We are analyzing https://link.springer.com/article/10.1007/s11010-005-6754-1.

Title:
Mitochondrial glycosidic residues contribute to the interaction between ruthenium amine complexes and the calcium uniporter | Molecular and Cellular Biochemistry
Description:
The role of glycosidic residues in the inhibitory properties of ruthenium complexes on mitochondrial calcium uptake was determined in mitoplasts. Our results showed that the binding and inhibitory properties of ruthenium amine complexes were modified when mitoplasts were exposed to N-glycosidase F action, but calcium uptake was not altered. N-linked proteins of the mitochondrial inner membrane were identified. We detected an 18-kDa protein that binds labeled Ru360 under control conditions, but failed to bind the inhibitor after deglycosilation. A relationship between this protein and the action of ruthenium amine inhibitors of the mitochondrial uniporter is proposed.
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Keywords {🔍}

google, scholar, cas, pubmed, article, mitochondrial, calcium, ruthenium, mitochondria, biochem, zazueta, transport, amine, uniporter, complexes, properties, complex, liver, biophys, privacy, cookies, content, biochemistry, cecilia, uptake, membrane, access, rat, bioenerg, biomembr, biol, chem, publish, search, correa, purification, inhibition, red, author, data, information, log, journal, research, molecular, cellular, glycosidic, residues, inhibitory, proteins,

Topics {✒️}

month download article/chapter ruthenium amine inhibitors dynamic o-linked glycosilation dubin–johnson–sprinz syndrome cecilia zazueta soluble ca2+-binding glyprotein mitochondrial calcium uniporter ruthenium amine complexes endogenous sialylated glycoproteins mitochondrial calcium uptake cellular biochemistry aims calcium uniporter published full article pdf mitochondrial ca2+ uniporter privacy choices/manage cookies mitochondrial calcium transport n-linked proteins article correa reverse uniport activity rat liver mitochondria rat heart mitochondria rat liver mitochondrial ox liver mitochondria beef heart mitochondria 2cl2] complex author correspondence mitochondrial ca2+ transport european economic area binds labeled ru360 check access apoptosis-inducing mechanism atpase c-subunit bovine serum albumin related subjects elsevier science publishers planar lipid bilayers fixed anionic sites single cardiac myocytes spleen cells induced extramitochondrial divalent cations x-ray structure colonia sección xvi instant access calcium uniporter mitochondrial outer membrane glycosidic residues mitochondrial uniporter deglycosilated glycoprotein hormones calcium uptake conditions privacy policy

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         description:The role of glycosidic residues in the inhibitory properties of ruthenium complexes on mitochondrial calcium uptake was determined in mitoplasts. Our results showed that the binding and inhibitory properties of ruthenium amine complexes were modified when mitoplasts were exposed to N-glycosidase F action, but calcium uptake was not altered. N-linked proteins of the mitochondrial inner membrane were identified. We detected an 18-kDa protein that binds labeled Ru360 under control conditions, but failed to bind the inhibitor after deglycosilation. A relationship between this protein and the action of ruthenium amine inhibitors of the mitochondrial uniporter is proposed.
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      description:The role of glycosidic residues in the inhibitory properties of ruthenium complexes on mitochondrial calcium uptake was determined in mitoplasts. Our results showed that the binding and inhibitory properties of ruthenium amine complexes were modified when mitoplasts were exposed to N-glycosidase F action, but calcium uptake was not altered. N-linked proteins of the mitochondrial inner membrane were identified. We detected an 18-kDa protein that binds labeled Ru360 under control conditions, but failed to bind the inhibitor after deglycosilation. A relationship between this protein and the action of ruthenium amine inhibitors of the mitochondrial uniporter is proposed.
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