{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["2(12)"],"submitter":["Watanabe K"],"pubmed_abstract":["All fundamental data about binding of the cyanide to a supramolecular complex composed of a per-O-methylated β-cyclodextrin dimer having an imidazole linker (Im3CD) and an anionic ferric porphyrin (Fe((III))TPPS) indicate that the Fe((III))TPPS/Im3CD complex is much better as an cyanide receptor in vivo than hydroxocobalamin, whose cyanide binding ability is lowered by its strong binding to serum proteins in the blood."],"journal":["ACS medicinal chemistry letters"],"pagination":["943-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4018087"],"repository":["biostudies-literature"],"pubmed_title":["Supramolecular ferric porphyrins as cyanide receptors in aqueous solution."],"pmcid":["PMC4018087"],"pubmed_authors":["Kano K","Kitagishi H","Watanabe K"],"additional_accession":[]},"is_claimable":false,"name":"Supramolecular ferric porphyrins as cyanide receptors in aqueous solution.","description":"All fundamental data about binding of the cyanide to a supramolecular complex composed of a per-O-methylated β-cyclodextrin dimer having an imidazole linker (Im3CD) and an anionic ferric porphyrin (Fe((III))TPPS) indicate that the Fe((III))TPPS/Im3CD complex is much better as an cyanide receptor in vivo than hydroxocobalamin, whose cyanide binding ability is lowered by its strong binding to serum proteins in the blood.","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Dec","modification":"2025-04-05T10:20:32.853Z","creation":"2019-03-27T01:28:02Z"},"accession":"S-EPMC4018087","cross_references":{"pubmed":["24900285"],"doi":["10.1021/ml200231x"]}}