fluorexon has been researched along with Idiopathic Parkinson Disease in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 3 (75.00) | 24.3611 |
2020's | 1 (25.00) | 2.80 |
Authors | Studies |
---|---|
Agnarsson, B; Hannestad, JK; Höök, F; Rocha, S; Wittung-Stafshede, P; Zhdanov, VP | 1 |
Bousset, L; Campbell, EM; Chaney, MJ; Chu, Y; Flavin, WP; Green, ZC; Kordower, JH; Melki, R; Skarpathiotis, S | 1 |
Apetri, M; Christiansen, G; Hrle, D; Otzen, DE; Rammes, G; Tepper, A; van Diggelen, F | 1 |
Claessens, MM; Lindhoud, S; Semerdzhiev, SA; Stefanovic, AN; Subramaniam, V | 1 |
4 other study(ies) available for fluorexon and Idiopathic Parkinson Disease
Article | Year |
---|---|
Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein.
Topics: alpha-Synuclein; Fluoresceins; Humans; Kinetics; Lipid Bilayers; Membrane Lipids; Membranes; Nerve Tissue Proteins; Neurons; Parkinson Disease; Phosphatidylglycerols; Protein Binding | 2020 |
Endocytic vesicle rupture is a conserved mechanism of cellular invasion by amyloid proteins.
Topics: alpha-Synuclein; Amyloidogenic Proteins; Animals; Autophagy; Biological Transport; Brain; Cells, Cultured; Female; Fluoresceins; Humans; Lewy Bodies; Male; Neurons; Parkinson Disease; Phosphatidylglycerols; Rats; Transport Vesicles; Unilamellar Liposomes | 2017 |
Two conformationally distinct α-synuclein oligomers share common epitopes and the ability to impair long-term potentiation.
Topics: Aldehydes; alpha-Synuclein; Animals; Circular Dichroism; Docosahexaenoic Acids; Epitopes; Fatty Acids, Unsaturated; Fluoresceins; Glutamine; Hippocampus; Humans; Light; Lipid Peroxidation; Long-Term Potentiation; Male; Mice; Mice, Inbred C57BL; Microscopy, Atomic Force; Neurons; Parkinson Disease; Protein Binding; Protein Structure, Secondary; Rats; Scattering, Radiation; Spectroscopy, Fourier Transform Infrared; Synapses | 2019 |
Oligomers of Parkinson's Disease-Related α-Synuclein Mutants Have Similar Structures but Distinctive Membrane Permeabilization Properties.
Topics: alpha-Synuclein; Cell Membrane Permeability; Fluoresceins; Humans; Membranes, Artificial; Multiprotein Complexes; Mutation, Missense; Parkinson Disease; Phosphatidylcholines; Phosphatidylethanolamines; Phosphatidylglycerols; Protein Binding; Scattering, Small Angle; X-Ray Diffraction | 2015 |