Cathepsin D in wild-type and Nuc1 RPE

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Invest. Ophthalmol. Vis. Sci ;44(9): doi: /iovs Figure Legend:
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Reduced copurification of selected co-opted host proteins with the viral replicase from yeast coexpressing WW-domain protein. Reduced copurification of.
A B CDK2 CDK2 inhibition P Activated KRAS P CP110 CP110
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Efficient copurification of selected co-opted host proteins with the viral replicase from yeast coexpressing TPR-domain protein or cyclophilin A (CypA).
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Expression of SvkA during development and induction of cytofission.
Caspases are activated earlier in young TA (yTA) than in KSC
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Figure Lysosome dysfunction observed in patient-derived fibroblasts with the TMEM106B p.Asp252Asn substitution Lysosome dysfunction observed in patient-derived.
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Induction of PARP cleavage (A) and activation of caspases (B) after treatment with a combination of TRAIL and cisplatin. Induction of PARP cleavage (A)
Fig. 6 The C9ORF72/SMCR8 complex regulates ULK1.
Fig. 3. Association between peak CTL019 expansion and response.
Expression of MtrE by wild-type and mtr120 mutant strains.
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Cathepsin D in wild-type and Nuc1 RPE Cathepsin D in wild-type and Nuc1 RPE. Western blotting with cathepsin D antibody. Cathepsin D in wild-type and Nuc1 RPE. Western blotting with cathepsin D antibody. RPE samples were as follows: Lane 1, 2-month-old wild type; lane 2, 2-month-old Nuc1; lane 3, 8-month-old wild type; lane 4, 8-month-old Nuc1. The immature (inactive) pro-enzyme form of cathepsin is present in all samples. The mature (active) form of the enzyme is present in the wild-type samples, but is barely detectable in the Nuc1 samples. Actin is shown as a loading control. J. Samuel Zigler, Jr et al. J Cell Sci 2011;124:523-531 © 2011.