| http://purl.uniprot.org/citations/31546678 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31546678 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31546678 | http://www.w3.org/2000/01/rdf-schema#comment | "Sea anemones' venom is rich in peptides acting on different biological targets, mainly on cytoplasmic membranes and ion channels. These animals are also a source of pancreatic α-amylase inhibitors, which have the ability to control the glucose level in the blood and can be used for the treatment of prediabetes and type 2 diabetes mellitus. Recently we have isolated and characterized magnificamide (44 aa, 4770 Da), the major α-amylase inhibitor of the sea anemone Heteractis magnifica mucus, which shares 84% sequence identity with helianthamide from Stichodactyla helianthus. Herein, we report some features in the action of a recombinant analog of magnificamide. The recombinant peptide inhibits porcine pancreatic and human saliva α-amylases with Ki's equal to 0.17 ± 0.06 nM and 7.7 ± 1.5 nM, respectively, and does not show antimicrobial or channel modulating activities. We have concluded that the main function of magnificamide is the inhibition of α-amylases; therefore, its functionally active recombinant analog is a promising agent for further studies as a potential drug candidate for the treatment of the type 2 diabetes mellitus."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.org/dc/terms/identifier | "doi:10.3390/md17100542"xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.org/dc/terms/identifier | "doi:10.3390/md17100542"xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Gladkikh I."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Gladkikh I."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Kim N."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Kim N."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Kozlovskaya E."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Kozlovskaya E."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Leychenko E."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Leychenko E."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Monastyrnaya M."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Monastyrnaya M."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Peigneur S."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Peigneur S."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Sintsova O."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Sintsova O."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Tytgat J."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Tytgat J."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Zelepuga E."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Zelepuga E."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Kalinovskii A."xsd:string |
| http://purl.uniprot.org/citations/31546678 | http://purl.uniprot.org/core/author | "Kalinovskii A."xsd:string |