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Article

Protein interactions within the N-end rule ubiquitin ligation pathway.

The Journal of biological chemistry - 14 Mar 2003

Siepmann Thomas J, Bohnsack Richard N, Tokgöz Zeynep, Baboshina Olga V, Haas Arthur L

Abstract excerpt

Rate studies have been employed as a reporter function to probe protein-protein interactions within a biochemically defined reconstituted N-end rule ubiquitin ligation pathway. The concentration dependence for E1-catalyzed HsUbc2b/E2(14kb) transthiolation is hyperbolic and yields K(m) values of 102 +/- 13 nm and 123 +/- 19 nm for high affinity binding to rabbit and human E1/Uba1 orthologs. Competitive inhibition...

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PMID: 12524449
DOI: 10.1074/jbc.M211240200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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