UBIQUITINATION-INDUCED CONFORMATIONAL CHANGE WITHIN THE DEIODINASE DIMER IS A SWITCH REGULATING ENZYME ACTIVITY

Autor: D. Vivek Sagar, G., Gereben, Balázs, Callebaut, Isabelle, Mornon, Jean-Paul, Zeöld, Anikó, S. da Silva, Wagner, Luongo, Cristina, Dentice, Monica, M. Tente, Susana, Beatriz, C., Freitas, G., W. Harney, John, Marie Zavacki, Ann, C. Bianco, Antonio

Publikováno v: Molecular Biology of the Cell
Molecular Biology of the Cell, 2007, 13, pp.4774-83. ⟨10.1128/MCB.00283-07⟩
Molecular Biology of the Cell, American Society for Cell Biology, 2007, 13, pp.4774-83. ⟨10.1128/MCB.00283-07⟩

International audience; Ubiquitination is a critical posttranslational regulator of protein stability and/or subcellular localization. Here we show that ubiquitination can also regulate proteins by transiently inactivating enzymatic function through

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::24f43e7c3a1df4fc0857e3a9f4b20302
https://hal.science/hal-00152172