IndraLab

Statements


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"For this, heterotypic Ub chains were assembled from 25 mg WT Ub, and the reaction was subsequently treated with OTUB1, which cleaved all Lys48-linkages within the polymers."

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"Immunoblot analysis revealed that ubiquitin chains were completely degraded by AMSH but neither by OTUB1 nor the GST control, further supporting our finding that TRIAD3 synthesises K63 linked ubiquitin chains in vitro, full length TRIAD3 protein as well as the TRIAD3-RBR 845 fragment."

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"OTUB1 has previously been reported to inhibit ubiquitylation of target proteins by interacting with and inhibiting E2 ubiquitin conjugating enzymes XREF_BIBR XREF_BIBR XREF_BIBR XREF_BIBR."

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"In sharp contrast, OTUB1 treatment diminished high-molecular-weight polyubiquitin chains and concomitantly caused the accumulation of short ubiquitin chains, indicating that the K48 linkage decorates [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In contrast to OTU1, which also negatively regulates ubiquitin-mediated degradation, Usp7 protein showed three-fold downregulation in CLas(+) organisms [8]."

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"These domains in OTUB1 are in close proximity to C23 and C204, raising the possibility that S-glutathionylation at either site regulates binding or orientation of either free Ub or E2-Ub enzyme."