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Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_8431d5b994ec4a4ca5d12daa3a68d3a3

Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

About this item

Full title

Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2016-10, Vol.7 (1), p.12960-12960, Article 12960

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Ubiquitin receptors decode ubiquitin signals into many cellular responses. Ubiquitin receptors also undergo coupled monoubiquitylation, and rapid deubiquitylation has hampered the characterization of the ubiquitylated state. Using bacteria that express a ubiquitylation apparatus, we purified and determined the crystal structure of the proteasomal u...

Alternative Titles

Full title

Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_8431d5b994ec4a4ca5d12daa3a68d3a3

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_8431d5b994ec4a4ca5d12daa3a68d3a3

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/ncomms12960

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