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dc.contributor.authorCecilia A. Souto-Guevara
dc.contributor.authorDiego Obiol
dc.contributor.authorCamila L. Bruno
dc.contributor.authorMariela S. Ferreira-Gomes
dc.contributor.authorJuan Pablo F. C. Rossi
dc.contributor.authorMarcelo D. Costabel
dc.contributor.authorIrene C. Mangialavori
dc.contributor.otherUniversidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Instituto de Química y Fisicoquímica Biológicas Dr. Alejandro Paladini (IQUIFIB)
dc.contributor.otherDepartamento de Física, Instituto de Física del Sur (IFISUR), Universidad Nacional del Sur (UNS), CONICET
dc.contributor.otherUniversidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Instituto de Química y Fisicoquímica Biológicas Dr. Alejandro Paladini (IQUIFIB)
dc.contributor.otherUniversidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Instituto de Química y Fisicoquímica Biológicas Dr. Alejandro Paladini (IQUIFIB)
dc.contributor.otherUniversidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Instituto de Química y Fisicoquímica Biológicas Dr. Alejandro Paladini (IQUIFIB)
dc.contributor.otherDepartamento de Física, Instituto de Física del Sur (IFISUR), Universidad Nacional del Sur (UNS), CONICET
dc.contributor.otherUniversidad de Buenos Aires, Facultad de Farmacia y Bioquímica, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Instituto de Química y Fisicoquímica Biológicas Dr. Alejandro Paladini (IQUIFIB)
dc.date.accessioned2024-06-30T11:19:45Z
dc.date.accessioned2025-10-08T08:27:15Z
dc.date.available2025-10-08T08:27:15Z
dc.date.issued01-06-2024
dc.identifier.urihttp://digilib.fisipol.ugm.ac.id/repo/handle/15717717/35934
dc.description.abstractAbstract Our research aimed to elucidate the mechanism by which aurintricarboxylic acid (ATA) inhibits plasma membrane Ca2+-ATPase (PMCA), a crucial enzyme responsible for calcium transport. Given the pivotal role of PMCA in cellular calcium homeostasis, understanding how it is inhibited by ATA holds significant implications for potentially regulating physiopathological cellular processes in which this pump is involved. Our experimental findings revealed that ATA employs multiple modes of action to inhibit PMCA activity, which are influenced by ATP but also by the presence of calcium and magnesium ions. Specifically, magnesium appears to enhance this inhibitory effect. Our experimental and in-silico results suggest that, unlike those reported in other proteins, ATA complexed with magnesium (ATA·Mg) is the molecule that inhibits PMCA. In summary, our study presents a novel perspective and establishes a solid foundation for future research efforts aimed at the development of new pharmacological molecules both for PMCA and other proteins.
dc.language.isoEN
dc.publisherNature Portfolio
dc.subject.lccMedicine
dc.titleMagnesium enhances aurintricarboxylic acid’s inhibitory action on the plasma membrane Ca2+-ATPase
dc.typeArticle
dc.description.keywordsPMCA, Plasma membrane Ca2+-ATPase
dc.description.keywordsATA, Inhibition mechanism
dc.description.keywordsATA-magnesium complex
dc.description.keywordsATA-binding site
dc.description.pages1-14
dc.description.doi10.1038/s41598-024-65465-8
dc.title.journalScientific Reports
dc.identifier.e-issn2045-2322
dc.identifier.oai543e1c90e7a44920bfb13a106b850f4b
dc.journal.infoVolume 14, Issue 1


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