Looking at the disordered proteins through the computational microscope

P Das, S Matysiak, J Mittal - ACS central science, 2018 - ACS Publications
Intrinsically disordered proteins (IDPs) have attracted wide interest over the past decade due
to their surprising prevalence in the proteome and versatile roles in cell physiology and …

Conformational studies of pathogenic expanded polyglutamine protein deposits from Huntington's disease

I Matlahov, PCA van der Wel - Experimental biology and …, 2019 - journals.sagepub.com
Huntington's disease, like other neurodegenerative diseases, continues to lack an effective
cure. Current treatments that address early symptoms ultimately fail Huntington's disease …

Monomeric huntingtin exon 1 has similar overall structural features for wild-type and pathological polyglutamine lengths

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 …

Structural basis of huntingtin fibril polymorphism revealed by cryogenic electron microscopy of exon 1 HTT fibrils

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 …

Aggregation landscapes of Huntingtin exon 1 protein fragments and the critical repeat length for the onset of Huntington's disease

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 …

OpenAWSEM with Open3SPN2: A fast, flexible, and accessible framework for large-scale coarse-grained biomolecular simulations

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 …

A free energy barrier caused by the refolding of an oligomeric intermediate controls the lag time of amyloid formation by hIAPP

AL Serrano, JP Lomont, LH Tu… - Journal of the …, 2017 - ACS Publications
Transiently populated oligomers formed en route to amyloid fibrils may constitute the most
toxic aggregates associated with many amyloid-associated diseases. Most nucleation …

[HTML][HTML] Tadpole-like conformations of huntingtin exon 1 are characterized by conformational heterogeneity that persists regardless of polyglutamine length

EA Newcombe, KM Ruff, A Sethi, AR Ormsby… - Journal of molecular …, 2018 - Elsevier
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 …

Exploring the interplay between fibrillization and amorphous aggregation channels on the energy landscapes of tau repeat isoforms

X Chen, M Chen, NP Schafer… - Proceedings of the …, 2020 - National Acad Sciences
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 …

Distinct oligomerization and fibrillization dynamics of amyloid core sequences of amyloid-beta and islet amyloid polypeptide

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 …