Advances in the understanding of protein misfolding and aggregation through molecular dynamics simulation

A Rahman, B Saikia, CR Gogoi, A Baruah - Progress in Biophysics and …, 2022 - Elsevier
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 …

Neuroinflammation in amyotrophic lateral sclerosis: role of redox (dys) regulation

N D'Ambrosi, M Cozzolino, MT Carrì - Antioxidants & Redox …, 2018 - liebertpub.com
Significance: Amyotrophic lateral sclerosis (ALS) is due to degeneration of upper and lower
motor neurons in the anterior horn of the spinal cord and in the motor cortex. Mechanisms …

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 …

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 …

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 …

Molecular dynamics of interaction of Sesamin and related compounds with the cancer marker β-catenin: an in silico study

BM Cavuturu, VV Bhandare… - Journal of …, 2019 - Taylor & Francis
By virtue of their regulatory role in the biological process, certain protein–protein complexes
form potential targets for designing and discovery of drugs. Alteration set in the controlled …

Cysteine to serine conversion at 111th position renders the disaggregation and retains the stabilization of detrimental SOD1 A4V mutant against amyotrophic lateral …

E Srinivasan, R Rajasekaran - Cell biochemistry and biophysics, 2018 - Springer
Protein aggregation is a hallmark of various neurodegenerative disorders, such as
amyotrophic lateral sclerosis (ALS) in humans. Mutations in Cu/Zn superoxide dismutase …

Structural distortions due to missense mutations in human formylglycine-generating enzyme leading to multiple sulfatase deficiency

D Meshach Paul, T Chadah… - Journal of …, 2018 - Taylor & Francis
The major candidate for multiple sulfatase deficiency is a defective formylglycine-generating
enzyme (FGE). Though adequately produced, mutations in FGE stall the activation of …

Computational investigation on electrostatic loop mutants instigating destabilization and aggregation on human SOD1 protein causing amyotrophic lateral sclerosis

E Srinivasan, R Rajasekaran - The Protein Journal, 2019 - Springer
Mutations in the gene encoding Cu/Zn Superoxide Dismutase 1 (SOD1) protein are
contemplated to be a protruding reason for Amyotrophic lateral sclerosis (ALS), which leads …

Defensin-based therapeutic peptide design in attenuating V30M TTR-induced Familial Amyloid Polyneuropathy

G Chandrasekhar, H Pengyong, G Pravallika, L Hailei… - 3 Biotech, 2023 - Springer
In the present study, we aimed to formulate an effective therapeutic candidate against V30M
mutant transthyretin (TTR) protein to hinder its pathogenic misfolding. Nicotiana alata …