☆ 4.6 Article

Cryo-EM structures of prion protein filaments from Gerstmann-Straussler-Scheinker disease

ACTA NEUROPATHOLOGICA (2022)

Related references

Note: Only part of the references are listed.

Review Multidisciplinary Sciences

Cryo-EM structures of amyloid-b 42 filaments from human brains

Yang Yang et al.

Summary: Filament assembly of A beta 42 peptides is a central event in Alzheimer's disease. This study provides cryo-EM structures of A beta 42 filaments from human brains, revealing two types of structurally related filaments. Understanding the structures of A beta 42 filaments from human brains may have important implications for the development of assembly inhibitors and improved imaging agents.

SCIENCE (2022)

Add to Collection

Article Biology

Assembly of recombinant tau into filaments identical to those of Alzheimer's disease and chronic traumatic encephalopathy

Sofia Lovestam et al.

Summary: This study reports the in vitro replication of tau filament structures from both Alzheimer's disease (AD) and chronic traumatic encephalopathy (CTE) using recombinant tau. The results suggest that post-translational modifications of tau and the presence of inorganic salts may modulate filament assembly.

ELIFE (2022)

Add to Collection

Review Biochemistry & Molecular Biology

High resolution single particle Cryo-EM refinement using JSPR

Chen Sun et al.

Summary: JSPR is a software developed at Purdue University for single particle cryo-EM image processing and 3D reconstruction, offering tools for symmetric and asymmetric reconstructions of viruses, ab initio reconstructions, high resolution refinements, and handling of image files. The software also includes features such as multiaberration alignments and automatic optimization of masking for map resolution assessment using true FSC.

PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY (2021)

Add to Collection

Article Multidisciplinary Sciences

Structure-based classification of tauopathies

Yang Shi et al.

Summary: The structures of tau filaments from different tauopathies vary, allowing for a hierarchical classification of these diseases. Some tauopathies share similar filament folds, while others have distinct folding patterns.

NATURE (2021)

Add to Collection

Article Biochemical Research Methods

Protein identification from electron cryomicroscopy maps by automated model building and side-chain matching

Thomas C. Terwilliger et al.

Summary: Using single-particle electron cryo-microscopy, researchers have developed a method to automatically interpret maps and create atomic models of proteins from reconstructions, resulting in successful identification of proteins based on correct sequence matching. This approach is highly effective for maps obtained at resolutions of 3.5 angstrom and better, with some utility even at resolutions as low as 4 angstrom.

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2021)

Add to Collection

Article Clinical Neurology

Structure of Tau filaments in Prion protein amyloidoses

Grace I. Hallinan et al.

Summary: The study analyzes Tau fibers from individuals affected by Prion-Protein cerebral amyloid angiopathy (PrP-CAA) and Gerstmann-Straussler-Scheinker (GSS) disease, showing a striking similarity to neurofibrillary tangles (NFTs) in Alzheimer's disease. Regardless of the primary amino acid sequence of the amyloid protein, similar molecular mechanisms are at play in the formation of identical Tau filaments, as supported by mass spectrometry and cryo-EM analyses.

ACTA NEUROPATHOLOGICA (2021)

Add to Collection

Article Biochemistry & Molecular Biology

High-resolution structure and strain comparison of infectious mammalian prions

Allison Kraus et al.

Summary: The study reveals the core structure of prions and the templating surface formed by individual monomers at fibril ends. Comparison to another prion strain shows differences in fibril morphology. These findings provide insights into the propagation of prions.

MOLECULAR CELL (2021)

Add to Collection

Review Neurosciences

Extracellular protein components of amyloid plaques and their roles in Alzheimer's disease pathology

M. Mahafuzur Rahman et al.

Summary: Alzheimer's disease is pathologically defined by the presence of A beta in extracellular senile plaques and tau in intracellular neurofibrillary tangles. Besides A beta, other constituents are accumulated in the plaques, mainly focusing on extracellular proteins, which may contribute to disruptions in the protein network and lead to AD and copathology. This review provides an overview of extracellular proteins interacting with A beta and their potential roles in AD pathology, as well as methods to analyze the incorporation of proteins in plaques.

MOLECULAR NEURODEGENERATION (2021)

Add to Collection

Article Multidisciplinary Sciences

Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM

Li-Qiang Wang et al.

Summary: This study revealed the structure of amyloid fibrils formed by full-length human PrP with E196K mutation, which differs from wild-type PrP and hamster brain-derived prion fibrils. The results highlight the importance of familial mutations in inducing different prion strains.

SCIENCE ADVANCES (2021)

Add to Collection

Article Biochemistry & Molecular Biology

Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core

Calina Glynn et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2020)

Add to Collection

Article Biochemistry & Molecular Biology

Cryo-EM structure of an amyloid fibril formed by full-length human prion protein

Li-Qiang Wang et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2020)

Add to Collection

Article Neurosciences

Gerstmann-Straussler-Scheinker disease revisited: accumulation of covalently-linked multimers of internal prion protein fragments

Laura Cracco et al.

ACTA NEUROPATHOLOGICA COMMUNICATIONS (2019)

Add to Collection

Article Biochemical Research Methods

New tools for the analysis and validation of cryo-EM maps and atomic models

Pavel V. Afonine et al.

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY (2018)

Add to Collection

Article Chemistry, Multidisciplinary

Structural Studies of Amyloid Fibrils by Paramagnetic Solid-State Nuclear Magnetic Resonance Spectroscopy

Theint Theint et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2018)

Add to Collection

Article Biochemical Research Methods

A fully automatic method yielding initial models from high-resolution cryo-electron microscopy maps

Thomas C. Terwilliger et al.

NATURE METHODS (2018)

Add to Collection

Article Neurosciences

Detection of tau in Gerstmann-Straussler-Scheinker disease (PRNP F198S) by [F-18]Flortaucipir PET

Shannon L. Risacher et al.

ACTA NEUROPATHOLOGICA COMMUNICATIONS (2018)

Add to Collection

Review Clinical Neurology

The function of the cellular prion protein in health and disease

Joel C. Watts et al.

ACTA NEUROPATHOLOGICA (2018)

Add to Collection

Article Medicine, Research & Experimental

Structural Biology of PrP Prions

Gerald Stubbs et al.

COLD SPRING HARBOR PERSPECTIVES IN MEDICINE (2017)

Add to Collection

Article Biochemistry & Molecular Biology

Helical reconstruction in RELION

Shaoda He et al.

JOURNAL OF STRUCTURAL BIOLOGY (2017)

Add to Collection

Article Multidisciplinary Sciences

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

Anthony W. P. Fitzpatrick et al.

NATURE (2017)

Add to Collection

Letter Biochemical Research Methods

MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy

Shawn Q. Zheng et al.

NATURE METHODS (2017)

Add to Collection

Article Multidisciplinary Sciences

Novel strain properties distinguishing sporadic prion diseases sharing prion protein genotype and prion type

Laura Cracco et al.

SCIENTIFIC REPORTS (2017)

Add to Collection

Article Biochemistry & Molecular Biology

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

Marcus D. Tuttle et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)

Add to Collection

Article Biochemistry & Molecular Biology

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

Marcus D. Tuttle et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2016)

Add to Collection

Article Biology

Automated structure refinement of macromolecular assemblies from cryo-EM maps using Rosetta

Ray Yu-Ruei Wang et al.

ELIFE (2016)

Add to Collection

Article Biochemistry & Molecular Biology

CTFFIND4: Fast and accurate defocus estimation from electron micrographs

Alexis Rohou et al.

JOURNAL OF STRUCTURAL BIOLOGY (2015)

Add to Collection

Article Biochemical Research Methods

Proteomics Analysis of Amyloid and Nonamyloid Prion Disease Phenotypes Reveals Both Common and Divergent Mechanisms of Neuropathogenesis

Roger A. Moore et al.

JOURNAL OF PROTEOME RESEARCH (2014)

Add to Collection

Letter Biotechnology & Applied Microbiology

ProteomeXchange provides globally coordinated proteomics data submission and dissemination

Juan A. Vizcaino et al.

NATURE BIOTECHNOLOGY (2014)

Add to Collection

Article Biochemistry & Molecular Biology

Burial of the Polymorphic Residue 129 in Amyloid Fibrils of Prion Stop Mutants

Lukasz Skora et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2013)

Add to Collection

Editorial Material Biochemistry & Molecular Biology

Conserved amyloid core structure of stop mutants of the human prion protein

Markus Zweckstetter

PRION (2013)

Add to Collection

Article Biochemistry & Molecular Biology

A Bayesian View on Cryo-EM Structure Determination

Sjors H. W. Scheres

JOURNAL OF MOLECULAR BIOLOGY (2012)

Add to Collection

Article Biochemistry & Molecular Biology

Common Structural Traits across Pathogenic Mutants of the Human Prion Protein and Their Implications for Familial Prion Diseases

Giulia Rossetti et al.

JOURNAL OF MOLECULAR BIOLOGY (2011)

Add to Collection

Article Biochemical Research Methods

Features and development of Coot

P. Emsley et al.

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY (2010)

Add to Collection

Article Biochemistry & Molecular Biology

Appion: An integrated, database-driven pipeline to facilitate EM image processing

Gabriel C. Lander et al.

JOURNAL OF STRUCTURAL BIOLOGY (2009)

Add to Collection

Article Biochemistry & Molecular Biology

EMAN2: An extensible image processing suite for electron microscopy

Guang Tang et al.

JOURNAL OF STRUCTURAL BIOLOGY (2007)

Add to Collection

Article Biochemistry & Molecular Biology

Automated molecular microscopy: The new Leginon system

C Suloway et al.

JOURNAL OF STRUCTURAL BIOLOGY (2005)

Add to Collection

Article Pathology

Prion proteins with different conformations accumulate in Geustmann-Straussler-Scheinker disease caused by A117V and F198S mutations

P Piccardo et al.

AMERICAN JOURNAL OF PATHOLOGY (2001)

Add to Collection

Review Neurosciences

Prion diseases of humans and animals: Their causes and molecular basis

J Collinge

ANNUAL REVIEW OF NEUROSCIENCE (2001)

Add to Collection

Article Multidisciplinary Sciences

NMR solution structure of the human prion protein

R Zahn et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2000)

Add to Collection

© Peeref 2019-2024. All rights reserved.