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
- 30 April 2011
- journal article
- review article
- Published by Elsevier BV in La Presse Médicale
- Vol. 40 (4), e219-e235
- https://doi.org/10.1016/j.lpm.2010.11.024
Abstract
No abstract availableKeywords
This publication has 100 references indexed in Scilit:
- The ubiquitin proteasome system in neuropathologyActa Neuropathologica, 2009
- Role of Synucleins in Alzheimer’s DiseaseNeurotoxicity Research, 2009
- Sarcoplasmic redistribution of nuclear TDP‐43 in inclusion body myositisMuscle & Nerve, 2009
- Mechanisms of tau-induced neurodegenerationActa Neuropathologica, 2009
- Inclusion-body myositis: muscle-fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer’s and Parkinson’s disease brainsActa Neuropathologica, 2008
- Molecular mechanisms of α-synuclein neurodegenerationBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 2008
- In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidizedFree Radical Biology & Medicine, 2008
- Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositisNeuroscience Letters, 2008
- Aβ inhibits the proteasome and enhances amyloid and tau accumulationNeurobiology of Aging, 2007
- Endoplasmic reticulum stress induces myostatin precursor protein and NF-κB in cultured human muscle fibers: Relevance to inclusion body myositisExperimental Neurology, 2007