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High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moieties

High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moieties

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_733934287

High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moieties

About this item

Full title

High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moieties

Publisher

London: Nature Publishing Group UK

Journal title

Nature protocols, 2010-05, Vol.5 (5), p.873-882

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

The post-translational modification of proteins with ubiquitin and ubiquitin-like proteins (Ubl) is vital to many cellular functions, and thus the identification of Ubl targets is key to understanding their function. In most cases, only a small proportion of the cellular pool of proteins is found conjugated to a particular Ubl, making identificatio...

Alternative Titles

Full title

High-stringency tandem affinity purification of proteins conjugated to ubiquitin-like moieties

Authors, Artists and Contributors

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_733934287

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_733934287

Other Identifiers

ISSN

1754-2189

E-ISSN

1750-2799

DOI

10.1038/nprot.2010.40

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