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Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Ubiquitin-positive, tau- and α-synuclein–negative inclusions are hallmarks of frontotemporal lobar degeneration with ubiquitin-positive inclusions and amyotrophic lateral sclerosis. Although theExpand
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A harmonized classification system for FTLD-TDP pathology
In 2006, two papers were published, each describing pathological heterogeneity in cases of frontotemporal lobar degeneration (FTLD) with ubiquitin-positive, tau-negative inclusions (FTLD-U) [7, 11].Expand
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Pathological heterogeneity of frontotemporal lobar degeneration with ubiquitin-positive inclusions delineated by ubiquitin immunohistochemistry and novel monoclonal antibodies.
Frontotemporal lobar degeneration with ubiquitin-positive inclusions (FTLD-U) is a common neuropathological subtype of frontotemporal dementia. Although this subtype of frontotemporal dementia isExpand
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TDP-43 proteinopathy: the neuropathology underlying major forms of sporadic and familial frontotemporal lobar degeneration and motor neuron disease
The rapid confirmation of the initial report by Neumann et al. (Science 314:130–133, 2006) that transactive response (TAR)-DNA-binding protein 43 (TDP-43) is the major disease protein linkingExpand
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TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: protein misfolding diseases without amyloidosis.
Herein, we review advances in understanding a group of disorders collectively known as TAR-DNA binding protein 43 (TDP-43) proteinopathies since the report that TDP-43 is the major disease proteinExpand
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Novel Monoclonal Antibodies Demonstrate Biochemical Variation of Brain Parkin with Age*
Autosomal recessive juvenile parkinsonism is a movement disorder associated with the degeneration of dopaminergic neurons in substantia nigra pars compacta. The loss of functional parkin caused byExpand
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DJ‐1 is present in a large molecular complex in human brain tissue and interacts with α‐synuclein
DJ‐1 is a ubiquitously expressed protein involved in various cellular processes including cell proliferation, RNA‐binding, and oxidative stress. Mutations that result in loss of DJ‐1 function lead toExpand
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Ubiquitination of alpha-synuclein is not required for formation of pathological inclusions in alpha-synucleinopathies.
alpha-Synucleinopathies, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy, are neurodegenerative disorders in which abnormal inclusions containing alpha-synucleinExpand
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Ubiquitination of α-Synuclein Is Not Required for Formation of Pathological Inclusions in α-Synucleinopathies
α-Synucleinopathies, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy, are neurodegenerative disorders in which abnormal inclusions containing α-synucleinExpand
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The environmental toxin arsenite induces tau hyperphosphorylation.
Abnormally hyperphosphorylated tau polymers known as paired helical filaments constitute one of the major characteristic lesions that lead to the demise of neurons in Alzheimer's disease. Here, weExpand
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