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Please use this identifier to cite or link to this item: http://dspace.bsu.edu.ru/handle/123456789/46629
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dc.contributor.authorGolubev, I. V.-
dc.contributor.authorGureev, V. V.-
dc.contributor.authorKorokin, M. V.-
dc.contributor.authorSerdyuk, E. A.-
dc.contributor.authorSoldatova, V. A.-
dc.date.accessioned2022-05-05T13:00:35Z-
dc.date.available2022-05-05T13:00:35Z-
dc.date.issued2020-
dc.identifier.citationPreclinical study of innovative peptides mimicking the tertiary structure of the α-helix B of erythropoietin / I.V. Golubev [et al.] // Research Results in Pharmacology. - 2020. - Vol. 6, № 2.- P. 85-96. - Doi: 10.3897/rrpharmacology.6.55385ru
dc.identifier.urihttp://dspace.bsu.edu.ru/handle/123456789/46629-
dc.description.abstractThe aim of this study was to examine the effectiveness of innovative peptides obtained by addition of polypeptide motifs with antiaggregation activity (Arg-Gly-Asp, Lys-Gly-Asp and Pro-Gly-Pro) to a peptide mimicking the tertiary structure of the α-helix B of erythropoietin pHBSP (Pyr-Glu-Gln-Leu-Glu-Arg-Ala-Leu-Asn-Ser-Ser)ru
dc.language.isoenru
dc.subjectmedicineru
dc.subjectpharmacologyru
dc.subjectpeptidesru
dc.subjecterythropoietin derivativeru
dc.subjectpreeclampsiaru
dc.subjectendothelial dysfunctionru
dc.subjectmicrocirculationru
dc.subjectplacentaru
dc.titlePreclinical study of innovative peptides mimicking the tertiary structure of the α-helix B of erythropoietinru
dc.typeArticleru
Appears in Collections:Vol. 6, № 2

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