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Literature DB >> 12846979

Parkinson's disease and related alpha-synucleinopathies are brain amyloidoses.

Abstract

A paradigm shift in understanding Parkinson's disease (PD) and related disorders is emerging from studies showing that alpha-synuclein (AS) gene mutations cause familial PD; AS is abnormally nitrated, phosphorylated, and ubiquitinated; AS forms neuronal and glial inclusions; AS fibrillizes in vitro; and AS transgenic animals develop neurodegeneration with AS amyloid inclusions. Thus, PD and related synucleinopathies are brain amyloidoses that may share similar mechanisms and targets for drug discovery.

Entities: Disease Gene

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Year: 2003 PMID： 12846979 DOI： 10.1111/j.1749-6632.2003.tb07468.x

Source DB: PubMed Journal: Ann N Y Acad Sci ISSN： 0077-8923 Impact factor: 5.691

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Cited

43 in total

1. Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling.

Authors: Christine C Jao; Ani Der-Sarkissian; Jeannie Chen; Ralf Langen
Journal: Proc Natl Acad Sci U S A Date: 2004-05-20 Impact factor: 11.205

2. Time-course of brain oxidative damage caused by intrastriatal administration of 6-hydroxydopamine in a rat model of Parkinson's disease.

Authors: Sofía Sánchez-Iglesias; Pablo Rey; Estefanía Méndez-Alvarez; José Luis Labandeira-García; Ramón Soto-Otero
Journal: Neurochem Res Date: 2006-12-12 Impact factor: 3.996

Review 3. Amyloidogenesis of natively unfolded proteins.

Authors: Vladimir N Uversky
Journal: Curr Alzheimer Res Date: 2008-06 Impact factor: 3.498

Review 4. Inflammation in the early stages of neurodegenerative pathology.

Authors: Preeti J Khandelwal; Alexander M Herman; Charbel E-H Moussa
Journal: J Neuroimmunol Date: 2011-08-05 Impact factor: 3.478

5. Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.

Authors: Irina L Derkatch; Susan M Uptain; Tiago F Outeiro; Rajaraman Krishnan; Susan L Lindquist; Susan W Liebman
Journal: Proc Natl Acad Sci U S A Date: 2004-08-23 Impact factor: 11.205

6. Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein.

Authors: Katerina E Paleologou; Adrian W Schmid; Carla C Rospigliosi; Hai-Young Kim; Gonzalo R Lamberto; Ross A Fredenburg; Peter T Lansbury; Claudio O Fernandez; David Eliezer; Markus Zweckstetter; Hilal A Lashuel
Journal: J Biol Chem Date: 2008-03-14 Impact factor: 5.157

Parkinson's disease and related alpha-synucleinopathies are brain amyloidoses.

1. Structure of membrane-bound alpha-synuclein studied by site-directed spin labeling.

2. Time-course of brain oxidative damage caused by intrastriatal administration of 6-hydroxydopamine in a rat model of Parkinson's disease.

Review 3. Amyloidogenesis of natively unfolded proteins.

Review 4. Inflammation in the early stages of neurodegenerative pathology.

5. Effects of Q/N-rich, polyQ, and non-polyQ amyloids on the de novo formation of the [PSI+] prion in yeast and aggregation of Sup35 in vitro.

6. Phosphorylation at Ser-129 but not the phosphomimics S129E/D inhibits the fibrillation of alpha-synuclein.

7. Protein disorder in the human diseasome: unfoldomics of human genetic diseases.

8. Unfoldomics of human diseases: linking protein intrinsic disorder with diseases.

9. Effects of Various Flavonoids on the α-Synuclein Fibrillation Process.

10. Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model.