Initial Diagnosis and Treatment Patterns in Parkinson's Disease

2010 ◽  
Vol 11 (3) ◽  
pp. B13-B14
Author(s):  
Marcy Tarrants ◽  
Maureen Lage ◽  
Marcy Tarrants ◽  
Jane Castelli-Haley
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Treatment Patterns ◽  
Initial Diagnosis ◽  
Diagnosis And Treatment

Multiparity after an initial diagnosis of Parkinson's disease: a report on a rare case

2008 ◽  
Vol 90 (5) ◽  
pp. 2005.e1-2005.e2 ◽  
Author(s):  
Raimundo Nonato Campos-Sousa ◽  
Kelson James Almeida ◽  
Alesse Ribeiro dos Santos ◽  
Pedro Vitor Lopes-Costa ◽  
Benedito Borges da Silva
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Rare Case ◽  
Initial Diagnosis

scholarly journals The initial diagnosis and management of Parkinson’s disease

2021 ◽  
Vol 50 (11) ◽  
pp. 793-800
Author(s):  
Sophie Waller ◽  
Laura Williams ◽  
Hugo Morales-Briceño ◽  
Victor SC Fung
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Initial Diagnosis ◽  
Diagnosis And Management

scholarly journals Cryo-EM structure of alpha-synuclein fibrils

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Ricardo Guerrero-Ferreira ◽  
Nicholas MI Taylor ◽  
Daniel Mona ◽  
Philippe Ringler ◽  
Matthias E Lauer ◽  
...  
Keyword(s):  
Electron Microscopy ◽  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Lewy Bodies ◽  
Alpha Synuclein ◽  
Diagnosis And Treatment ◽  
Lewy Neurites ◽  
Cryo Electron Microscopy ◽  
High Concentrations ◽  
Hydrophobic Cleft

Parkinson’s disease is a progressive neuropathological disorder that belongs to the class of synucleinopathies, in which the protein alpha-synuclein is found at abnormally high concentrations in affected neurons. Its hallmark are intracellular inclusions called Lewy bodies and Lewy neurites. We here report the structure of cytotoxic alpha-synuclein fibrils (residues 1–121), determined by cryo-electron microscopy at a resolution of 3.4 Å. Two protofilaments form a polar fibril composed of staggered β-strands. The backbone of residues 38 to 95, including the fibril core and the non-amyloid component region, are well resolved in the EM map. Residues 50–57, containing three of the mutation sites associated with familial synucleinopathies, form the interface between the two protofilaments and contribute to fibril stability. A hydrophobic cleft at one end of the fibril may have implications for fibril elongation, and invites for the design of molecules for diagnosis and treatment of synucleinopathies.

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