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Chemical Biology & Drug Design|December 21, 2016
Protective effects of β-sheet breaker α/β-hybrid peptide against amyloid β-induced neuronal apoptosis in vitroSourav Kumar, Ashim Paul, Sourav Kalita, et al.
International Journal of Biological Macromolecules|April 18, 2020
An amyloidogenic hexapeptide from the cataract-associated γD-crystallin is a model for the full-length protein and is inhibited by naphthoquinone-tryptophan hybridsMalak Abu-Hussien, Guru KrishnaKumar Viswanathan, Esraa Haj, et al.
Chemical Science|October 4, 2017
Near UV-Visible electronic absorption originating from charged amino acids in a monomeric proteinSaumya Prasad, Imon Mandal, Shubham Singh, et al.
ACS Omega|August 29, 2019
FeCl<sub>3</sub>-Mediated Side Chain Modification of Aspartic Acid- and Glutamic Acid-Containing Peptides on a Solid SupportRajat Subhra Giri, Srinivasa Rao Manne, Gobinda Dolai, et al.
Molecules (Basel, Switzerland)|December 15, 2018
Inhibitory Effect of Naphthoquinone-Tryptophan Hybrid towards Aggregation of PAP f39 Semen AmyloidGuru KrishnaKumar Viswanathan, Satabdee Mohapatra, Ashim Paul, et al.
ACS Chemical Neuroscience|July 9, 2019
Antagonistic Activity of Naphthoquinone-Based Hybrids toward Amyloids Associated with Alzheimer's Disease and Type-2 DiabetesAshim Paul, Guru Krishnakumar Viswanathan, Satabdee Mahapatra, et al.
International Journal of Biological Macromolecules|January 9, 2022
The contribution of individual residues of an aggregative hexapeptide derived from the human γD-crystallin to its amyloidogenicityMalak Abu-Hussien, Guru Krishnakumar Viswanathan, Luba Simhaev, et al.
Frontiers in Molecular Biosciences|April 11, 2019
Novel Mannitol-Based Small Molecules for Inhibiting Aggregation of α-Synuclein Amyloids in Parkinson's DiseaseAshim Paul, Bo-Dou Zhang, Satabdee Mohapatra, et al.
Scientific Reports|February 21, 2019
Novel model of secreted human tau protein reveals the impact of the abnormal N-glycosylation of tau on its aggregation propensityYelena Losev, Ashim Paul, Moran Frenkel-Pinter, et al.
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