Dissecting how ALS-associated D290V mutation enhances pathogenic aggregation of hnRNPA2286–291 peptides: Dynamics and conformational ensembles
The aggregation of RNA binding proteins, including hnRNPA1/2, TDP-43 and FUS, is
heavily implicated in causing or increasing disease risk for a series of neurodegenerative …
heavily implicated in causing or increasing disease risk for a series of neurodegenerative …
Dissecting how ALS-associated D290V mutation enhances pathogenic aggregation of hnRNPA2286-291 peptides: Dynamics and conformational ensembles
Y Tan, Y Chen, X Liu, Y Tang, Z Lao… - International journal of … - pubmed.ncbi.nlm.nih.gov
The aggregation of RNA binding proteins, including hnRNPA1/2, TDP-43 and FUS, is
heavily implicated in causing or increasing disease risk for a series of neurodegenerative …
heavily implicated in causing or increasing disease risk for a series of neurodegenerative …
Dissecting how ALS-associated D290V mutation enhances pathogenic aggregation of hnRNPA2286-291 peptides: Dynamics and conformational ensembles.
Y Tan, Y Chen, X Liu, Y Tang, Z Lao… - International Journal of …, 2023 - europepmc.org
The aggregation of RNA binding proteins, including hnRNPA1/2, TDP-43 and FUS, is
heavily implicated in causing or increasing disease risk for a series of neurodegenerative …
heavily implicated in causing or increasing disease risk for a series of neurodegenerative …