The Molecular Chaperone Hsp90 Modulates Intermediate Steps of Amyloid Assembly of the Parkinson-related Protein α-Synuclein

Unique copper-induced oligomers mediate alpha-synuclein toxicity

(2009) Josephine A. Wright et al.   FASEB JOURNAL

Multiple Tight Phospholipid-Binding Modes of α-Synuclein Revealed by Solution NMR Spectroscopy

(2009) Christina R. Bodner et al.   JOURNAL OF MOLECULAR BIOLOGY

Rab11a and HSP90 Regulate Recycling of Extracellular  -Synuclein

(2009) J. Liu et al.   JOURNAL OF NEUROSCIENCE

The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

(2009) Moritz Mickler et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90

(2009) Martin Hessling et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Interactions between Hsp70 and the Hydrophobic Core of α-Synuclein Inhibit Fibril Assembly†

(2008) Kelvin C. Luk et al.   BIOCHEMISTRY

Novel suppressors of α-synuclein toxicity identified using yeast

(2008) Jun Liang et al.   HUMAN MOLECULAR GENETICS

The Hsp90 Chaperone Machinery Regulates Signaling by Modulating Ligand Binding Clefts

(2008) William B. Pratt et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Hsp90 Chaperone Machinery

(2008) Sebastian Karl Wandinger et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Conserved Conformational Changes in the ATPase Cycle of Human Hsp90

(2008) Klaus Richter et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

CHIP Targets Toxic α-Synuclein Oligomers for Degradation

(2008) Julie E. Tetzlaff et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

A novel HSP90 chaperone complex regulates intracellular vesicle transport

(2008) G. P. Lotz et al.   JOURNAL OF CELL SCIENCE

Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle

(2008) Daniel R. Southworth et al.   MOLECULAR CELL

Formation of Toxic Oligomeric α-Synuclein Species in Living Cells

(2008) Tiago Fleming Outeiro et al.   PLoS One

The fold of  -synuclein fibrils

(2008) M. Vilar et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA