Форма представления | Статьи в зарубежных журналах и сборниках |
Год публикации | 2015 |
Язык | английский |
|
Курбангалиева Альмира Рафаэловна, автор
Танака Кацунори , автор
|
Библиографическое описание на языке оригинала |
Taichi M. Cell surface and in vivo interaction of dendrimeric N-glycoclusters / M. Taichi, S. Kitazume, K. K. H. Vong, R. Imamaki, A. Kurbangalieva, N. Taniguchi, K. Tanaka // Glycoconj. J. – 2015. – V. 32. – P. 497–503. |
Аннотация |
While many examples have been reported that glycoclusters interact with target lectins more strongly than single molecules of glycans, through multivalency effects, literature examples to support lectin interactions/modulations on cell surface and in live animals is quite rare. Our N-glycoclusters, which were efficiently prepared by immobilizing 16 molecules of the asparagine-linked glycans (N-glycans) onto a lysine-based dendron template through histidine-mediated Huisgen cycloaddition, were shown to efficiently detect platelet endothelial cell adhesion molecule (PECAM) on human umbilical vein endothelial cells (HUVEC) as a α(2-6)-sialylated oligosaccharides recognizing lectin. Furthermore, the identity of the N-glycans on our N-glycoclusters allowed kontrol over organ-selective accumulation and serum clearance properties when intravenously injected into mice. |
Ключевые слова |
asparagine-linked glycans, dendrimer, platelet endothelial cell adhesion molecule, glycocluster, in vivo imaging, lectin |
Название журнала |
Glycoconjugate Journal
|
URL |
http://link.springer.com/article/10.1007/s10719-015-9594-6 |
Пожалуйста, используйте этот идентификатор, чтобы цитировать или ссылаться на эту карточку |
https://repository.kpfu.ru/?p_id=135636 |
Полная запись метаданных |
Поле DC |
Значение |
Язык |
dc.contributor.author |
Курбангалиева Альмира Рафаэловна |
ru_RU |
dc.contributor.author |
Танака Кацунори |
ru_RU |
dc.date.accessioned |
2015-01-01T00:00:00Z |
ru_RU |
dc.date.available |
2015-01-01T00:00:00Z |
ru_RU |
dc.date.issued |
2015 |
ru_RU |
dc.identifier.citation |
Taichi M. Cell surface and in vivo interaction of dendrimeric N-glycoclusters / M. Taichi, S. Kitazume, K. K. H. Vong, R. Imamaki, A. Kurbangalieva, N. Taniguchi, K. Tanaka // Glycoconj. J. – 2015. – V. 32. – P. 497–503. |
ru_RU |
dc.identifier.uri |
https://repository.kpfu.ru/?p_id=135636 |
ru_RU |
dc.description.abstract |
Glycoconjugate Journal |
ru_RU |
dc.description.abstract |
While many examples have been reported that glycoclusters interact with target lectins more strongly than single molecules of glycans, through multivalency effects, literature examples to support lectin interactions/modulations on cell surface and in live animals is quite rare. Our N-glycoclusters, which were efficiently prepared by immobilizing 16 molecules of the asparagine-linked glycans (N-glycans) onto a lysine-based dendron template through histidine-mediated Huisgen cycloaddition, were shown to efficiently detect platelet endothelial cell adhesion molecule (PECAM) on human umbilical vein endothelial cells (HUVEC) as a α(2-6)-sialylated oligosaccharides recognizing lectin. Furthermore, the identity of the N-glycans on our N-glycoclusters allowed kontrol over organ-selective accumulation and serum clearance properties when intravenously injected into mice. |
ru_RU |
dc.language.iso |
ru |
ru_RU |
dc.subject |
asparagine-linked glycans |
ru_RU |
dc.subject |
dendrimer |
ru_RU |
dc.subject |
platelet endothelial cell adhesion molecule |
ru_RU |
dc.subject |
glycocluster |
ru_RU |
dc.subject |
in vivo imaging |
ru_RU |
dc.subject |
lectin |
ru_RU |
dc.title |
Cell surface and in vivo interaction of dendrimeric N-glycoclusters |
ru_RU |
dc.type |
Статьи в зарубежных журналах и сборниках |
ru_RU |
|