1,2-dioleoyl-sn-glycero-3-phosphoglycerol has been researched along with Parkinson Disease in 3 studies
*Parkinson Disease: A progressive, degenerative neurologic disease characterized by a TREMOR that is maximal at rest, retropulsion (i.e. a tendency to fall backwards), rigidity, stooped posture, slowness of voluntary movements, and a masklike facial expression. Pathologic features include loss of melanin containing neurons in the substantia nigra and other pigmented nuclei of the brainstem. LEWY BODIES are present in the substantia nigra and locus coeruleus but may also be found in a related condition (LEWY BODY DISEASE, DIFFUSE) characterized by dementia in combination with varying degrees of parkinsonism. (Adams et al., Principles of Neurology, 6th ed, p1059, pp1067-75) [MeSH]
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (33.33) | 29.6817 |
| 2010's | 2 (66.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Bousset, L; Campbell, EM; Chaney, MJ; Chu, Y; Flavin, WP; Green, ZC; Kordower, JH; Melki, R; Skarpathiotis, S | 1 |
| Claessens, MM; Lindhoud, S; Semerdzhiev, SA; Stefanovic, AN; Subramaniam, V | 1 |
| Fischer, P; Herrmann, A; Stöckl, M; Wanker, E | 1 |
3 other study(ies) available for 1,2-dioleoyl-sn-glycero-3-phosphoglycerol and Parkinson Disease
| Article | Year |
|---|---|
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 |
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 |
Alpha-synuclein selectively binds to anionic phospholipids embedded in liquid-disordered domains.
Topics: alpha-Synuclein; Amino Acid Sequence; Anions; Binding Sites; Cell Membrane; Fatty Acids; Fluorescent Dyes; Hydrophobic and Hydrophilic Interactions; Lipids; Microscopy, Fluorescence; Molecular Sequence Data; Molecular Weight; Mutation; Parkinson Disease; Phosphatidic Acids; Phosphatidylcholines; Phosphatidylglycerols; Phosphatidylinositol 4,5-Diphosphate; Phosphatidylserines; Phospholipids; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Rhodamines; Static Electricity; Surface Properties; Unilamellar Liposomes | 2008 |