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fluorexon and Idiopathic Parkinson Disease

fluorexon has been researched along with Idiopathic Parkinson Disease in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's0 (0.00)29.6817
2010's3 (75.00)24.3611
2020's1 (25.00)2.80

Authors

AuthorsStudies
Agnarsson, B; Hannestad, JK; Höök, F; Rocha, S; Wittung-Stafshede, P; Zhdanov, VP1
Bousset, L; Campbell, EM; Chaney, MJ; Chu, Y; Flavin, WP; Green, ZC; Kordower, JH; Melki, R; Skarpathiotis, S1
Apetri, M; Christiansen, G; Hrle, D; Otzen, DE; Rammes, G; Tepper, A; van Diggelen, F1
Claessens, MM; Lindhoud, S; Semerdzhiev, SA; Stefanovic, AN; Subramaniam, V1

Other Studies

4 other study(ies) available for fluorexon and Idiopathic Parkinson Disease

ArticleYear
Single-vesicle imaging reveals lipid-selective and stepwise membrane disruption by monomeric α-synuclein.
    Proceedings of the National Academy of Sciences of the United States of America, 2020, 06-23, Volume: 117, Issue:25

    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.
    Acta neuropathologica, 2017, Volume: 134, Issue:4

    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.
    PloS one, 2019, Volume: 14, Issue:3

    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.
    Biochemistry, 2015, May-26, Volume: 54, Issue:20

    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