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

Journal of neuropathology and experimental neurology, 2012-08, Vol.71 (8), p.680-693

2012

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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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Endoplasmic Reticulum Stress and Unfolded Protein Response in Inclusion Body Myositis Muscle

The American journal of pathology, 2004, Vol.164 (1), p.1-7

2004

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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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Novel demonstration of conformationally modified tau in sporadic inclusion-body myositis muscle fibers

Neuroscience letters, 2011-10, Vol.503 (3), p.229-233

2011

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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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Endoplasmic reticulum stress induces myostatin precursor protein and NF-κB in cultured human muscle fibers: Relevance to inclusion body myositis

Experimental neurology, 2007-04, Vol.204 (2), p.610-618

2007

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Inclusion-Body Myositis: Newest Concepts of Pathogenesis and Relation to Aging and Alzheimer Disease

Journal of neuropathology and experimental neurology, 2001-01, Vol.60 (1), p.1-14

2001

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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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Homocysteine‐induced endoplasmic reticulum protein (Herp) is up‐regulated in sporadic inclusion‐body myositis and in endoplasmic reticulum stress‐induced cultured human muscle fibers

Journal of neurochemistry, 2006-03, Vol.96 (5), p.1491-1499

2006

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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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Cystatin C colocalizes with amyloid‐β and coimmunoprecipitates with amyloid‐β precursor protein in sporadic inclusion‐body myositis muscles

Journal of neurochemistry, 2003-06, Vol.85 (6), p.1539-1546

2003

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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

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

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

Endoplasmic Reticulum Stress and Unfolded Protein Response in Inclusion Body Myositis Muscle

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

Novel demonstration of conformationally modified tau in sporadic inclusion-body myositis muscle fibers

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

Endoplasmic reticulum stress induces myostatin precursor protein and NF-κB in cultured human muscle fibers: Relevance to inclusion body myositis

Inclusion-Body Myositis: Newest Concepts of Pathogenesis and Relation to Aging and Alzheimer Disease

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

Homocysteine‐induced endoplasmic reticulum protein (Herp) is up‐regulated in sporadic inclusion‐body myositis and in endoplasmic reticulum stress‐induced cultured human muscle fibers

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

Cystatin C colocalizes with amyloid‐β and coimmunoprecipitates with amyloid‐β precursor protein in sporadic inclusion‐body myositis muscles

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