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Exploring the role of p97 and its UBX-domain cofactors through identification of their interacting proteins

Exploring the role of p97 and its UBX-domain cofactors through identification of their interacting proteins

Research output: Chapter in Book/Report/Conference proceedingChapter (peer-reviewed)

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Info

Original languageEnglish
TitleUbiquitin family modifiers and the proteasome
Subtitlereviews and protocols
EditorsR. Jürgen Dohmen , Martin Scheffner
PublisherHumana Press
Publication date2012
Pages305-312
Number of pages8
ISBN (Electronic)9781617794742
ISBN (Print)9781617794735
DOIs
StatePublished

Publication series

NameMethods in molecular biology
PublisherHumana Press
Volume832
ISSN (Print)1064-3745

Abstract

The elucidation of protein-protein interaction networks can provide preliminary insights into the function of uncharacterized proteins based on the interactions they establish in the cell. Here, we describe a protein immunoprecipitation protocol that can be used in combination with mass spectrometry analysis to identify the p97 interactome as well as specific subgroups of proteins interacting with its UBX-domain adaptors. This approach aims to dissect the role played by individual UBX cofactors within the complex array of cellular functions performed by p97. © 2012 Springer Science+Business Media, LLC.

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