Synchrotron FTIR micro-spectroscopy for structural analysis of Lewy bodies in the brain of Parkinson’s disease patients

Probing the Sources of the Apparent Irreproducibility of Amyloid Formation: Drastic Changes in Kinetics and a Switch in Mechanism Due to Micellelike Oligomer Formation at Critical Concentrations of IAPP

(2015) Jeffrey R. Brender et al.   JOURNAL OF PHYSICAL CHEMISTRY B

Conformational heterogeneity of α -synuclein in membrane

(2014) Josh V. Vermaas et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour

(2014) Giuliana Fusco et al.   Nature Communications

Synchrotron FTIR reveals lipid around and within amyloid plaques in transgenic mice and Alzheimer's disease brain

(2013) Catherine R. Liao et al.   ANALYST

Prion-like spreading of pathological α-synuclein in brain

(2013) Masami Masuda-Suzukake et al.   BRAIN

Structural and functional characterization of two alpha-synuclein strains

(2013) Luc Bousset et al.   Nature Communications

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

α-Synuclein and Neuronal Cell Death

(2012) Toru Yasuda et al.   MOLECULAR NEUROBIOLOGY

The Lewy Body in Parkinson’s Disease and Related Neurodegenerative Disorders

(2012) Koichi Wakabayashi et al.   MOLECULAR NEUROBIOLOGY

Expression pattern and localization of alpha-synuclein in the human enteric nervous system

(2012) Martina Böttner et al.   NEUROBIOLOGY OF DISEASE

Development of scattering near-field optical microspectroscopy apparatus using an infrared synchrotron radiation source

(2012) Yuka Ikemoto et al.   OPTICS COMMUNICATIONS

Pathological  -Synuclein Transmission Initiates Parkinson-like Neurodegeneration in Nontransgenic Mice

(2012) K. C. Luk et al.   SCIENCE

The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency

(2011) Jeffrey R. Brender et al.   BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES

Pale Neurites, Premature α-Synuclein Aggregates with Centripetal Extension from Axon Collaterals

(2011) Toshiro Kanazawa et al.   BRAIN PATHOLOGY

Helical Conformation of the SEVI Precursor Peptide PAP248-286, a Dramatic Enhancer of HIV Infectivity, Promotes Lipid Aggregation and Fusion

(2009) Jeffrey R. Brender et al.   BIOPHYSICAL JOURNAL

Conversion of Wild-type α-Synuclein into Mutant-type Fibrils and Its Propagation in the Presence of A30P Mutant

(2009) Motokuni Yonetani et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Exogenous  -synuclein fibrils seed the formation of Lewy body-like intracellular inclusions in cultured cells

(2009) K. C. Luk et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Evaluation of α-synuclein immunohistochemical methods used by invited experts

(2008) Thomas G. Beach et al.   ACTA NEUROPATHOLOGICA

Red Blood Cells Are the Major Source of Alpha-Synuclein in Blood

(2008) Robin Barbour et al.   Neurodegenerative Diseases