Conformational Behavior of Human α-Synuclein is Modulated by Familial Parkinson’s Disease Point Mutations A30P and A53T
- 9 October 2002
- journal article
- Published by Elsevier in NeuroToxicology
- Vol. 23 (4-5) , 553-567
- https://doi.org/10.1016/s0161-813x(02)00066-9
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Heparin and Other Glycosaminoglycans Stimulate the Formation of Amyloid Fibrils from α-Synuclein in VitroBiochemistry, 2002
- Fibrils Formed in Vitro from α-Synuclein and Two Mutant Forms Linked to Parkinson's Disease are Typical AmyloidBiochemistry, 2000
- Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapyProceedings of the National Academy of Sciences, 2000
- Aluminum-containing antacids as a cause of idiopathic Parkinson's diseaseMedical Hypotheses, 1999
- Effects of the mutations Ala30 to Pro and Ala53 to Thr on the physical and morphological properties of α‐synuclein protein implicated in Parkinson's diseaseFEBS Letters, 1998
- Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson diseaseNature Medicine, 1998
- Synthetic filaments assembled from C‐terminally truncated α‐synucleinFEBS Letters, 1998
- The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and diseasePublished by Elsevier ,1998
- INFRARED AND LASER‐RAMAN SPECTROSCOPIC STUDIES OF THERMALLY‐INDUCED GLOBULAR PROTEIN GELSInternational Journal of Peptide and Protein Research, 1981
- PHASE AND ELECTRON MICROSCOPIC OBSERVATIONS OF LEWY BODIES AND MELANIN GRANULES IN THE SUBSTANTIA NIGRA AND LOCUS CAERULEUS IN PARKINSONʼS DISEASEJournal of Neuropathology and Experimental Neurology, 1965