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dc.contributor.authorZhang, X.en
dc.contributor.authorAdwal, A.en
dc.contributor.authorTurner, A.en
dc.contributor.authorCallen, D.en
dc.contributor.authorAbell, A.en
dc.identifier.citationACS Medicinal Chemistry Letters, 2016; 7(12):1039-1043en
dc.descriptionPublication Date (Web): September 13, 2016en
dc.description.abstractProteasome is a large proteinase complex that degrades proteins via its three catalytic activities. Among these activities, the “chymotrypsin-like” activity has emerged as the focus of drug discovery in cancer therapy. Here, we report new peptidomimetic boronates that are highly specific for the chymotrypsin-like catalytic activity of the proteasome. These new specific proteasome inhibitors were demonstrated to have higher in vitro potency and selective cytotoxicity for cancer cells compared to benchmark proteasome inhibitors: bortezomib and carfilzomib. In breast cancer cell lines, treatment with 1a or 2a induced accumulation of the high molecular weight polyubiqutinated proteins at similar levels observed for bortezomib and carfilzomib, indicating that cancer cell death caused by 1a/2a is chiefly due to proteasome inhibition.en
dc.description.statementofresponsibilityXiaozhou Zhang, Alaknanda Adwal, Andrew G. Turner, David F. Callen, and Andrew D. Abellen
dc.publisherAmerican Chemical Societyen
dc.rights© American Chemical Societyen
dc.subject26S proteasome inhibitors; boronic ester; chymotrypsin-like activity; immunoproteasome; solid canceren
dc.titleNew peptidomimetic boronates for selective inhibition of the chymotrypsin-like activity of the 26S proteasomeen
dc.typeJournal articleen
pubs.library.collectionMedical Sciences publicationsen
dc.identifier.orcidCallen, D. [0000-0002-6189-9991]en
dc.identifier.orcidAbell, A. [0000-0002-0604-2629]en
Appears in Collections:Medical Sciences publications

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