Inter-Site Cooperativity of Calmodulin N-Terminal Domain and Phosphorylation Synergistically Improve...
Inter-Site Cooperativity of Calmodulin N-Terminal Domain and Phosphorylation Synergistically Improve the Affinity and Selectivity for Uranyl
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Switzerland: MDPI AG
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English
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Switzerland: MDPI AG
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Uranyl-protein interactions participate in uranyl trafficking or toxicity to cells. In addition to their qualitative identification, thermodynamic data are needed to predict predominant mechanisms that they mediate in vivo. We previously showed that uranyl can substitute calcium at the canonical EF-hand binding motif of calmodulin (CaM) site I. Her...
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Inter-Site Cooperativity of Calmodulin N-Terminal Domain and Phosphorylation Synergistically Improve the Affinity and Selectivity for Uranyl
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TN_cdi_doaj_primary_oai_doaj_org_article_b00ced0c32114e55a3fa4838f0f0d24a
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_b00ced0c32114e55a3fa4838f0f0d24a
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ISSN
2218-273X
E-ISSN
2218-273X
DOI
10.3390/biom12111703
