N-terminal acetylation is critical for forming α-helical oligomer of α-synuclein

α-Synuclein in Central Nervous System and from Erythrocytes, Mammalian Cells, andEscherichia coliExists Predominantly as Disordered Monomer

(2012) Bruno Fauvet et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Allostery in a Disordered Protein: Oxidative Modifications to α-Synuclein Act Distally To Regulate Membrane Binding

(2011) Eva Sevcsik et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

(2011) Tim Bartels et al.   NATURE

A soluble  -synuclein construct forms a dynamic tetramer

(2011) W. Wang et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

N-Terminal Acetylation Acts as an Avidity Enhancer Within an Interconnected Multiprotein Complex

(2011) D. C. Scott et al.   SCIENCE

Targeted Amino-Terminal Acetylation of Recombinant Proteins in E. coli

(2010) Matthew Johnson et al.   PLoS One

α-Synuclein Binds Large Unilamellar Vesicles as an Extended Helix†

(2009) Adam J. Trexler et al.   BIOCHEMISTRY

Interplay of  -synuclein binding and conformational switching probed by single-molecule fluorescence

(2009) A. C. M. Ferreon et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans

(2009) T. Arnesen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural characterization of α-synuclein in an aggregation prone state

(2009) Min-Kyu Cho et al.   PROTEIN SCIENCE