Single-molecule FRET studies on alpha-synuclein oligomerization of Parkinson’s disease genetically related mutants

Fast Flow Microfluidics and Single-Molecule Fluorescence for the Rapid Characterization of α-Synuclein Oligomers

(2015) Mathew H. Horrocks et al.   ANALYTICAL CHEMISTRY

Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation

(2015) Serene W. Chen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation

(2015) Dhiman Ghosh et al.   Scientific Reports

Early Sodium Dodecyl Sulfate Induced Collapse of α-Synuclein Correlates with Its Amyloid Formation

(2014) Sujit Basak et al.   ACS Chemical Neuroscience

Co-existence of Two Different α-Synuclein Oligomers with Different Core Structures Determined by Hydrogen/Deuterium Exchange Mass Spectrometry

(2014) Wojciech Paslawski et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

The Newly Discovered Parkinson’s Disease Associated Finnish Mutation (A53E) Attenuates α-Synuclein Aggregation and Membrane Binding

(2014) Dhiman Ghosh et al.   BIOCHEMISTRY

The novel Parkinson's disease linked mutation G51D attenuates in vitro aggregation and membrane binding of  -synuclein, and enhances its secretion and nuclear localization in cells

(2014) M.-B. Fares et al.   HUMAN MOLECULAR GENETICS

A novel α-synuclein mutation A53E associated with atypical multiple system atrophy and Parkinson's disease-type pathology

(2014) Petra Pasanen et al.   NEUROBIOLOGY OF AGING

Nucleation-conversion-polymerization reactions of biological macromolecules with prenucleation clusters

(2014) Gonzalo A. Garcia et al.   PHYSICAL REVIEW E

Structures of the E46K Mutant-Type α-Synuclein Protein and Impact of E46K Mutation on the Structures of the Wild-Type α-Synuclein Protein

(2013) Olivia Wise-Scira et al.   ACS Chemical Neuroscience

Structures and Free Energy Landscapes of the A53T Mutant-Type α-Synuclein Protein and Impact of A53T Mutation on the Structures of the Wild-Type α-Synuclein Protein with Dynamics

(2013) Orkid Coskuner et al.   ACS Chemical Neuroscience

α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson’s disease and multiple system atrophy?

(2013) Aoife P. Kiely et al.   ACTA NEUROPATHOLOGICA

The Parkinson’s Disease-Associated H50Q Mutation Accelerates α-Synuclein Aggregation in Vitro

(2013) Dhiman Ghosh et al.   BIOCHEMISTRY

A Relationship between the Aggregation Rates of α-Synuclein Variants and the β-Sheet Populations in Their Monomeric Forms

(2013) Carlo Camilloni et al.   JOURNAL OF PHYSICAL CHEMISTRY B

A novel  -synuclein missense mutation in Parkinson disease

(2013) C. Proukakis et al.   NEUROLOGY

Site-Specific Perturbations of Alpha-Synuclein Fibril Structure by the Parkinson's Disease Associated Mutations A53T and E46K

(2013) Luisel R. Lemkau et al.   PLoS One

Wildtype and A30P Mutant Alpha-Synuclein Form Different Fibril Structures

(2013) Søren Bang Nielsen et al.   PLoS One

Proliferation of amyloid- 42 aggregates occurs through a secondary nucleation mechanism

(2013) S. I. A. Cohen et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Structural and functional characterization of two alpha-synuclein strains

(2013) Luc Bousset et al.   Nature Communications

Direct Observation of the Interconversion of Normal and Toxic Forms of α-Synuclein

(2012) Nunilo Cremades et al.   CELL

Mutant Protein A30P α-Synuclein Adopts Wild-type Fibril Structure, Despite Slower Fibrillation Kinetics

(2012) Luisel R. Lemkau et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Single Molecule Fluorescence under Conditions of Fast Flow

(2011) Mathew H. Horrocks et al.   ANALYTICAL CHEMISTRY

The extracellular chaperone clusterin sequesters oligomeric forms of the amyloid-β1−40 peptide

(2011) Priyanka Narayan et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Familial Parkinson disease mutations influence α-synuclein assembly

(2011) Kenjiro Ono et al.   NEUROBIOLOGY OF DISEASE

Low-resolution structure of a vesicle disrupting  -synuclein oligomer that accumulates during fibrillation

(2011) L. Giehm et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

In vivo demonstration that  -synuclein oligomers are toxic

(2011) B. Winner et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Vulnerability of mesostriatal dopaminergic neurons in Parkinson’s disease

(2011) Tomás González-Hernández   Frontiers in Neuroanatomy

Early Aggregation Steps in α-Synuclein as Measured by FCS and FRET: Evidence for a Contagious Conformational Change

(2010) Sangeeta Nath et al.   BIOPHYSICAL JOURNAL

Identification of a helical intermediate in trifluoroethanol-induced alpha-synuclein aggregation

(2010) V. L. Anderson et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Conserved core of amyloid fibrils of wild type and A30P mutant α-synuclein

(2010) Min-Kyu Cho et al.   PROTEIN SCIENCE

Pre-fibrillar α-synuclein variants with impaired β-structure increase neurotoxicity in Parkinson's disease models

(2009) Damla Pinar Karpinar et al.   EMBO JOURNAL

E46K Parkinson’s-Linked Mutation Enhances C-Terminal-to-N-Terminal Contacts in α-Synuclein

(2009) Carla C. Rospigliosi et al.   JOURNAL OF MOLECULAR BIOLOGY

Sequence determinants regulating fibrillation of human α-synuclein

(2008) Hyun-Jung Koo et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Multiparametric Fluorescence Detection of Early Stages in the Amyloid Protein Aggregation of Pyrene-labeled α-Synuclein

(2008) Shyamala Thirunavukkuarasu et al.   JOURNAL OF MOLECULAR BIOLOGY

Solid-State NMR Reveals Structural Differences between Fibrils of Wild-Type and Disease-Related A53T Mutant α-Synuclein

(2008) Henrike Heise et al.   JOURNAL OF MOLECULAR BIOLOGY

Direct characterization of amyloidogenic oligomers by single-molecule fluorescence

(2008) A. Orte et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA