Alpha-synuclein aggregation in Parkinson's disease
E Srinivasan, G Chandrasekhar… - Frontiers in …, 2021 - frontiersin.org
Parkinson's disease (PD), a neurodegenerative disorder characterized by distinct aging-
independent loss of dopaminergic neurons in substantia nigra pars compacta (SNpc) region …
independent loss of dopaminergic neurons in substantia nigra pars compacta (SNpc) region …
Advances in the understanding of protein misfolding and aggregation through molecular dynamics simulation
Aberrant protein folding known as protein misfolding is counted as one of the striking factors
of neurodegenerative diseases. The extensive range of pathologies caused by protein …
of neurodegenerative diseases. The extensive range of pathologies caused by protein …
Spontaneous formation of β-sheet nano-barrels during the early aggregation of Alzheimer's amyloid beta
Soluble low-molecular-weight oligomers formed during the early aggregation of amyloid
peptides have been hypothesized as a major toxic species of amyloidogenesis. Herein, we …
peptides have been hypothesized as a major toxic species of amyloidogenesis. Herein, we …
Amphiphilic surface chemistry of fullerenols is necessary for inhibiting the amyloid aggregation of alpha-synuclein NACore
Featuring small sizes, caged structures, low cytotoxicity and the capability to cross biological
barriers, fullerene hydroxy derivatives named fullerenols have been explored as …
barriers, fullerene hydroxy derivatives named fullerenols have been explored as …
SOD1 oligomers in amyotrophic lateral sclerosis
ES Choi, NV Dokholyan - Current opinion in structural biology, 2021 - Elsevier
Highlights•SOD1 trimers are the toxic species responsible for cell death rather than large
aggregates.•Stability of the native SOD1 dimer decreases cellular toxicity whereas …
aggregates.•Stability of the native SOD1 dimer decreases cellular toxicity whereas …
Quantum chemical and molecular mechanics studies on the assessment of interactions between resveratrol and mutant SOD1 (G93A) protein
E Srinivasan, R Rajasekaran - Journal of computer-aided molecular …, 2018 - Springer
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease that has been
associated with mutations in metalloenzyme superoxide dismutase (SOD1) causing protein …
associated with mutations in metalloenzyme superoxide dismutase (SOD1) causing protein …
Molecular binding response of naringin and naringenin to H46R mutant SOD1 protein in combating protein aggregation using density functional theory and discrete …
E Srinivasan, R Rajasekaran - Progress in biophysics and molecular …, 2019 - Elsevier
Amyotrophic lateral sclerosis (ALS) is a calamitous neurodegenerative disorder
characterized by denervation of upper and lower motor neurons. Numerous hypotheses …
characterized by denervation of upper and lower motor neurons. Numerous hypotheses …
SOD1 in amyotrophic lateral sclerosis development–in silico analysis and molecular dynamics of A4F and A4V variants
ANR Da Silva, GRC Pereira… - Journal of Cellular …, 2019 - Wiley Online Library
Amyotrophic lateral sclerosis (ALS) is a neurodegenerative disease that is characterized by
the selective loss of motor neurons. Approximately 5% to 10% of patients with ALS have a …
the selective loss of motor neurons. Approximately 5% to 10% of patients with ALS have a …
Rational design of linear tripeptides against the aggregation of human mutant SOD1 protein causing amyotrophic lateral sclerosis
E Srinivasan, R Rajasekaran - Journal of the Neurological Sciences, 2019 - Elsevier
Formation of protein aggregation is considered a hallmark feature of various neurological
diseases. Amyotrophic lateral sclerosis is one such devastating neurodegenerative disorder …
diseases. Amyotrophic lateral sclerosis is one such devastating neurodegenerative disorder …
[HTML][HTML] Discovery of Novel Inhibitors against ALS-Related SOD1 (A4V) Aggregation through the Screening of a Chemical Library Using Differential Scanning …
M Giannakou, I Akrani, A Tsoka… - …, 2024 - pmc.ncbi.nlm.nih.gov
Background: Cu/Zn Superoxide Dismutase 1 (SOD1) is a 32 kDa cytosolic dimeric
metalloenzyme that neutralizes superoxide anions into oxygen and hydrogen peroxide …
metalloenzyme that neutralizes superoxide anions into oxygen and hydrogen peroxide …