Nejvíce citovaný článek - PubMed ID 22988810
Dimerization of an immunoactivating peptide derived from mycobacterial hsp65 using N-hydroxysuccinimide based bifunctional reagents is critical for its antitumor properties
The binding of monosaccharides and short peptides to lymphocyte receptors (human CD69 and rat NKR-P1A) was first reported in 1994 and then in a number of subsequent publications. Based on this observation, numerous potentially high-affinity saccharide ligands have been synthesized over the last two decades in order to utilize their potential in antitumor therapy. Due to significant inconsistencies in their reported binding properties, we decided to re-examine the interaction between multiple ligands and CD69 or NKR-P1A. Using NMR titration and isothermal titration calorimetry we were unable to detect the binding of the tested ligands such as N-acetyl-D-hexosamines and oligopeptides to both receptors, which contradicts the previous observations published in more than twenty papers over the last fifteen years.
- MeSH
- CD antigeny metabolismus MeSH
- diferenciační antigeny T-lymfocytů metabolismus MeSH
- krysa rodu Rattus MeSH
- lektiny typu C metabolismus MeSH
- lidé MeSH
- oligopeptidy chemická syntéza farmakologie MeSH
- polysacharidy chemická syntéza farmakologie MeSH
- receptory imunologické metabolismus MeSH
- rekombinantní proteiny metabolismus MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- krysa rodu Rattus MeSH
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- CD antigeny MeSH
- CD69 antigen MeSH Prohlížeč
- diferenciační antigeny T-lymfocytů MeSH
- Klrb1a protein, rat MeSH Prohlížeč
- lektiny typu C MeSH
- oligopeptidy MeSH
- polysacharidy MeSH
- receptory imunologické MeSH
- rekombinantní proteiny MeSH