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1 hromosome 10p14 and designated it OPTN (for "optineurin").
2 uitin and subsequent recruitment of Nemo and Optineurin.
5 . cerevisiae Atg19, Atg34 and the human p62, Optineurin and NDP52 cargo receptors interact with the E
11 functional complex consisting of myosin VI, optineurin, and probably the GTPase Rab8 plays a role in
12 dimeric cargo adaptor protein of myosin VI, optineurin, and the myosin VI-binding segment from a mon
13 uilin 2, p62, valosin-containing protein and optineurin are all linked to aggrephagy, a cargo-specifi
14 of optineurin in mitophagy, as mutations in optineurin are causative for amyotrophic lateral scleros
16 rs previously linked to xenophagy, NDP52 and optineurin, are the primary receptors for PINK1- and par
17 In a yeast 2-hybrid screen we identified optineurin as a binding partner for myosin VI at the Gol
18 our study establishes an important role for optineurin as an autophagy receptor in parkin-mediated m
19 ucose-transporter binding protein (GIPC) and optineurin binding and a site that binds specifically an
20 On the other hand, the overexpression of optineurin blocks the protective effect of E3-14.7K on c
21 d by expression of siRNA-resistant wild-type optineurin, but not by an ALS-associated mutant in the u
23 complex containing IKKalpha and IKKbeta, and optineurin cannot substitute for NEMO in lipopolysacchar
24 found three genes associated with glaucoma, optineurin, cochlin, and CYP1B1 (cytochrome P450, family
27 In contrast, neither transfection of the optineurin constructs pOPTN(WT)-EGFP and pOPTN(E50K)-EGF
28 The autophagy cargo receptors p62, NDP52 and Optineurin detect incoming bacteria that have become ass
29 ed that the two glaucoma genes, myocilin and optineurin, exhibited differential effects on neurite ou
31 n is a homolog of NEMO, and mutations in the optineurin gene are found in a subset of patients with g
33 encoding myocilin and the gene OPTN encoding optineurin have been identified to harbor causal mutatio
35 utes for protein clearance, in processing of optineurin in a retinal ganglion cell model line RGC5 an
36 These results reveal a physiologic role for optineurin in dampening TNFalpha signaling, and this rol
50 -expressed wild-type and mutant myocilin and optineurin on neurite outgrowth in neuronal cells, we tr
51 al sclerosis (ALS)-associated genes, such as optineurin (OPTN) and angiogenin (ANG), showed that the
52 in innate immunity and autophagy, including optineurin (OPTN) and p62 (SQSTM1/sequestosome), both of
60 NEMO)-related polyubiquitin-binding protein, optineurin (OPTN), as a novel binding partner of TBK1.
62 ed mitochondria requires autophagy receptors optineurin (OPTN), NDP52 (CALCOCO2), TAX1BP1, and p62 (S
64 nce binding to candidate mitophagy receptors optineurin (OPTN), sequestosome-1 (p62), and nuclear dot
67 FP-N1 (mock control) as well as myocilin and optineurin plasmids including pMYOC(WT)-EGFP, pMYOC(P370
68 sion and tissue distribution between the two optineurin proteins suggests that this nonhuman primate
69 oreactive to anti-ubiquitin were seen in the optineurin pulldown, indicating that optineurin was ubiq
70 Once recruited to mitochondria, NDP52 and optineurin recruit the autophagy factors ULK1, DFCP1 and
72 protein levels because microRNA silencing of optineurin resulted in markedly enhanced TNFalpha-induce
74 FP and pOPTN(E50K)-EGFP nor the myocilin and optineurin small-interfering RNA treatments induced sign
75 oversial, with in vitro studies finding that optineurin suppressed TNF-mediated NF-kappaB activation
76 In cells overexpressing wild type and E50K optineurin, the level of the proteasome regulatory beta5
78 onstrate the parkin-dependent recruitment of optineurin to mitochondria damaged by depolarization or
79 er mitochondrial membrane proteins, allowing optineurin to stably associate with ubiquitinated mitoch
82 in binding domain; in the absence of parkin, optineurin transiently localizes to damaged mitochondria
84 ed macrophages (BMDMs) from mice carrying an optineurin Ub-binding point mutation had normal TLR-medi
85 ion, we generated a mouse in which wild-type optineurin was replaced by the polyubiquitin binding-def
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