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A close association of torsinA and α-synuclein in Lewy bodies a fluorescence resonance energy transf...

A close association of torsinA and α-synuclein in Lewy bodies a fluorescence resonance energy transf...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1850427

A close association of torsinA and α-synuclein in Lewy bodies a fluorescence resonance energy transfer study

About this item

Full title

A close association of torsinA and α-synuclein in Lewy bodies a fluorescence resonance energy transfer study

Publisher

Bethesda, MD: American Society for Investigative Pathology

Journal title

The American journal of pathology, 2001-07, Vol.159 (1), p.339-344

Language

English

Formats

Publication information

Publisher

Bethesda, MD: American Society for Investigative Pathology

More information

Scope and Contents

Contents

TorsinA, a novel protein in which a mutation causes dominant, early onset torsion dystonia, may serve as a chaperone for misfolded proteins that require refolding or degradation. It has been hypothesized that misfolded alpha-synuclein, a protein in which two mutations cause autosomal dominantly inherited Parkinson's disease, serves as a nidus for t...

Alternative Titles

Full title

A close association of torsinA and α-synuclein in Lewy bodies a fluorescence resonance energy transfer study

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1850427

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_1850427

Other Identifiers

ISSN

0002-9440

E-ISSN

1525-2191

DOI

10.1016/S0002-9440(10)61700-2

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