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1 agy-regulatory proteins LC3 (LC3-II) and p62/Sequestosome.
2 show that deficiency of either autophagy or sequestosome 1 (p62 or SQSTM) led to inflammasome hypera
3 nscription factor resulting from accumulated sequestosome 1 (SQSTM1 or p62) in Atg7(-)/(-) macrophage
5 ochondrial association of autophagosomal p62/sequestosome 1 (SQSTM1) and processed microtubule-associ
7 anonical ubiquitin-like autophagy receptors [sequestosome 1 (SQSTM1), microtubule-associated protein
8 umorigenesis, genetic down-regulation of p62/sequestosome 1 (SQSTM1), the autophagy substrate that ac
13 FHOD3 also prevents its interaction with p62/sequestosome 1 and its recruitment to autophagosomes.
14 er autophagy-mediated down-regulation of p62/sequestosome 1 contributes to its pro-survival role, we
17 d protein-1 light chain beta II (LC3II), and sequestosome 1(SQSTM1), in a membrane-enriched fraction,
19 d phosphorylated the autophagic adaptor p62 (sequestosome 1) on Ser-403, a residue essential for its
20 he levels of the autophagy-cargo protein p62/sequestosome 1, and the lipidated form of microtubule-as
25 athways and enhances the interaction between sequestosome 1/p62 and caspase-8, which leads to the agg
26 that increased levels of the adaptor protein Sequestosome 1/p62 are observed in human breast cancers
27 hat the ubiquitin-associated (UBA) domain of sequestosome 1/p62 displays a preference for binding K63
28 tudies have shown that deletion of the mouse sequestosome 1/p62 gene results in mature-onset obesity
29 at the SH(2) domain at the amino terminus of sequestosome 1/p62 interacts with IRS-1 upon insulin sti
32 Autophagic adaptors referred to as SLRs (sequestosome 1/p62-like receptors) are themselves a cate
36 idate mitophagy receptors optineurin (OPTN), sequestosome-1 (p62), and nuclear dot protein 52 (NDP52)
38 ress but dependent on the autophagic protein sequestosome-1 (SQSTM1), which was involved in the degra
41 e otherwise unrelated Ub-binding protein p62/Sequestosome-1 have been shown to be sequestered into ag
42 ition, rifampicin decreased the level of p62/sequestosome-1 in the brain without affecting the increa
43 mechanism, the autophagic adapter p62/SQSTM1/Sequestosome-1 is an N-recognin that binds type-1 and ty
45 the interaction surface for the adaptor p62/Sequestosome-1, which is required for IL-1 signaling to
48 including optineurin (OPTN) and p62 (SQSTM1/sequestosome), both of which have also been implicated i
49 such fusion proteins, SET-Nup214 and SQSTM1 (sequestosome)-Nup214, both containing C-terminal portion
50 of TRAF6 was apparently mediated by the p62 sequestosome protein, which is a factor important for se
51 ved proteins (SLiPs) into autophagosomes via sequestosome (SQSTM1, p62) mediated association of ubiqu
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