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For: Gadhe L, Sakunthala A, Mukherjee S, Gahlot N, Bera R, Sawner AS, Kadu P, Maji SK. Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis. Biophys Chem 2021;281:106736. [PMID: 34923391 DOI: 10.1016/j.bpc.2021.106736] [Cited by in Crossref: 10] [Cited by in F6Publishing: 9] [Article Influence: 5.0] [Reference Citation Analysis]
Number Citing Articles
1 Mukherjee S, Sakunthala A, Gadhe L, Poudyal M, Sawner AS, Kadu P, Maji SK. Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis. J Mol Biol 2023;435:167713. [PMID: 35787838 DOI: 10.1016/j.jmb.2022.167713] [Cited by in Crossref: 4] [Cited by in F6Publishing: 4] [Article Influence: 4.0] [Reference Citation Analysis]
2 Ge WY, Deng X, Shi WP, Lin WJ, Chen LL, Liang H, Wang XT, Zhang TD, Zhao FZ, Guo WH, Yin DC. Amyloid Protein Cross-Seeding Provides a New Perspective on Multiple Diseases In Vivo. Biomacromolecules 2023;24:1-18. [PMID: 36507729 DOI: 10.1021/acs.biomac.2c01233] [Reference Citation Analysis]
3 Poudyal M, Sakunthala A, Mukherjee S, Gadhe L, Maji S. Phase separation and other forms of α-Synuclein self-assemblies. Essays in Biochemistry 2022. [DOI: 10.1042/ebc20220055] [Reference Citation Analysis]
4 Slekiene N, Snitka V, Bruzaite I, Ramanavicius A. Influence of TiO2 and ZnO Nanoparticles on α-Synuclein and β-Amyloid Aggregation and Formation of Protein Fibrils. Materials 2022;15:7664. [DOI: 10.3390/ma15217664] [Reference Citation Analysis]
5 Li M, Fan Y, Li Q, Wang X, Zhao L, Zhu M, Schroder N. Liquid-Liquid Phase Separation Promotes Protein Aggregation and Its Implications in Ferroptosis in Parkinson’s Disease Dementia. Oxidative Medicine and Cellular Longevity 2022;2022:1-13. [DOI: 10.1155/2022/7165387] [Reference Citation Analysis]
6 Brender JR, Ramamoorthy A, Gursky O, Bhunia A. Intrinsic disorder and structural biology: Searching where the light isn't. Biophysical Chemistry 2022. [DOI: 10.1016/j.bpc.2022.106912] [Reference Citation Analysis]
7 Goloborshcheva VV, Kucheryanu VG, Voronina NA, Teterina EV, Ustyugov AA, Morozov SG. Synuclein Proteins in MPTP-Induced Death of Substantia Nigra Pars Compacta Dopaminergic Neurons. Biomedicines 2022;10:2278. [DOI: 10.3390/biomedicines10092278] [Reference Citation Analysis]
8 Wang Y, Wu S, Li Q, Lang W, Li W, Jiang X, Wan Z, Chen J, Wang H. Epigallocatechin-3-gallate: A phytochemical as a promising drug candidate for the treatment of Parkinson’s disease. Front Pharmacol 2022;13:977521. [DOI: 10.3389/fphar.2022.977521] [Reference Citation Analysis]
9 Kawahata I, Finkelstein DI, Fukunaga K. Pathogenic Impact of α-Synuclein Phosphorylation and Its Kinases in α-Synucleinopathies. Int J Mol Sci 2022;23:6216. [PMID: 35682892 DOI: 10.3390/ijms23116216] [Cited by in Crossref: 5] [Cited by in F6Publishing: 3] [Article Influence: 5.0] [Reference Citation Analysis]
10 Nomoto A, Nishinami S, Shiraki K. Affinity of aromatic amino acid side chains in amino acid solvents. Biophysical Chemistry 2022. [DOI: 10.1016/j.bpc.2022.106831] [Reference Citation Analysis]
11 Lan-Mark S, Miller Y. Insights into the Interactions that Trigger the Primary Nucleation of Polymorphic α-Synuclein Dimers. ACS Chem Neurosci 2022;13:370-8. [PMID: 35044156 DOI: 10.1021/acschemneuro.1c00754] [Cited by in Crossref: 3] [Cited by in F6Publishing: 2] [Article Influence: 3.0] [Reference Citation Analysis]
12 Sakunthala A, Datta D, Navalkar A, Gadhe L, Kadu P, Patel K, Mehra S, Kumar R, Chatterjee D, Sengupta K, Padinhateeri R, Maji SK. Size-dependent secondary nucleation and amplification of α-synuclein amyloid fibrils.. [DOI: 10.1101/2021.12.28.474324] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 0.5] [Reference Citation Analysis]