In silico investigation on the inhibition of Aβ42 aggregation by Aβ40 peptide by potential of mean force study M Dutta, VSK Mattaparthi Journal of Biomolecular Structure and Dynamics 36 (3), 741-752, 2018 | 13 | 2018 |
Inhibition of Aβ1–42 peptide aggregation using short ss-oligonucleotide as polyions: an in silico approach M Dutta, VSK Mattaparthi Journal of Biomolecular Structure and Dynamics 35 (7), 1401-1406, 2017 | 7 | 2017 |
A Computational Approach to Understand the Interactions Stabilizing the A beta (1-42) Oligomers M Dutta, A Deb, D Das, VSK Mattaparthi Biointerface Res. Appl. Chem 11, 8804-8817, 2021 | 3 | 2021 |
A comparative study to elucidate the inhibitory mechanism of a 6-mer fragment of amyloid-beta 42 peptide as a potential therapeutic in Alzheimer’s disease M Dutta, VSK Mattaparthi Current Science 114 (6), 1207-1213, 2018 | 3 | 2018 |
Cross-seeding interaction between amyloid β and tau protein can enhance aggregation M Dutta, R Chutia, V Satish Kumar Mattaparthi Current Biotechnology 6 (3), 273-279, 2017 | 3 | 2017 |
39 Inhibition of Aβ aggregation in Alzheimer’s disease using the poly-ion short single stranded DNA: in silico study M Dutta, MVS Kumar Journal of Biomolecular Structure and Dynamics 33 (sup1), 27-27, 2015 | 2 | 2015 |
Structural Characterization of Amyloid β17-42 Dimer by Potential of Mean Force Analysis: Insights from Molecular Dynamics Simulations M Dutta, R Chutia, V Satish Kumar Mattaparthi Protein and Peptide Letters 24 (7), 650-660, 2017 | 1 | 2017 |
In silico study on the stuctural dynamics of amyloid-β peptide (Aβ1-42), its aggregation pathway and inhibition: to control the geriatric epidemic, Alzheimer's disease M Dutta Tezpur University, 2017 | | 2017 |
Investigations on the Structural Characteristics that Seed the Aggregation of Amyloid-β 1-42 Peptide: Insights from Molecular Dynamics Simulations MDADM Kumar Current Proteomics 13 (3), 172-178, 2016 | | 2016 |