aggregation or phase separation of wild-type and RNA-binding deficient TDP-43. Notably, neither the NTD nor the LCD (low complexity domain) could phase separate when they were separate from each other. I also examined if the NTD and the LCD are transferrable to other proteins. This study will give insights into the condensation and aggregation mechanism of pathologic TDP-43.en_US
dc.publisherNanyang Technological Universityen_US
dc.subjectScience::Biological sciences::Molecular biologyen_US
dc.titleRoles of TDP-43 domains in RNA-free phase separationen_US
dc.typeFinal Year Project (FYP)en_US
dc.contributor.supervisorChoe Young Junen_US
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.description.degreeBachelor of Science in Biological Sciencesen_US
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Appears in Collections:SBS Student Reports (FYP/IA/PA/PI)
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