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Lett."},{"key":"10.1016\/j.jmb.2019.10.013_bib145","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/s00401-008-0402-2","article-title":"White matter lesions in the brain with frontotemporal lobar degeneration with motor neuron disease: TDP-43-immunopositive inclusions co-localize with p62, but not ubiquitin","volume":"116","author":"Hiji","year":"2008","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.jmb.2019.10.013_bib146","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.bbrc.2014.10.066","article-title":"NDP52 associates with phosphorylated tau in brains of an Alzheimer disease mouse model","volume":"454","author":"Kim","year":"2014","journal-title":"Biochem. Biophys. Res. 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A."},{"key":"10.1016\/j.jmb.2019.10.013_bib192","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1182\/blood-2018-02-833475","article-title":"Loss of the selective autophagy receptor p62 impairs murine myeloid leukemia progression and mitophagy","volume":"133","author":"Nguyen","year":"2019","journal-title":"Blood"},{"key":"10.1016\/j.jmb.2019.10.013_bib193","doi-asserted-by":"crossref","first-page":"27879","DOI":"10.1074\/jbc.M110.119537","article-title":"Nix is critical to two distinct phases of mitophagy, reactive oxygen species-mediated autophagy induction and Parkin-ubiquitin-p62-mediated mitochondrial priming","volume":"285","author":"Ding","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.jmb.2019.10.013_bib194","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1038\/ncb2012","article-title":"PINK1\/Parkin-mediated mitophagy is dependent on VDAC1 and p62\/SQSTM1","volume":"12","author":"Geisler","year":"2010","journal-title":"Nat. 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