| http://purl.uniprot.org/citations/10527495 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10527495 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10527495 | http://www.w3.org/2000/01/rdf-schema#comment | "We have used solid-phase chemistry to synthesize proteins equivalent to a human ubiquitin precursor (ubiquitin-52-amino-acid ribosomal protein fusion; UBICEP52) and representative of isopeptide-linked ubiquitin-protein conjugates [ubiquitin-(epsilonN)-lysine]; these proteins were precisely cleaved by a purified recombinant Drosophila deubiquitinating enzyme (DUB), UCH-D. Along with the previously synthesized ubiquitin-(alphaN)-valine, these synthetic proteins were used as substrates to assess the catalytic capacities of a number of diverse DUBs expressed in Escherichia coli: human HAUSP; mouse Unp; and yeast Ubps 1p, 2p, 3p, 6p, 11p, and 15p and Yuh1p. Distinct specificities of these enzymes were detected; notably, in addition to UCH-D, isopeptidase activity [ubiquitin-(epsilonN)-lysine cleavage] was only associated with Yuh1p, Unp, Ubp1p, and Ubp2p. Additionally, human placental 26S proteasomes were only able to cleave UBICEP52 and ubiquitin-(epsilonN)-lysine, suggesting that 26S proteasome-associated DUBs are class II-like. This work demonstrates that the synthetic approach offers an alternative to recombinant methods for the production of small proteins in vitro."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.org/dc/terms/identifier | "doi:10.1006/abio.1999.4234"xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.org/dc/terms/identifier | "doi:10.1006/abio.1999.4234"xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Brown A."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Brown A."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Wang P."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Wang P."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Layfield R."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Layfield R."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Landon M."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Landon M."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Baker R."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Baker R."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Mayer R.J."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Mayer R.J."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Love S."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Love S."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Ramage R."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Ramage R."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Muir T."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Muir T."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Franklin K."xsd:string |
| http://purl.uniprot.org/citations/10527495 | http://purl.uniprot.org/core/author | "Franklin K."xsd:string |