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Posttranslational modification and mutation of histidine 50 trigger alpha synuclein aggregation and...

Posttranslational modification and mutation of histidine 50 trigger alpha synuclein aggregation and...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4365527

Posttranslational modification and mutation of histidine 50 trigger alpha synuclein aggregation and toxicity

About this item

Full title

Posttranslational modification and mutation of histidine 50 trigger alpha synuclein aggregation and toxicity

Publisher

England: BioMed Central Ltd

Journal title

Molecular neurodegeneration, 2015-03, Vol.10 (1), p.8-8

Language

English

Formats

Publication information

Publisher

England: BioMed Central Ltd

More information

Scope and Contents

Contents

Aggregation and aggregation-mediated formation of toxic alpha synuclein (aSyn) species have been linked to the pathogenesis of sporadic and monogenic Parkinson's disease (PD). A novel H50Q mutation of aSyn, resulting in the substitution of histidine by glutamine, has recently been identified in PD patients. We have previously shown that the lipid p...

Alternative Titles

Full title

Posttranslational modification and mutation of histidine 50 trigger alpha synuclein aggregation and toxicity

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4365527

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_4365527

Other Identifiers

ISSN

1750-1326

E-ISSN

1750-1326

DOI

10.1186/s13024-015-0004-0

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