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  • This work reveals new structural relationships in the complex process of the interaction between activation receptors of natural killer cells (rat NKR-P1, human CD69) and novel bivalent carbohydrate glycomimetics. The length, glycosylation pattern and linker structure of receptor ligands were examined with respect to their ability to precipitate the receptor protein from solution, which simulates the in vivo process of receptor aggregation during NK cell activation. It was found that di-LacdiNAc triazole compounds show optimal performance, reaching up to 100 percent precipitation of the present protein receptors, and achieving high immunostimulatory activities without any tendency to trigger activation-induced apoptosis. In the synthesis of the compounds tested, two enzymatic approaches were applied
  • This work reveals new structural relationships in the complex process of the interaction between activation receptors of natural killer cells (rat NKR-P1, human CD69) and novel bivalent carbohydrate glycomimetics. The length, glycosylation pattern and linker structure of receptor ligands were examined with respect to their ability to precipitate the receptor protein from solution, which simulates the in vivo process of receptor aggregation during NK cell activation. It was found that di-LacdiNAc triazole compounds show optimal performance, reaching up to 100 percent precipitation of the present protein receptors, and achieving high immunostimulatory activities without any tendency to trigger activation-induced apoptosis. In the synthesis of the compounds tested, two enzymatic approaches were applied (en)
Title
  • Enzymatic synthesis of dimeric glycomimetic ligands of NK cell activation receptors
  • Enzymatic synthesis of dimeric glycomimetic ligands of NK cell activation receptors (en)
skos:prefLabel
  • Enzymatic synthesis of dimeric glycomimetic ligands of NK cell activation receptors
  • Enzymatic synthesis of dimeric glycomimetic ligands of NK cell activation receptors (en)
skos:notation
  • RIV/61388971:_____/11:00366522!RIV12-AV0-61388971
http://linked.open...avai/predkladatel
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA303/09/0477), P(GD305/09/H008), P(GP203/09/P024), S, Z(AV0Z50200510), Z(MSM0021620808)
http://linked.open...iv/cisloPeriodika
  • 12
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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  • 197799
http://linked.open...ai/riv/idVysledku
  • RIV/61388971:_____/11:00366522
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • beta-N-Acetylhexosaminidase; alactosyltransferase; Enzymatic glycosylation (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • NL - Nizozemsko
http://linked.open...ontrolniKodProRIV
  • [A8591FAF158C]
http://linked.open...i/riv/nazevZdroje
  • Carbohydrate Research
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
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http://linked.open...v/svazekPeriodika
  • 346
http://linked.open...iv/tvurceVysledku
  • Adámek, David
  • Bezouška, Karel
  • Bojarová, Pavla
  • Elling, L.
  • Křen, Vladimír
  • Křenek, Karel
  • Kuzma, Marek
  • Pelantová, Helena
  • Slámová, Kristýna
  • Christensen, H.
  • Drozdová, Anna
  • Hensen, B.
  • Jensen, H. H.
  • Krupová, Monika
  • Weignerová, Lenka
http://linked.open...ain/vavai/riv/wos
  • 000292852100029
http://linked.open...n/vavai/riv/zamer
issn
  • 0008-6215
number of pages
http://bibframe.org/vocab/doi
  • 10.1016/j.carres.2011.04.043
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