Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? (Q45300712)

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scientific article published in July 2000

Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson’s disease?

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English	Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?	scientific article published in July 2000	Is there a cause-and-effect relationship between α-synuclein fibrillization and Parkinson’s disease?

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

11 December 2017

Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease? (English)

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Europe PubMed Central

PubMed publication ID

11 December 2017

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Parkinson's disease

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author name string

M S Goldberg

1

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Europe PubMed Central

PubMed publication ID

11 December 2017

P T Lansbury

2

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11 December 2017

language of work or name

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publication date

1 July 2000

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11 December 2017

Nature Cell Biology

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11 December 2017

2

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11 December 2017

7

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11 December 2017

E115-9

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11 December 2017

Prospects for new restorative and neuroprotective treatments in Parkinson's disease

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New animal models for Parkinson's disease

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Neuropathology of Parkinson's disease

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Dementia with Lewy bodies

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Evolution of amyloid: what normal protein folding may tell us about fibrillogenesis and disease

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Structural neurology: are seeds at the root of neuronal degeneration?

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Parkinson disease in twins: an etiologic study

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Mutation in the alpha-synuclein gene identified in families with Parkinson's disease

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Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease

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alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies

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Synphilin-1 associates with alpha-synuclein and promotes the formation of cytosolic inclusions

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The precursor protein of non-A beta component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system

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NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded

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Accelerated in vitro fibril formation by a mutant alpha-synuclein linked to early-onset Parkinson disease

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Molecular neurobiology--a conference sponsored by the NIMH.

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Binding of alpha-synuclein to brain vesicles is abolished by familial Parkinson's disease mutation.

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Mice lacking alpha-synuclein display functional deficits in the nigrostriatal dopamine system

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Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders

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A Drosophila model of Parkinson's disease

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Amyloid fibrillogenesis: themes and variations

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Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein

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Observation of metastable Abeta amyloid protofibrils by atomic force microscopy

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Assembly of A beta amyloid protofibrils: an in vitro model for a possible early event in Alzheimer's disease

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Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid

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Contribution of somal Lewy bodies to neuronal death

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Early phenotypic changes in transgenic mice that overexpress different mutants of amyloid precursor protein in brain

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Plaque-independent disruption of neural circuits in Alzheimer's disease mouse models

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Neurological illness in transgenic mice expressing a prion protein with an insertional mutation.

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Genetic suppression of polyglutamine toxicity in Drosophila

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The ubiquitin pathway in Parkinson's disease

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Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

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Implications of macromolecular crowding for protein assembly.

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Aggregation of N-terminal huntingtin is dependent on the length of its glutamine repeats

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Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's disease

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Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1.

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Chaperones Hsp70 and Hsp40 suppress aggregate formation and apoptosis in cultured neuronal cells expressing truncated androgen receptor protein with expanded polyglutamine tract

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Analysis of the role of heat shock protein (Hsp) molecular chaperones in polyglutamine disease

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Identifiers

10.1038/35017124

1 reference

Europe PubMed Central

PubMed publication ID

11 December 2017

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

11 December 2017

ResearchGate publication ID

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