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galanthus transcaucasicus/upala
Veza se sprema u međuspremnik
5 rezultatima
The role of natural products in the discovery of new drug candidates for the treatment of neurodegenerative disorders II: Alzheimer's disease.
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Prijava Registriraj se
The present review is part II in a series (part I focuses on Parkinson's Disease) that addresses the value of natural product chemistry in the discovery of medicines for the treatment of neurodegenerative disorders. Data reviewed document that a host of products from plant species and derivatives
Donor treatment with mycophenolate mofetil: protection against ischemia-reperfusion injury in the rat.
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BACKGROUND
Mycophenolic acid, the active metabolite of mycophenolate mofetil, inhibits the glycosylation of cell membrane glycoproteins. We hypothesized that impaired glycosylation of cell adhesion molecules on endothelial cells in vivo results in decreased susceptibility to inflammation or
Safety concerns for the potential use of cyanovirin-N as a microbicidal anti-HIV agent.
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Prijava Registriraj se
Based on its antiviral activity profile, cyanovirin-N (CV-N) holds great potential for anti-HIV microbicidal application. However, limited data are available on the possible side-effects of this lectin. A detailed investigation was carried out to obtain better insights in the cytotoxic, inflammatory
Regulation of neutrophil function by selective targeting of glycan epitopes expressed on the integrin CD11b/CD18.
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Prijava Registriraj se
Polymorphonuclear neutrophils (PMNs) play a critical role in the innate immune response to invading pathogens. However, dysregulated mucosal trafficking of PMNs and associated epithelial tissue damage is a pathological hallmark of numerous inflammatory conditions including inflammatory bowel
Phagocytosis stimulates alternative glycosylation of macrosialin (mouse CD68), a macrophage-specific endosomal protein.
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Macrosialin (mouse CD68), a macrophage-specific member of the lysosomal-associated membrane protein family, displays N-linked glycosylation and a heavily sialylated, mucin-like domain. We show that phagocytosis of zymosan by inflammatory peritoneal macrophages potently alters glycan processing of
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