4.6 Article

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

Related references

Note: Only part of the references are listed.
Article Clinical Neurology

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

John L. Robinson et al.

ACTA NEUROPATHOLOGICA (2013)

Article Clinical Neurology

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

Elisa Evangelisti et al.

CURRENT ALZHEIMER RESEARCH (2013)

Article Biochemistry & Molecular Biology

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

Lei-Lei Jiang et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2013)

Article Biochemistry & Molecular Biology

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

Daniel Wright et al.

PHOTOCHEMISTRY AND PHOTOBIOLOGY (2013)

Review Biochemistry & Molecular Biology

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

Emanuele Buratti et al.

TRENDS IN BIOCHEMICAL SCIENCES (2012)

Article Biochemistry & Molecular Biology

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

Akash Saini et al.

CHEMBIOCHEM (2011)

Review Biochemistry & Molecular Biology

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

Elena Garcia-Fruitos et al.

FEBS JOURNAL (2011)

Review Biochemistry & Molecular Biology

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

Pietro Gatti-Lafranconi et al.

FEBS JOURNAL (2011)

Article Cell Biology

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

Mariagioia Zampagni et al.

JOURNAL OF CELLULAR AND MOLECULAR MEDICINE (2011)

Article Biochemistry & Molecular Biology

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

Weirui Guo et al.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2011)

Article Chemistry, Multidisciplinary

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

Allan K. -H. Chen et al.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2010)

Article Biotechnology & Applied Microbiology

Quality control of inclusion bodies in Escherichia coli

Britta Juergen et al.

MICROBIAL CELL FACTORIES (2010)

Article Chemistry, Multidisciplinary

Solid-State NMR Spectroscopy Reveals that E. coli Inclusion Bodies of HET-s(218-289) are Amyloids

Christian Wasmer et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2009)

Article Biochemistry & Molecular Biology

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

Brian S. Johnson et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2009)

Article Biotechnology & Applied Microbiology

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

Raimon Sabate et al.

MICROBIAL CELL FACTORIES (2009)

Review Biochemistry & Molecular Biology

Towards revealing the structure of bacterial inclusion bodies

Lei Wang

PRION (2009)

Review Biochemistry & Molecular Biology

Amyloids in bacterial inclusion bodies

Natalia S. de Groot et al.

TRENDS IN BIOCHEMICAL SCIENCES (2009)

Article Clinical Neurology

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

Masato Hasegawa et al.

ANNALS OF NEUROLOGY (2008)

Article Clinical Neurology

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

Julian R. Thorpe et al.

JOURNAL OF NEURAL TRANSMISSION (2008)

Article Biochemistry & Molecular Biology

Bacterial inclusion bodies contain amyloid-like structure

Lei Wang et al.

PLOS BIOLOGY (2008)

Article Biochemistry & Molecular Biology

TDP-43 proteinopathies: Neurodegenerative protein misfolding diseases without amyloidosis

Linda K. Kwong et al.

NEUROSIGNALS (2008)

Article Pathology

TDP-43 in familial and sporadic frontotemporal lobar degeneration with ubiquitin inclusions

Nigel J. Cairns et al.

AMERICAN JOURNAL OF PATHOLOGY (2007)

Article Clinical Neurology

TDP-43 immunoreactivity in hippocampal sclerosis and Alzheimer's disease

Catalina Amador-Ortiz et al.

ANNALS OF NEUROLOGY (2007)

Article Multidisciplinary Sciences

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

Manuela Neumann et al.

SCIENCE (2006)

Review Biotechnology & Applied Microbiology

Protein quality in bacterial inclusion bodies

S Ventura et al.

TRENDS IN BIOTECHNOLOGY (2006)

Article Biochemistry & Molecular Biology

Amyloid-like properties of bacterial inclusion bodies

M Carrió et al.

JOURNAL OF MOLECULAR BIOLOGY (2005)

Article Biochemistry & Molecular Biology

Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins

M Umetsu et al.

FEBS LETTERS (2004)

Article Biochemistry & Molecular Biology

FT-IR study of heterologous protein expression in recombinant Escherichia coli strains

D Ami et al.

BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS (2003)

Article Biochemistry & Molecular Biology

Vaccination with soluble Aβ oligomers generates toxicity-neutralizing antibodies

MP Lambert et al.

JOURNAL OF NEUROCHEMISTRY (2001)

Article Physics, Condensed Matter

Self-assembly and structure transformations in living polymers forming fibrils

IA Nyrkova et al.

EUROPEAN PHYSICAL JOURNAL B (2000)