Pathogenic Considerations in Sporadic Inclusion-Body Myositis, a Degenerative Muscle Disease Associated With Aging and Abnormalities of Myoproteostasis

Tau Aggregation and Toxicity in Tauopathic Neurodegenerative Diseases

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Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis

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Long-term observational study of sporadic inclusion body myositis

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Sporadic inclusion-body myositis: Conformational multifactorial ageing-related degenerative muscle disease associated with proteasomal and lysosomal inhibition, endoplasmic reticulum stress, and accumulation of amyloid-β42 oligomers and phosphorylated tau

(2011) Valerie Askanas et al.   PRESSE MEDICALE

Novel demonstration of amyloid-β oligomers in sporadic inclusion-body myositis muscle fibers

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Impaired Autophagy in Sporadic Inclusion-Body Myositis and in Endoplasmic Reticulum Stress-Provoked Cultured Human Muscle Fibers

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Misframed Proteins and Neurodegeneration: A Novel View on Alzheimer’s and Parkinson’s Diseases

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PET has no clothes

(2010) M. P. Laakso et al.   NEUROLOGY

In sporadic inclusion body myositis muscle fibres TDP-43-positive inclusions are less frequent and robust than p62 inclusions, and are not associated with paired helical filaments

(2010) C. D'Agostino et al.   NEUROPATHOLOGY AND APPLIED NEUROBIOLOGY

Increased BACE1 mRNA and noncoding BACE1-antisense transcript in sporadic inclusion-body myositis muscle fibers—Possibly caused by endoplasmic reticulum stress

(2010) Anna Nogalska et al.   NEUROSCIENCE LETTERS

Selective Molecular Alterations in the Autophagy Pathway in Patients with Lewy Body Disease and in Models of α-Synucleinopathy

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Amyloid-β42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis

(2009) Gaetano Vattemi et al.   ACTA NEUROPATHOLOGICA

Increased plasma amyloid-β42 protein in sporadic inclusion body myositis

(2009) Wilson F. Abdo et al.   ACTA NEUROPATHOLOGICA

The ubiquitin proteasome system in neuropathology

(2009) Norman L. Lehman   ACTA NEUROPATHOLOGICA

p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis

(2009) Anna Nogalska et al.   ACTA NEUROPATHOLOGICA

Mechanisms of tau-induced neurodegeneration

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Phenolic Compounds Prevent Alzheimer’s Pathology through Different Effects on the Amyloid-β Aggregation Pathway

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Inclusion Body Myositis: A Degenerative Muscle Disease Associated with Intra-Muscle Fiber Multi-Protein Aggregates, Proteasome Inhibition, Endoplasmic Reticulum Stress and Decreased Lysosomal Degradation

(2009) Valerie Askanas et al.   BRAIN PATHOLOGY

Protein Targets of Oxidative Damage in Human Neurodegenerative Diseases with Abnormal Protein Aggregates

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Autophagy Is Required to Maintain Muscle Mass

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Identification of Physiological and Toxic Conformations in Aβ42 Aggregates

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In AβPP-overexpressing cultured human muscle fibers proteasome inhibition enhances phosphorylation of AβPP751 and GSK3β activation: effects mitigated by lithium and apparently relevant to sporadic inclusion-body myositis

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TAR DNA-Binding Protein 43 Accumulation in Protein Aggregate Myopathies

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A Role for NBR1 in Autophagosomal Degradation of Ubiquitinated Substrates

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Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis

(2009) Mohammad Salajegheh et al.   MUSCLE & NERVE

Role of Synucleins in Alzheimer’s Disease

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Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins

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TDP-43 accumulation is common in myopathies with rimmed vacuoles

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Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer’s and Parkinson’s disease brains

(2008) Valerie Askanas et al.   ACTA NEUROPATHOLOGICA

Phase 2 study of sodium phenylbutyrate in ALS

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Inflammation induces tau pathology in inclusion body myositis model via glycogen synthase kinase-3β

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Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression

(2008) Tadanori Hamano et al.   EUROPEAN JOURNAL OF NEUROSCIENCE

In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidized

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Parkin is recruited selectively to impaired mitochondria and promotes their autophagy

(2008) Derek Narendra et al.   JOURNAL OF CELL BIOLOGY

The ubiquitin-proteasome system in Alzheimer's disease

(2008) Salvatore Oddo   JOURNAL OF CELLULAR AND MOLECULAR MEDICINE

TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia

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Expression of a noncoding RNA is elevated in Alzheimer's disease and drives rapid feed-forward regulation of β-secretase

(2008) Mohammad Ali Faghihi et al.   NATURE MEDICINE

Decreased SIRT1 deacetylase activity in sporadic inclusion-body myositis muscle fibers

(2008) Anna Nogalska et al.   NEUROBIOLOGY OF AGING

Amyloid-β protein impairs Ca2+ release and contractility in skeletal muscle

(2008) Alexander Shtifman et al.   NEUROBIOLOGY OF AGING

Lithium, a Potential Protective Drug in Alzheimer’s Disease

(2008) T. Engel et al.   Neurodegenerative Diseases

Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis

(2008) Theresa J. Kannanayakal et al.   NEUROSCIENCE LETTERS

Adapting Proteostasis for Disease Intervention

(2008) William E. Balch et al.   SCIENCE