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 …
either the central nervous system or a variety of peripheral tissues. Structural and dynamic …
Superoxide dismutase 1 in health and disease: how a frontline antioxidant becomes neurotoxic
Cu/Zn superoxide dismutase (SOD1) is a frontline antioxidant enzyme catalysing superoxide
breakdown and is important for most forms of eukaryotic life. The evolution of aerobic …
breakdown and is important for most forms of eukaryotic life. The evolution of aerobic …
A Zn‐dependent structural transition of SOD1 modulates its ability to undergo phase separation
The misfolding and mutation of Cu/Zn superoxide dismutase (SOD1) is commonly
associated with amyotrophic lateral sclerosis (ALS). SOD1 can accumulate within stress …
associated with amyotrophic lateral sclerosis (ALS). SOD1 can accumulate within stress …
Stabilization of protein-protein interactions in drug discovery
Introduction: PPIs are involved in every disease and specific modulation of these PPIs with
small molecules would significantly improve our prospects of developing therapeutic agents …
small molecules would significantly improve our prospects of developing therapeutic agents …
Atomic structure of a toxic, oligomeric segment of SOD1 linked to amyotrophic lateral sclerosis (ALS)
Fibrils and oligomers are the aggregated protein agents of neuronal dysfunction in ALS
diseases. Whereas we now know much about fibril architecture, atomic structures of disease …
diseases. Whereas we now know much about fibril architecture, atomic structures of disease …
The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation
Abstract Superoxide dismutase-1 (SOD1) mutants, including those with unaltered enzymatic
activity, are known to cause amyotrophic lateral sclerosis (ALS). Several destabilizing factors …
activity, are known to cause amyotrophic lateral sclerosis (ALS). Several destabilizing factors …
Fighting against amyotrophic lateral sclerosis (ALS) with flavonoids: a computational approach to inhibit superoxide dismutase (SOD1) mutant aggregation
SM Noorbakhsh Varnosfaderani… - Journal of …, 2025 - Taylor & Francis
Protein aggregation is a biological process that occurs when proteins misfold. Misfolding
and aggregation of human superoxide dismutase (hSOD1) cause a neurodegenerative …
and aggregation of human superoxide dismutase (hSOD1) cause a neurodegenerative …
Probing structural and electronic dynamics with ultrafast electron microscopy
In this Perspective, we provide an overview of the field of ultrafast electron microscopy
(UEM). We begin by briefly discussing the emergence of methods for probing ultrafast …
(UEM). We begin by briefly discussing the emergence of methods for probing ultrafast …
Comprehensive in silico analysis and molecular dynamics of the superoxide dismutase 1 (SOD1) variants related to amyotrophic lateral sclerosis
Amyotrophic Lateral Sclerosis (ALS) is the most frequent motor neuron disorder, with a
significant social and economic burden. ALS remains incurable, and the only drugs …
significant social and economic burden. ALS remains incurable, and the only drugs …
The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis
Few proteins have come under such intense scrutiny as superoxide dismutase-1 (SOD1).
For almost a century, scientists have dissected its form, function and then later its …
For almost a century, scientists have dissected its form, function and then later its …