Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphs

Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis

(2019) Lynn Radamaker et al.   Nature Communications

Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient

(2019) Paolo Swuec et al.   Nature Communications

Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids

(2019) Falk Liberta et al.   Nature Communications

Novel tau filament fold in chronic traumatic encephalopathy encloses hydrophobic molecules

(2019) Benjamin Falcon et al.   NATURE

Cryo-EM structures of four polymorphic TDP-43 amyloid cores

(2019) Qin Cao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Cryo-EM structure of alpha-synuclein fibrils

(2018) Ricardo Guerrero-Ferreira et al.   eLife

Automated map sharpening by maximization of detail and connectivity

(2018) Thomas C. Terwilliger et al.   Acta Crystallographica Section D-Structural Biology

Real-space refinement in PHENIX for cryo-EM and crystallography

(2018) Pavel V. Afonine et al.   Acta Crystallographica Section D-Structural Biology

Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy

(2018) Yaowang Li et al.   CELL RESEARCH

Cryo-EM structures of tau filaments from Alzheimer’s disease

(2017) Anthony W. P. Fitzpatrick et al.   NATURE

Spatiotemporal Proteomic Profiling of Huntington’s Disease Inclusions Reveals Widespread Loss of Protein Function

(2017) Fabian Hosp et al.   Cell Reports

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

(2016) Michael T. Colvin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

α-Synuclein Amyloid Fibrils with Two Entwined, Asymmetrically Associated Protofibrils

(2015) Altaira D. Dearborn et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Automatic estimation and correction of anisotropic magnification distortion in electron microscopes

(2015) Timothy Grant et al.   JOURNAL OF STRUCTURAL BIOLOGY

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

(2015) Alexis Rohou et al.   JOURNAL OF STRUCTURAL BIOLOGY

Structure of the toxic core of α-synuclein from invisible crystals

(2015) Jose A. Rodriguez et al.   NATURE

Evidence for α-synuclein prions causing multiple system atrophy in humans with parkinsonism

(2015) Stanley B. Prusiner et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

How cryo-EM is revolutionizing structural biology

(2015) Xiao-chen Bai et al.   TRENDS IN BIOCHEMICAL SCIENCES

Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6

(2015) Timothy Grant et al.   eLife

The H50Q Mutation Induces a 10-fold Decrease in the Solubility of α-Synuclein

(2014) Riccardo Porcari et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The H50Q Mutation Enhances α-Synuclein Aggregation, Secretion, and Toxicity

(2014) Ossama Khalaf et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Divergent effects of the H50Q and G51DSNCAmutations on the aggregation of α-synuclein

(2014) Nicola J. Rutherford et al.   JOURNAL OF NEUROCHEMISTRY

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

(2013) Dhiman Ghosh et al.   BIOCHEMISTRY

Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease

(2013) Silke Appel-Cresswell et al.   MOVEMENT DISORDERS

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

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

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

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

Out-of-register  -sheets suggest a pathway to toxic amyloid aggregates

(2012) C. Liu et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

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

(2012) K. C. Luk et al.   SCIENCE

Solid-State NMR Studies of Amyloid Fibril Structure

(2011) Robert Tycko   Annual Review of Physical Chemistry

Features and development ofCoot

(2010) P. Emsley et al.   ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY

Structure-neurotoxicity relationships of amyloid  -protein oligomers

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