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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

Acta neuropathologica, 2008-12, Vol.116 (6), p.583-595

2008

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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

Acta neuropathologica, 2009-09, Vol.118 (3), p.407-413

2009

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

Acta neuropathologica, 2011-11, Vol.122 (5), p.627-636

2011

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

The American journal of pathology, 2010-09, Vol.177 (3), p.1377-1387

2010

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Luminescent Conjugated Oligothiophenes for Sensitive Fluorescent Assignment of Protein Inclusion Bodies

Chembiochem : a European journal of chemical biology, 2013-03, Vol.14 (5), p.607-616

2013

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Sporadic inclusion-body myositis: A degenerative muscle disease associated with aging, impaired muscle protein homeostasis and abnormal mitophagy

Biochimica et biophysica acta, 2015-04, Vol.1852 (4), p.633-643

2015

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Sodium phenylbutyrate reverses lysosomal dysfunction and decreases amyloid-β42 in an in vitro-model of inclusion-body myositis

Neurobiology of disease, 2014-05, Vol.65, p.93-101

2014

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Activation of the γ-secretase complex and presence of γ-secretase-activating protein may contribute to Aβ42 production in sporadic inclusion-body myositis muscle fibers

Neurobiology of disease, 2012-10, Vol.48 (1), p.141-149

2012

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Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanisms

Current opinion in neurology, 2002-10, Vol.15 (5), p.525-531

2002

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Diagnostic histochemistry and clinical-pathological testings as molecular pathways to pathogenesis and treatment of the ageing neuromuscular system: a personal view

Biochimica et biophysica acta, 2015-04, Vol.1852 (4), p.563-584

Engel, W. King

2015

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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

Brain pathology (Zurich, Switzerland), 2009-07, Vol.19 (3), p.493-506

2009

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Inclusion-body myositis: A myodegenerative conformational disorder associated with Aβ, protein misfolding, and proteasome inhibition

Neurology, 2006-01, Vol.66 (1_suppl_1)

2006

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Molecular pathology and pathogenesis of inclusion-body myositis

Microscopy research and technique, 2005-07, Vol.67 (3-4), p.114-120

2005

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Inclusion-body myositis, a multifactorial muscle disease associated with aging: current concepts of pathogenesis

Current opinion in rheumatology, 2007-11, Vol.19 (6), p.550-559

2007

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Inclusion-body myositis: clinical, diagnostic, and pathologic aspects

Neurology, 2006-01, Vol.66 (2 Suppl 1), p.S20

2006

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Activation of the Unfolded Protein Response in Sporadic Inclusion-Body Myositis but Not in Hereditary GNE Inclusion-Body Myopathy

Journal of neuropathology and experimental neurology, 2015-06, Vol.74 (6), p.538-546

2015

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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

La Presse médicale (1983), 2011-04, Vol.40 (4), p.e219-e235

2011

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Sporadic inclusion-body myositis and hereditary inclusion-body myopathies: current concepts of diagnosis and pathogenesis

Current opinion in rheumatology, 1998-11, Vol.10 (6), p.530-542

1998

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

Neuroscience letters, 2010-05, Vol.474 (3), p.140-143

2010

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Dysferlin is a newly identified binding partner of AβPP and it co-aggregates with amyloid-β42 within sporadic inclusion-body myositis (s-IBM) muscle fibers

Acta neuropathologica, 2013-11, Vol.126 (5), p.781-783

2013

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Unfolding Story of Inclusion-Body Myositis and Myopathies: Role of Misfolded Proteins, Amyloid-β, Cholesterol, and Aging

Journal of child neurology, 2003-03, Vol.18 (3), p.185-190

2003

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Amyloid- beta 42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis

Acta neuropathologica, 2009-05, Vol.117 (5), p.569-574

2009

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

Acta neuropathologica, 2010-11, Vol.120 (5), p.661-666

2010

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Assessment: symptomatic treatment for muscle cramps (an evidence-based review): report of the Therapeutics and Technology Assessment Subcommittee of the American Academy of Neurology

Neurology, 2010-10, Vol.75 (15), p.1397; author reply 1398-1399

Mauskop, Alexander

2010

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Presence of BACE1 and BACE2 in muscle fibres of patients with sporadic inclusion-body myositis

The Lancet (British edition), 2001-12, Vol.358 (9297), p.1962-1964

2001

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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

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

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

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

Luminescent Conjugated Oligothiophenes for Sensitive Fluorescent Assignment of Protein Inclusion Bodies

Sporadic inclusion-body myositis: A degenerative muscle disease associated with aging, impaired muscle protein homeostasis and abnormal mitophagy

Sodium phenylbutyrate reverses lysosomal dysfunction and decreases amyloid-β42 in an in vitro-model of inclusion-body myositis

Activation of the γ-secretase complex and presence of γ-secretase-activating protein may contribute to Aβ42 production in sporadic inclusion-body myositis muscle fibers

Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanisms

Diagnostic histochemistry and clinical-pathological testings as molecular pathways to pathogenesis and treatment of the ageing neuromuscular system: a personal view

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

Inclusion-body myositis: A myodegenerative conformational disorder associated with Aβ, protein misfolding, and proteasome inhibition

Molecular pathology and pathogenesis of inclusion-body myositis

Inclusion-body myositis, a multifactorial muscle disease associated with aging: current concepts of pathogenesis

Inclusion-body myositis: clinical, diagnostic, and pathologic aspects

Activation of the Unfolded Protein Response in Sporadic Inclusion-Body Myositis but Not in Hereditary GNE Inclusion-Body Myopathy

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

Sporadic inclusion-body myositis and hereditary inclusion-body myopathies: current concepts of diagnosis and pathogenesis

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

Dysferlin is a newly identified binding partner of AβPP and it co-aggregates with amyloid-β42 within sporadic inclusion-body myositis (s-IBM) muscle fibers

Unfolding Story of Inclusion-Body Myositis and Myopathies: Role of Misfolded Proteins, Amyloid-β, Cholesterol, and Aging

Amyloid- beta 42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis

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

Assessment: symptomatic treatment for muscle cramps (an evidence-based review): report of the Therapeutics and Technology Assessment Subcommittee of the American Academy of Neurology

Presence of BACE1 and BACE2 in muscle fibres of patients with sporadic inclusion-body myositis

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