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W King Engel

Showing results (11-20 of 39) with videos related to

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Current Opinion in Neurology|September 28, 2002
Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanismsValerie Askanas, W King Engel
Journal of Child Neurology|May 7, 2003
Unfolding story of inclusion-body myositis and myopathies: role of misfolded proteins, amyloid-beta, cholesterol, and agingValerie Askanas, W King Engel
Brain Pathology (Zurich, Switzerland)|July 1, 2009
Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradationValerie Askanas, W King Engel, Anna Nogalska
Neuroscience Letters|March 19, 2010
Increased BACE1 mRNA and noncoding BACE1-antisense transcript in sporadic inclusion-body myositis muscle fibers--possibly caused by endoplasmic reticulum stressAnna Nogalska, W King Engel, Valerie Askanas
Biochimica Et Biophysica Acta|September 22, 2014
Sporadic inclusion-body myositis: A degenerative muscle disease associated with aging, impaired muscle protein homeostasis and abnormal mitophagyValerie Askanas, W King Engel, Anna Nogalska
Journal of Neuropathology and Experimental Neurology|July 19, 2012
Pathogenic considerations in sporadic inclusion-body myositis, a degenerative muscle disease associated with aging and abnormalities of myoproteostasisValerie Askanas, W King Engel, Anna Nogalska
The American Journal of Pathology|December 26, 2003
Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscleGaetano Vattemi, W King Engel, Janis McFerrin, et al.
Acta Neuropathologica|June 29, 2005
Myostatin is increased and complexes with amyloid-beta within sporadic inclusion-body myositis muscle fibersSławomir Wójcik, W King Engel, Janis McFerrin, et al.
Neurobiology of Disease|January 30, 2014
Sodium phenylbutyrate reverses lysosomal dysfunction and decreases amyloid-β42 in an in vitro-model of inclusion-body myositisAnna Nogalska, Carla D'Agostino, W King Engel, et al.
Journal of Neurochemistry|June 6, 2003
Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis musclesGaetano Vattemi, W King Engel, Janis McFerrin, et al.
Pageof 4

Showing results (11-20 of 39) with videos related to

Sort By:
Pageof 4
Current Opinion in Neurology|September 28, 2002
Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanismsValerie Askanas, W King Engel
Journal of Child Neurology|May 7, 2003
Unfolding story of inclusion-body myositis and myopathies: role of misfolded proteins, amyloid-beta, cholesterol, and agingValerie Askanas, W King Engel
Brain Pathology (Zurich, Switzerland)|July 1, 2009
Inclusion body myositis: a degenerative muscle disease associated with intra-muscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradationValerie Askanas, W King Engel, Anna Nogalska
Neuroscience Letters|March 19, 2010
Increased BACE1 mRNA and noncoding BACE1-antisense transcript in sporadic inclusion-body myositis muscle fibers--possibly caused by endoplasmic reticulum stressAnna Nogalska, W King Engel, Valerie Askanas
Biochimica Et Biophysica Acta|September 22, 2014
Sporadic inclusion-body myositis: A degenerative muscle disease associated with aging, impaired muscle protein homeostasis and abnormal mitophagyValerie Askanas, W King Engel, Anna Nogalska
Journal of Neuropathology and Experimental Neurology|July 19, 2012
Pathogenic considerations in sporadic inclusion-body myositis, a degenerative muscle disease associated with aging and abnormalities of myoproteostasisValerie Askanas, W King Engel, Anna Nogalska
The American Journal of Pathology|December 26, 2003
Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscleGaetano Vattemi, W King Engel, Janis McFerrin, et al.
Acta Neuropathologica|June 29, 2005
Myostatin is increased and complexes with amyloid-beta within sporadic inclusion-body myositis muscle fibersSławomir Wójcik, W King Engel, Janis McFerrin, et al.
Neurobiology of Disease|January 30, 2014
Sodium phenylbutyrate reverses lysosomal dysfunction and decreases amyloid-β42 in an in vitro-model of inclusion-body myositisAnna Nogalska, Carla D'Agostino, W King Engel, et al.
Journal of Neurochemistry|June 6, 2003
Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis musclesGaetano Vattemi, W King Engel, Janis McFerrin, et al.
Pageof 4