Show simple item record

dc.contributor.authorDange, Thomas
dc.contributor.authorSmith, David
dc.contributor.authorNoy, Tahel
dc.contributor.authorRommel, Philipp C.
dc.contributor.authorJurzitza, Lukas
dc.contributor.authorCordero, Radames B.
dc.contributor.authorLegendre, Anne
dc.contributor.authorFinley, Daniel
dc.contributor.authorGoldberg, Alfred L.
dc.contributor.authorSchmidt, Marion
dc.date.accessioned2019-10-05T09:46:55Z
dc.date.issued2011
dc.identifier.citationDange, Thomas, David Smith, Tahel Noy, Philipp C. Rommel, Lukas Jurzitza, Radames J. B. Cordero, Anne Legendre, Daniel Finley, Alfred L. Goldberg, and Marion Schmidt. 2011. “Blm10 Protein Promotes Proteasomal Substrate Turnover by an Active Gating Mechanism.” Journal of Biological Chemistry 286 (50): 42830–39. https://doi.org/10.1074/jbc.m111.300178.
dc.identifier.issn0021-9258
dc.identifier.issn1083-351X
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:41483170*
dc.description.abstractBackground: Association of the proteasome core with activators regulates proteasome activity. Results: Blm10 association increases proteasome activity toward peptides and the unstructured proteasome substrate tau-441. This process is mediated by the C terminus of Blm10. Conclusion: C-terminal docking-mediated proteasome activation by Blm10 facilitates the turnover of peptide and protein substrates.Significance: Blm10 contributes to the regulation of proteasome activity.
dc.language.isoen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology
dash.licenseLAA
dc.titleBlm10 Protein Promotes Proteasomal Substrate Turnover by an Active Gating Mechanism
dc.typeJournal Article
dc.description.versionVersion of Record
dc.relation.journalThe Journal of Biological Chemistry
dash.depositing.authorFinley, Daniel::55733c495443e58aeebdb3090cda00e5::600
dc.date.available2019-10-05T09:46:55Z
dash.workflow.comments1Science Serial ID 109711
dc.identifier.doi10.1074/jbc.M111.300178
dash.source.volume286;50
dash.source.page42830


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record