Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler
Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler
About this item
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Author / Creator
Liwocha, Joanna , Krist, David T. , van der Heden van Noort, Gerbrand J. , Hansen, Fynn M. , Truong, Vinh H. , Karayel, Ozge , Purser, Nicholas , Houston, Daniel , Burton, Nicole , Bostock, Mark J. , Sattler, Michael , Mann, Matthias , Harrison, Joseph S. , Kleiger, Gary , Ovaa, Huib and Schulman, Brenda A.
Publisher
New York: Nature Publishing Group US
Journal title
Language
English
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Publication information
Publisher
New York: Nature Publishing Group US
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Scope and Contents
Contents
Virtually all aspects of cell biology are regulated by a ubiquitin code where distinct ubiquitin chain architectures guide the binding events and itineraries of modified substrates. Various combinations of E2 and E3 enzymes accomplish chain formation by forging isopeptide bonds between the C terminus of their transiently linked donor ubiquitin and...
Alternative Titles
Full title
Linkage-specific ubiquitin chain formation depends on a lysine hydrocarbon ruler
Authors, Artists and Contributors
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Primary Identifiers
Record Identifier
TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7904580
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7904580
Other Identifiers
ISSN
1552-4450
E-ISSN
1552-4469
DOI
10.1038/s41589-020-00696-0
