The interplay between protein phosphorylation and ubiquitylation in the NF-ĸB pathway [electronic resource] / Zhijian 'James' Chen.

By: Chen, Zhijian 'James' [spk]Material type: FilmFilmSeries: Henry Stewart talksBiomedical & life sciences collection. Protein phosphorylation: Publisher: London : Henry Stewart Talks, 2010Description: 1 online resource (1 streaming video file (30 min.) : color, sound)Subject(s): NF-kappa B | Phosphorylation | UbiquitinationOnline resources: Click here to access online | Series
Contents:
Contents: Ubiquitination is a reversible covalent modification, akin to phosphorylation -- Ubiquitination regulates protein kinase activity through proteasome-independent mechanisms -- K63-linked polyubiquitination activates TAK1 and IKK in the NF-kappaB pathway -- Deubiquitination enzymes inhibit protein kinases in the NF-kappaB pathway -- Protein kinase regulation by ubiquitin is important in innate and adaptive immunity.
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Animated audio-visual presentation with synchronized narration.

Title from title frames.

Contents: Ubiquitination is a reversible covalent modification, akin to phosphorylation -- Ubiquitination regulates protein kinase activity through proteasome-independent mechanisms -- K63-linked polyubiquitination activates TAK1 and IKK in the NF-kappaB pathway -- Deubiquitination enzymes inhibit protein kinases in the NF-kappaB pathway -- Protein kinase regulation by ubiquitin is important in innate and adaptive immunity.

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