Ubiquitination-Induced Conformational Change within the Deiodinase Dimer Is a Switch Regulating Enzyme Activity

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 conformational change in a dimeric enzyme, which can be reversed upon deub...

पूर्ण विवरण

में बचाया:
ग्रंथसूची विवरण
मुख्य लेखकों: Sagar, G. D. Vivek, Gereben, Balázs, Callebaut, Isabelle, Mornon, Jean-Paul, Zeöld, Anikó, da Silva, Wagner S., Luongo, Cristina, Dentice, Monica, Tente, Susana M., Freitas, Beatriz C. G., Harney, John W., Zavacki, Ann Marie, Bianco, Antonio C.
स्वरूप: Artigo
भाषा:Inglês
प्रकाशित: American Society for Microbiology 2007
विषय:
Articles
ऑनलाइन पहुंच:https://ncbi.nlm.nih.gov/pmc/articles/PMC1951476/
https://ncbi.nlm.nih.gov/pubmed/17452445
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/MCB.00283-07
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