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 …

SOD1 in ALS: taking stock in pathogenic mechanisms and the role of glial and muscle cells

C Peggion, V Scalcon, ML Massimino, K Nies… - Antioxidants, 2022 - mdpi.com
Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disorder characterized by
the loss of motor neurons in the brain and spinal cord. While the exact causes of ALS are still …

Cryo-EM structure of an amyloid fibril formed by full-length human SOD1 reveals its conformational conversion

LQ Wang, Y Ma, HY Yuan, K Zhao, MY Zhang… - Nature …, 2022 - nature.com
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease. Misfolded Cu, Zn-
superoxide dismutase (SOD1) has been linked to both familial and sporadic ALS. SOD1 …

Large SOD1 aggregates, unlike trimeric SOD1, do not impact cell viability in a model of amyotrophic lateral sclerosis

C Zhu, MV Beck, JD Griffith… - Proceedings of the …, 2018 - National Acad Sciences
Aberrant accumulation of misfolded Cu, Zn superoxide dismutase (SOD1) is a hallmark of
SOD1-associated amyotrophic lateral sclerosis (ALS), an invariably fatal neurodegenerative …

Amyotrophic lateral sclerosis: proteins, proteostasis, prions, and promises

L McAlary, YL Chew, JS Lum, NJ Geraghty… - Frontiers in Cellular …, 2020 - frontiersin.org
Amyotrophic lateral sclerosis (ALS) is characterized by the progressive degeneration of the
motor neurons that innervate muscle, resulting in gradual paralysis and culminating in the …

Role of charged residues of the “electrostatic loop” of hSOD1 in promotion of aggregation: Implications for the mechanism of ALS-associated mutations under …

E Mavadat, B Seyedalipour, S Hosseinkhani… - International Journal of …, 2023 - Elsevier
Protein misfolding and amyloid formation are hallmarks of numerous diseases, including
amyotrophic lateral sclerosis (ALS), in which hSOD1 aggregation is involved in …

Structural insights into the role of reduced cysteine residues in SOD1 amyloid filament formation

Y Baek, H Kim, D Lee, D Kim, E Jo, SH Roh… - Proceedings of the …, 2025 - pnas.org
The formation of superoxide dismutase 1 (SOD1) filaments has been implicated in
amyotrophic lateral sclerosis (ALS). Although the disulfide bond formed between Cys57 and …

A systematic and comprehensive review on disease-causing genes in amyotrophic lateral sclerosis

E Srinivasan, R Rajasekaran - Journal of Molecular Neuroscience, 2020 - Springer
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disorder and is characterized by
degeneration and axon loss from the upper motor neuron, that descends from the lower …

Tailoring the positive and negative solvatochromism for chalcone analogues to detect heterozygous protein co-aggregation

B Yulong, W Wang, H Yanan, W Jichun… - Chemical …, 2023 - pubs.rsc.org
It is rare for one fluorophore scaffold to harbor both positive and negative solvatochromism.
Herein, we tailor chalcone analogues to achieve both positive-and negative-polarity …

Tryptophan 32 mediates SOD1 toxicity in a in vivo motor neuron model of ALS and is a promising target for small molecule therapeutics

MG DuVal, VK Hinge, N Snyder, R Kanyo… - Neurobiology of …, 2019 - Elsevier
SOD1 misfolding, toxic gain of function, and spread are proposed as a pathological basis of
amyotrophic lateral sclerosis (ALS), but the nature of SOD1 toxicity has been difficult to …