Towards elucidation of the role of ubiquitination in the pathogenesis of parkinson's disease with semisynthetic ubiquitinated α-synuclein

Mirva Hejjaoui; Mahmood Haj-Yahya; K. S.Ajish Kumar; Ashraf Brik; Hilal A. Lashuel

doi:10.1002/anie.201005546

Towards elucidation of the role of ubiquitination in the pathogenesis of parkinson's disease with semisynthetic ubiquitinated α-synuclein

Mirva Hejjaoui, Mahmood Haj-Yahya, K. S.Ajish Kumar, Ashraf Brik, Hilal A. Lashuel

Department of Chemistry

Research output: Contribution to journal › Article › peer-review

101 Scopus citations

Abstract

Ubiquitinate me here: The semisynthesis and characterization of a site-specifically monoubiquitinated form of α-synuclein (see picture) enabled investigation of the effect of ubiquitination on membrane binding, oligomerization, and fibrillogenesis. The introduction of specific ubiquitin modifications into α-synuclein will shed light on the role of ubiquitination in regulating the function(s) of α-synuclein in health and disease.

Original language	English
Pages (from-to)	405-409
Number of pages	5
Journal	Angewandte Chemie - International Edition
Volume	50
Issue number	2
DOIs	https://doi.org/10.1002/anie.201005546
State	Published - 10 Jan 2011

Keywords

Parkinson's disease
aggregation
proteins
semisynthesis
ubiquitination

ASJC Scopus subject areas

Catalysis
General Chemistry

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10.1002/anie.201005546

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AU - Kumar, K. S.Ajish

AU - Brik, Ashraf

AU - Lashuel, Hilal A.

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Towards elucidation of the role of ubiquitination in the pathogenesis of parkinson's disease with semisynthetic ubiquitinated α-synuclein

Abstract

Keywords

ASJC Scopus subject areas

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