Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation.
Meier, Franziska
Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation. [electronic resource] - Journal of the American Chemical Society Mar 2012 - 5468-71 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
1520-5126
10.1021/ja300094r doi
Amino Acid Sequence
Disulfides--chemistry
Humans
Models, Molecular
Molecular Sequence Data
Parkinson Disease--metabolism
Protein Conformation
Ubiquitin--chemistry
Ubiquitination
alpha-Synuclein--chemistry
Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation. [electronic resource] - Journal of the American Chemical Society Mar 2012 - 5468-71 p. digital
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
1520-5126
10.1021/ja300094r doi
Amino Acid Sequence
Disulfides--chemistry
Humans
Models, Molecular
Molecular Sequence Data
Parkinson Disease--metabolism
Protein Conformation
Ubiquitin--chemistry
Ubiquitination
alpha-Synuclein--chemistry