Muralidharan Chandrakesan

Nature of the Amyloid-β Monomer and the Monomer-Oligomer Equilibrium

Suman Nag, Bidyut Sarkar, Arkarup Bandyopadhyay et al. · Journal of Biological Chemistry · 2011 · 182 citations · Full text

Neurodegenerative Diseases, Single Molecule Biophysics, Alzheimer's Disease +12

Significant Structural Differences between Transient Amyloid‐β Oligomers and Less‐Toxic Fibrils in Regions Known To Harbor Familial Alzheimer′s Mutations

Bidyut Sarkar, Venus Singh Mithu, Bappaditya Chandra et al. · Angewandte Chemie International Edition · 2014 · 92 citations

Curcumin Alters the Salt Bridge-containing Turn Region in Amyloid β(1–42) Aggregates

Venus Singh Mithu, Bidyut Sarkar, Debanjan Bhowmik et al. · Journal of Biological Chemistry · 2014 · 65 citations · Full text

Zn++ Binding Disrupts the Asp23-Lys28 Salt Bridge without Altering the Hairpin-Shaped Cross-β Structure of Aβ42 Amyloid Aggregates

Venus Singh Mithu, Bidyut Sarkar, Debanjan Bhowmik et al. · Biophysical Journal · 2011 · 61 citations · Full text

Zn++ Binding Disrupts, Aβ42 Amyloid Aggregates, Biochemistry +8

A folding transition underlies the emergence of membrane affinity in amyloid-β

Suman Nag, Bidyut Sarkar, Muralidharan Chandrakesan et al. · Physical Chemistry Chemical Physics · 2013 · 37 citations

Proteinlipid Interaction, Protein Assembly, Tertiary Fold +14