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Med"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1111\/j.1651-2227.1988.tb10767.x","article-title":"The natural history of liver disease in alpha 1 antitrypsin deficient children","volume":"77","author":"T Sveger","year":"1988","journal-title":"Acta Peadiatr Scand"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"2076","DOI":"10.1378\/chest.128.4.2076","article-title":"Alpha 1 antitrypsin deficiency in 26 years-old subjects: lung, liver and protease\/protease inhibitor studies","volume":"128","author":"E Piitulainen","year":"2005","journal-title":"Chest"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"22791","DOI":"10.1074\/jbc.271.37.22791","article-title":"Degradation of a mutant secretory protein, alpha1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity","volume":"271","author":"D Qu","year":"1996","journal-title":"J Biol 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inducible mouse model unravels ubiquitin\/proteasome system impairment and permanent recovery attributable to aggregate formation","volume":"30","author":"Z Ortega","year":"2010","journal-title":"J Neurosci"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1146\/annurev.biochem.67.1.425","article-title":"The ubiquitin system","volume":"67","author":"A Hershko","year":"1998","journal-title":"Annu Rev Biochem"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1093\/hmg\/10.10.1049","article-title":"Altered proteasomal function due to the expression of polyglutamine expanded truncated N-terminal huntingtin induces apoptosis by caspase activation through mitochondrial cytochrome c release","volume":"10","author":"NR Jana","year":"2001","journal-title":"Hum Mol Genet"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1097\/00001756-200308060-00006","article-title":"Impaired degradation of PKCalpha by proteasome in a 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Bennett","year":"2005","journal-title":"Mol Cell"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"34150","DOI":"10.1074\/jbc.M204955200","article-title":"A rhodopsin mutant linked to autosomal dominant retinitis pigmentosa is prone to aggregate and interacts with the ubiquitin-proteasome system","volume":"277","author":"ME Illing","year":"2002","journal-title":"J Biol Chem"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"1007","DOI":"10.1016\/S0896-6273(02)01125-X","article-title":"Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome disfunction selectively affects catecholaminergic neurons","volume":"36","author":"L Petrucelli","year":"2002","journal-title":"Neuron"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1093\/hmg\/ddg161","article-title":"Transglutaminase potentiates ligand-dependent proteasome disfunction induced by polyglutamine-expanded androgen receptor","volume":"12","author":"LM Mandrusiak","year":"2003","journal-title":"Hum Mol Genet"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.1242\/jcs.03438","article-title":"Dose-dependent inhibition of proteasome activity by a mutant ubiquitin associated with neurodegenerative disease","volume":"120","author":"P Van Tijn","year":"2007","journal-title":"J Cell Sci"},{"key":"ref54","first-page":"713","article-title":"Prions and the proteasome Biochim Biophys Acta","volume":"1782","author":"P Deriziotis","year":"2008"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1083\/jcb.201110093","article-title":"Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease","volume":"196","author":"M Hipp","year":"2012","journal-title":"J Cell Biol"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"1325","DOI":"10.1111\/j.1471-4159.2004.02453.x","article-title":"Focal dysfunction of the proteasome: a pathogenic factor in a mouse model of 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activity","volume":"101","author":"F Gillardon","year":"2007","journal-title":"J Neurochem"},{"key":"ref60","first-page":"187","article-title":"Theory and Practice of Histological Techniques","author":"J Bancroft","year":"1980","journal-title":"Churchill-Livingstone NY 2"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"1300","DOI":"10.1016\/S0960-9822(07)00560-X","article-title":"The univector plasmid-fusion system, a method for rapid construction of recombinant DNA without restriction enzymes","volume":"8","author":"Q Liu","year":"1998","journal-title":"Current Biology"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1006\/jsbi.1999.4174","article-title":"EMAN: semiautomated software for high-resolution single-particle reconstructions","volume":"128","author":"SJ Ludtke","year":"1999","journal-title":"J Struct Biol"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1006\/jsbi.1996.0030","article-title":"SPIDER and WEB: processing and visualization of images in 3D electron microscopy and other fields","volume":"116","author":"J Frank","year":"1996","journal-title":"J Structural Biology"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"10403","DOI":"10.1073\/pnas.96.18.10403","article-title":"Epoxomycin, a potent and selective proteasome inhibitor, exhibits in vivo anti-inflammatory activity","volume":"96","author":"L Meng","year":"1999","journal-title":"Proc Natl Acad Sci USA"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"8582","DOI":"10.1074\/jbc.M509043200","article-title":"Importance of the different proteolytic sites of the proteasome and the efficacy of inhibitors varies with the protein substrate","volume":"281","author":"AF Kisselev","year":"2006","journal-title":"J Biol Chem"},{"key":"ref66","first-page":"183421","article-title":"Cdc48: A Swiss Army Knife of Cell Biology","volume":"2013","author":"GH Baek","year":"2013","journal-title":"J Amino 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