Amyloid oligomers: A joint experimental/computational perspective on Alzheimer's disease, Parkinson's disease, type II diabetes, and amyotrophic lateral sclerosis

PH Nguyen, A Ramamoorthy, BR Sahoo… - Chemical …, 2021 - ACS Publications
Protein misfolding and aggregation is observed in many amyloidogenic diseases affecting
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …

[HTML][HTML] A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins

AG Kikhney, DI Svergun - FEBS letters, 2015 - Elsevier
Small-angle X-ray scattering (SAXS) is a biophysical method to study the overall shape and
structural transitions of biological macromolecules in solution. SAXS provides low resolution …

Structural analysis of intrinsically disordered proteins by small-angle X-ray scattering

P Bernado, DI Svergun - Molecular biosystems, 2012 - pubs.rsc.org
Small-angle scattering of X-rays (SAXS) is an established method to study the overall
structure and structural transitions of biological macromolecules in solution. For folded …

Dynamic protein interaction networks and new structural paradigms in signaling

V Csizmok, AV Follis, RW Kriwacki… - Chemical …, 2016 - ACS Publications
Understanding signaling and other complex biological processes requires elucidating the
critical roles of intrinsically disordered proteins (IDPs) and regions (IDRs), which represent∼ …

A real-time surface enhanced raman spectroscopy study of plasmonic photothermal cell death using targeted gold nanoparticles

M Aioub, MA El-Sayed - Journal of the American Chemical …, 2016 - ACS Publications
Plasmonic nanoparticles are increasingly utilized in biomedical applications including
imaging, diagnostics, drug delivery, and plasmonic photothermal therapy (PPT). PPT …

[HTML][HTML] Folding versus aggregation: polypeptide conformations on competing pathways

TR Jahn, SE Radford - Archives of biochemistry and biophysics, 2008 - Elsevier
Protein aggregation has now become recognised as an important and generic aspect of
protein energy landscapes. Since the discovery that numerous human diseases are caused …

Controlling allosteric networks in proteins

NV Dokholyan - Chemical reviews, 2016 - ACS Publications
Allosteric transition, defined as conformational changes induced by ligand binding, is one of
the fundamental properties of proteins. Allostery has been observed and characterized in …

Tau local structure shields an amyloid-forming motif and controls aggregation propensity

D Chen, KW Drombosky, Z Hou, L Sari… - Nature …, 2019 - nature.com
Tauopathies are neurodegenerative diseases characterized by intracellular amyloid
deposits of tau protein. Missense mutations in the tau gene (MAPT) correlate with …

An efficient method for estimating the hydrodynamic radius of disordered protein conformations

M Nygaard, BB Kragelund, E Papaleo… - Biophysical journal, 2017 - cell.com
Intrinsically disordered proteins play important roles throughout biology, yet our
understanding of the relationship between their sequences, structural properties, and …

General purpose water model can improve atomistic simulations of intrinsically disordered proteins

PS Shabane, S Izadi, AV Onufriev - Journal of chemical theory …, 2019 - ACS Publications
Unconstrained atomistic simulations of intrinsically disordered proteins and peptides (IDP)
remain a challenge: widely used,“general purpose” water models tend to favor overly …