Huntington's disease, like other neurodegenerative diseases, continues to lack an effective cure. Current treatments that address early symptoms ultimately fail Huntington's disease …
JB Warner IV, KM Ruff, PS Tan, EA Lemke… - Journal of the …, 2017 - ACS Publications
Huntington's disease is caused by expansion of a polyglutamine (polyQ) domain within exon 1 of the huntingtin gene (Httex1). The prevailing hypothesis is that the monomeric Httex1 …
S Nazarov, A Chiki, D Boudeffa… - Journal of the American …, 2022 - ACS Publications
The lack of detailed insight into the structure of aggregates formed by the huntingtin protein (HTT) has hampered the efforts to develop therapeutics and diagnostics targeting pathology …
M Chen, PG Wolynes - … of the National Academy of Sciences, 2017 - National Acad Sciences
Huntington's disease (HD) is a neurodegenerative disease caused by an abnormal expansion in the polyglutamine (polyQ) track of the Huntingtin (HTT) protein. The severity of …
W Lu, C Bueno, NP Schafer, J Moller… - PLoS computational …, 2021 - journals.plos.org
We present OpenAWSEM and Open3SPN2, new cross-compatible implementations of coarse-grained models for protein (AWSEM) and DNA (3SPN2) molecular dynamics …
Transiently populated oligomers formed en route to amyloid fibrils may constitute the most toxic aggregates associated with many amyloid-associated diseases. Most nucleation …
Abstract Soluble huntingtin exon 1 (Httex1) with expanded polyglutamine (polyQ) engenders neurotoxicity in Huntington's disease. To uncover the physical basis of this toxicity, we …
Filaments made up of different isoforms of tau protein are associated with a variety of neurodegenerative diseases. Filaments made up of the 4R-tau isoform, which has four …
Y Sun, B Wang, X Ge, F Ding - Physical Chemistry Chemical Physics, 2017 - pubs.rsc.org
A direct observation of amyloid aggregation from isolated peptides to cross-β fibrils is crucial for understanding the nucleation-dependence process, but the corresponding macroscopic …