Search Results - "Saini, Rajneet Kaur"
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Unveiling the inhibitory mechanism of peptidomimetic inhibitor against Aβ42 aggregation and protofibril disaggregation by molecular dynamics
Published in Journal of molecular liquids (01-08-2021)“…The peptidomimetic compound C1 stabilized the non-aggregation-prone helical conformation of the Aβ42 monomer. C1 destabilized the S-shaped Aβ42 protofibril…”
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Impact of Mutations on the Conformational Transition from α‑Helix to β‑Sheet Structures in Arctic-Type Aβ40: Insights from Molecular Dynamics Simulations
Published in ACS omega (15-09-2020)“…The amyloid-β (Aβ) protein aggregation into toxic oligomers and fibrils has been recognized as a key player in the pathogenesis of Alzheimer’s disease. Recent…”
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How L17A/F19A Double Mutation Diminish Aβ40 Aggregation in Alzheimer's Disease: Key Insights from Molecular Dynamics Simulations
Published in Biophysical journal (07-02-2020)Get full text
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Targeting Human Islet Amyloid Polypeptide Aggregation and Toxicity in Type 2 Diabetes: An Overview of Peptide-Based Inhibitors
Published in Chemical research in toxicology (16-11-2020)“…Type 2 diabetes (T2D) is a chronic metabolic disease characterized by insulin resistance and a progressive loss of pancreatic islet β-cell mass, which leads to…”
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Molecular insights into Aβ42 protofibril destabilization with a fluorinated compound D744: A molecular dynamics simulation study
Published in Journal of molecular recognition (01-12-2017)“…The aggregation of amyloid β‐peptide (Aβ42) into toxic oligomers, fibrils, has been identified as a key process in Alzheimer's disease (AD) progression. The…”
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Insights into the inhibitory mechanism of a resveratrol and clioquinol hybrid against Aβ42 aggregation and protofibril destabilization: A molecular dynamics simulation study
Published in Journal of biomolecular structure & dynamics (13-08-2019)“…Amyloid-β (Aβ) peptide instinctively aggregate and form plaques in the brain of Alzheimer's disease (AD) patients. At present, there is no cure or treatment…”
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Effect of Piedmont mutation (L34V) on the structure, dynamics, and aggregation of Alzheimer’s Aβ40 peptide
Published in Journal of molecular graphics & modelling (01-06-2020)“…The amyloid-β (Aβ) aggregation in the brain has been associated with the development of Alzheimer’s disease (AD). The previous studies have reported that…”
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Impact of K16A and K28A mutation on the structure and dynamics of amyloid-β42 peptide in Alzheimer's disease: key insights from molecular dynamics simulations
Published in Journal of biomolecular structure & dynamics (11-02-2020)“…The aggregation of amyloid-β 42 (Aβ 42 ) peptide into toxic oligomers and fibrils is a key step in the Alzheimer disease pathogenesis. The recent studies…”
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Molecular insights into the effect L17A/F19A double mutation on the structure and dynamics of Aβ40: A molecular dynamics simulation study
Published in Journal of cellular biochemistry (01-11-2018)“…The aggregation of amyloid‐β (Aβ) peptide has been associated with the pathogenesis of Alzheimer disease. The recent studies highlighted that L17A/F19A double…”
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10
Molecular insights into the effect L17A/F19A double mutation on the structure and dynamics of Aβ 40 : A molecular dynamics simulation study
Published in Journal of cellular biochemistry (01-11-2018)“…The aggregation of amyloid-β (Aβ) peptide has been associated with the pathogenesis of Alzheimer disease. The recent studies highlighted that L17A/F19A double…”
Get full text
Journal Article -
11
Molecular insights into Aβ 42 protofibril destabilization with a fluorinated compound D744: A molecular dynamics simulation study
Published in Journal of molecular recognition (01-12-2017)“…The aggregation of amyloid β-peptide (Aβ ) into toxic oligomers, fibrils, has been identified as a key process in Alzheimer's disease (AD) progression. The…”
Get full text
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12
Molecular insights into A[beta]42 protofibril destabilization with a fluorinated compound D744: A molecular dynamics simulation study
Published in Journal of molecular recognition (01-12-2017)“…The aggregation of amyloid [beta]-peptide (A[beta]42) into toxic oligomers, fibrils, has been identified as a key process in Alzheimer's disease (AD)…”
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13
Impact of K16A and K28A mutation on the structure and dynamics of amyloid-β 42 peptide in Alzheimer's disease: key insights from molecular dynamics simulations
Published in Journal of biomolecular structure & dynamics (11-02-2020)“…The aggregation of amyloid-β (Aβ ) peptide into toxic oligomers and fibrils is a key step in the Alzheimer disease pathogenesis. The recent studies highlighted…”
Get full text
Journal Article -
14
Insights into the inhibitory mechanism of a resveratrol and clioquinol hybrid against Aβ 42 aggregation and protofibril destabilization: A molecular dynamics simulation study
Published in Journal of biomolecular structure & dynamics (13-08-2019)“…Amyloid-β (Aβ) peptide instinctively aggregate and form plaques in the brain of Alzheimer's disease (AD) patients. At present, there is no cure or treatment…”
Get full text
Journal Article -
15
Effect of Piedmont mutation (L34V) on the structure, dynamics, and aggregation of Alzheimer's Aβ 40 peptide
Published in Journal of molecular graphics & modelling (01-06-2020)“…The amyloid-β (Aβ) aggregation in the brain has been associated with the development of Alzheimer's disease (AD). The previous studies have reported that…”
Get full text
Journal Article -
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Insights into the Inhibitory Mechanism of Dicyanovinyl‐Substituted J147 Derivative against Aβ42 Aggregation and Protofibril Destabilization: A Molecular Dynamics Simulation Study
Published in ChemistrySelect (Weinheim) (01-02-2017)“…The self‐assembly of amyloid β‐peptide (Aβ) into β‐sheet enriched fibrillar aggregates is associated with Alzheimer's disease (AD). A disease modifying therapy…”
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Insights into the Inhibitory Mechanism of Dicyanovinyl‐Substituted J147 Derivative against Aβ 42 Aggregation and Protofibril Destabilization: A Molecular Dynamics Simulation Study
Published in ChemistrySelect (Weinheim) (01-02-2017)“…The self‐assembly of amyloid β‐peptide (Aβ) into β‐sheet enriched fibrillar aggregates is associated with Alzheimer's disease (AD). A disease modifying therapy…”
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