TDP-43 Inclusion Bodies Formed in Bacteria Are Structurally Amorphous, Non-Amyloid and Inherently Toxic to Neuroblastoma Cells

Inclusions in frontotemporal lobar degeneration with TDP-43 proteinopathy (FTLD-TDP) and amyotrophic lateral sclerosis (ALS), but not FTLD with FUS proteinopathy (FTLD-FUS), have properties of amyloid

(2013) Eileen H. Bigio et al.   ACTA NEUROPATHOLOGICA

Lipid Rafts Mediate Amyloid-Induced Calcium Dyshomeostasis and Oxidative Stress in Alzheimer’s Disease

(2013) Elisa Evangelisti et al.   Current Alzheimer Research

Structural Transformation of the Amyloidogenic Core Region of TDP-43 Protein Initiates Its Aggregation and Cytoplasmic Inclusion

(2013) Lei-Lei Jiang et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

TDP-43 skeins show properties of amyloid in a subset of ALS cases

(2012) John L. Robinson et al.   ACTA NEUROPATHOLOGICA

Protective Properties of NovelS-Acyl-Glutathione Thioesters Against Ultraviolet-induced Oxidative Stress

(2012) Daniel Wright et al.   PHOTOCHEMISTRY AND PHOTOBIOLOGY

TDP-43: gumming up neurons through protein–protein and protein–RNA interactions

(2012) Emanuele Buratti et al.   TRENDS IN BIOCHEMICAL SCIENCES

Delineation of the Core Aggregation Sequences of TDP-43 C-Terminal Fragment

(2011) Akash Saini et al.   CHEMBIOCHEM

Biological role of bacterial inclusion bodies: a model for amyloid aggregation

(2011) Elena García-Fruitós et al.   FEBS Journal

Concepts and tools to exploit the potential of bacterial inclusion bodies in protein science and biotechnology

(2011) Pietro Gatti-Lafranconi et al.   FEBS Journal

TDP-43: the relationship between protein aggregation and neurodegeneration in amyotrophic lateral sclerosis and frontotemporal lobar degeneration

(2011) Robert H. Baloh   FEBS Journal

An ALS-associated mutation affecting TDP-43 enhances protein aggregation, fibril formation and neurotoxicity

(2011) Weirui Guo et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Large Proteins Have a Great Tendency to Aggregate but a Low Propensity to Form Amyloid Fibrils

(2011) Hassan Ramshini et al.   PLoS One

Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form

(2010) Aaron Kerman et al.   ACTA NEUROPATHOLOGICA

A comparison of the biochemical modifications caused by toxic and non-toxic protein oligomers in cells

(2010) Mariagioia Zampagni et al.   JOURNAL OF CELLULAR AND MOLECULAR MEDICINE

Induction of Amyloid Fibrils by the C-Terminal Fragments of TDP-43 in Amyotrophic Lateral Sclerosis

(2010) Allan K.-H. Chen et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Quality control of inclusion bodies in Escherichia coli

(2010) Britta Jürgen et al.   Microbial Cell Factories

Mutant TAR DNA-binding protein-43 induces oxidative injury in motor neuron-like cell

(2010) W. Duan et al.   NEUROSCIENCE

Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue

(2010) Liqun Liu-Yesucevitz et al.   PLoS One

Towards revealing the structure of bacterial inclusion bodies

(2010) Lei Wang   Prion

Phosphorylation of S409/410 of TDP-43 is a consistent feature in all sporadic and familial forms of TDP-43 proteinopathies

(2009) Manuela Neumann et al.   ACTA NEUROPATHOLOGICA

Solid-State NMR Spectroscopy Reveals thatE. coliInclusion Bodies of HET-s(218-289) are Amyloids

(2009) Christian Wasmer et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Agitation and High Ionic Strength Induce Amyloidogenesis of a Folded PDZ Domain in Native Conditions

(2009) Alessandro Sicorello et al.   BIOPHYSICAL JOURNAL

TDP-43 Is Intrinsically Aggregation-prone, and Amyotrophic Lateral Sclerosis-linked Mutations Accelerate Aggregation and Increase Toxicity

(2009) Brian S. Johnson et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Characterization of the amyloid bacterial inclusion bodies of the HET-s fungal prion

(2009) Raimon Sabaté et al.   Microbial Cell Factories

Amyloids in bacterial inclusion bodies

(2009) Natalia S. de Groot et al.   TRENDS IN BIOCHEMICAL SCIENCES

Ultrastructural localization of TDP-43 in filamentous neuronal inclusions in various neurodegenerative diseases

(2008) Wen-Lang Lin et al.   ACTA NEUROPATHOLOGICA

Enrichment of C-Terminal Fragments in TAR DNA-Binding Protein-43 Cytoplasmic Inclusions in Brain but not in Spinal Cord of Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

(2008) Lionel M. Igaz et al.   AMERICAN JOURNAL OF PATHOLOGY

Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

(2008) Masato Hasegawa et al.   ANNALS OF NEUROLOGY

Fine structural analysis of the neuronal inclusions of frontotemporal lobar degeneration with TDP-43 proteinopathy

(2008) Julian R. Thorpe et al.   JOURNAL OF NEURAL TRANSMISSION

Bacterial Inclusion Bodies Contain Amyloid-Like Structure

(2008) Lei Wang et al.   PLOS BIOLOGY

Vaccination with soluble Aβ oligomers generates toxicity-neutralizing antibodies

(2003) Mary P. Lambert et al.   JOURNAL OF NEUROCHEMISTRY