CORD-19:ba334a8f734285257878e0df4e64a6131818d0c6 / 20891-21227 JSONTXT

{"project":"CORD-19_Custom_license_subset","denotations":[{"id":"T100","span":{"begin":0,"end":336},"obj":"Sentence"}],"text":"Bacterial expression of the latter (i.e., ub-nsp12-His 6 ) still resulted in an unstable protein, but co-expression of the ubiquitin protease Ubp1, which can hydrolyse the ub-nsp12 fusion site to produce a recombinant nsp12-His 6 containing the natural nsp12 N-terminus, significantly improved its stability (te Velthuis et al., 2010a)."}

{"project":"CORD-19-Sentences","denotations":[{"id":"TextSentencer_T100","span":{"begin":0,"end":336},"obj":"Sentence"},{"id":"T29875","span":{"begin":0,"end":336},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Bacterial expression of the latter (i.e., ub-nsp12-His 6 ) still resulted in an unstable protein, but co-expression of the ubiquitin protease Ubp1, which can hydrolyse the ub-nsp12 fusion site to produce a recombinant nsp12-His 6 containing the natural nsp12 N-terminus, significantly improved its stability (te Velthuis et al., 2010a)."}

{"project":"Epistemic_Statements","denotations":[{"id":"T37","span":{"begin":0,"end":336},"obj":"Epistemic_statement"}],"text":"Bacterial expression of the latter (i.e., ub-nsp12-His 6 ) still resulted in an unstable protein, but co-expression of the ubiquitin protease Ubp1, which can hydrolyse the ub-nsp12 fusion site to produce a recombinant nsp12-His 6 containing the natural nsp12 N-terminus, significantly improved its stability (te Velthuis et al., 2010a)."}