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Proteins|November 30, 2020
Are granulins copper sequestering proteins?Anukool A Bhopatkar, Vijayaraghavan RangachariThe Journal of Biological Chemistry|January 9, 2020
Granulins modulate liquid-liquid phase separation and aggregation of the prion-like C-terminal domain of the neurodegeneration-associated protein TDP-43Anukool A Bhopatkar, Vladimir N Uversky, Vijayaraghavan RangachariProgress in Molecular Biology and Translational Science|August 24, 2020
Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functionsAnukool A Bhopatkar, Vladimir N Uversky, Vijayaraghavan RangachariBiophysical Journal|May 1, 2022
Charge and redox states modulate granulin-TDP-43 coacervation toward phase separation or aggregationAnukool A Bhopatkar, Shailendra Dhakal, Hannah G Abernathy, et al.The Biochemical Journal|February 21, 2019
Cysteine-rich granulin-3 rapidly promotes amyloid-β fibrils in both redox statesAnukool A Bhopatkar, Gaurav Ghag, Lauren M Wolf, et al.The Journal of Biological Chemistry|August 3, 2023
Flanking regions, amyloid cores, and polymorphism: the potential interplay underlying structural diversityAnukool A Bhopatkar, Rakez KayedCommunications Biology|June 21, 2023
Biomolecular condensates - extant relics or evolving microcompartments?Vijayaraghavan RangachariBMC Bioinformatics|October 16, 2010
Dynamics of protofibril elongation and association involved in Aβ42 peptide aggregation in Alzheimer's diseasePreetam Ghosh, Amit Kumar, Bhaswati Datta, et al.Mathematical Biosciences|January 17, 2016
Determination of critical nucleation number for a single nucleation amyloid-β aggregation modelPreetam Ghosh, Ashwin Vaidya, Amit Kumar, et al.Protein Expression and Purification|March 29, 2020
Cloning, expression and purification of the low-complexity region of RanBP9 proteinShailendra Dhakal, Krishna Sapkota, Faqing Huang, et al.Pageof 6