Samir K Maji, PhD
Affiliations: | 2009- | Biosciences and Bioengineering | Indian Institute of Technology Bombay, Mumbai, Maharashtra, India |
Area:
Neurodegenerative diseases, Synucleins, p53, amyloidWebsite:
http://www.bio.iitb.ac.in/~maji/wp/Google:
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Parents
Sign in to add mentorDavid B. Teplow | post-doc | 2005-2006 | |
Roland Riek | post-doc | 2006-2008 | ETH Zürich |
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Publications
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Ahlawat S, Mehra S, Gowda CM, et al. (2024) Solid-state NMR assignment of α-synuclein polymorph prepared from helical intermediate. Biomolecular Nmr Assignments |
Mukherjee S, Poudyal M, Dave K, et al. (2024) Protein misfolding and amyloid nucleation through liquid-liquid phase separation. Chemical Society Reviews |
Mahato J, Mukherjee R, Bose A, et al. (2023) Sensitized Emission Imaging Allows Nanoscale Surface Polarity Mapping of α-Synuclein Amyloid Fibrils. Acs Chemical Neuroscience |
Poudyal M, Sakunthala A, Mukherjee S, et al. (2022) Phase separation and other forms of α-Synuclein self-assemblies. Essays in Biochemistry |
Mahato J, Ray S, Maji SK, et al. (2022) Spectrally Resolved FRET Microscopy of α-Synuclein Phase-Separated Liquid Droplets. Methods in Molecular Biology (Clifton, N.J.). 2551: 425-447 |
Mehra S, Ahlawat S, Kumar H, et al. (2022) α-Synuclein aggregation intermediates form fibril polymorphs with distinct prion-like properties. Journal of Molecular Biology. 167761 |
Sakunthala A, Datta D, Navalkar A, et al. (2022) Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification. The Journal of Physical Chemistry Letters. 6427-6438 |
Mukherjee S, Sakunthala A, Gadhe L, et al. (2022) Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis. Journal of Molecular Biology. 167713 |
Chatterjee D, Jacob RS, Ray S, et al. (2022) Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids. Elife. 11 |
Gadhe L, Sakunthala A, Mukherjee S, et al. (2021) Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis. Biophysical Chemistry. 281: 106736 |