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

Research output: Contribution to journalArticle

72 Citations (Scopus)

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 languageEnglish
Pages (from-to)405-409
Number of pages5
JournalAngewandte Chemie - International Edition
Volume50
Issue number2
DOIs
Publication statusPublished - 10 Jan 2011
Externally publishedYes

Fingerprint

Synucleins
Oligomerization
Ubiquitination
Parkinson Disease
Health
Membranes
Ubiquitin

Keywords

  • aggregation
  • Parkinson's disease
  • proteins
  • semisynthesis
  • ubiquitination

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis

Cite this

Towards elucidation of the role of ubiquitination in the pathogenesis of parkinson's disease with semisynthetic ubiquitinated α-synuclein. / Hejjaoui, Mirva; Haj-Yahya, Mahmood; Kumar, K. S Ajish; Brik, Ashraf; Lashuel, Hilal A.

In: Angewandte Chemie - International Edition, Vol. 50, No. 2, 10.01.2011, p. 405-409.

Research output: Contribution to journalArticle

Hejjaoui, Mirva ; Haj-Yahya, Mahmood ; Kumar, K. S Ajish ; Brik, Ashraf ; Lashuel, Hilal A. / Towards elucidation of the role of ubiquitination in the pathogenesis of parkinson's disease with semisynthetic ubiquitinated α-synuclein. In: Angewandte Chemie - International Edition. 2011 ; Vol. 50, No. 2. pp. 405-409.
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