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Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology

Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_68610019

Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology

About this item

Full title

Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology

Publisher

London: Nature Publishing Group UK

Journal title

Nature cell biology, 2006-07, Vol.8 (7), p.700-710

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Protein ubiquitination regulates many cellular processes, including protein degradation, signal transduction, DNA repair and cell division. In the classical model, a uniform polyubiquitin chain that is linked through Lys 48 is required for recognition and degradation by the 26S proteasome. Here, we used a reconstituted system and quantitative mass...

Alternative Titles

Full title

Quantitative analysis of in vitro ubiquitinated cyclin B1 reveals complex chain topology

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_proquest_miscellaneous_68610019

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_68610019

Other Identifiers

ISSN

1465-7392

E-ISSN

1476-4679

DOI

10.1038/ncb1436

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