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sambucus cerulea/carie dentaire

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Differences in terminal carbohydrate structures of sialomucin in the murine nasal cavity.

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Terminal carbohydrate structures of sialomucin in the murine nasal cavity were characterized by means of lectin histochemistry. Two kinds of biotinylated lectins (Maackia amurensis agglutinin and Sambucus nigra agglutinin), which recognize sialic acid residues, showed marked differences in their

Anti-Toxoplasma activities of methanolic extract of Sambucus nigra (Caprifoliaceae) fruits and leaves.

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Toxoplasma gondii is an obligatory intracellular parasite that infects a wide range of warm-blooded animals and humans. Considering the severity of toxoplasmosis, side effects of current treatments, and the contribution of the ethnopharmacological knowledge for the treatment of parasitic infections,
Differences in cell surface carbohydrates and in laminin and fibronectin synthesis between 2 Ehrlich ascites tumor (EAT) cell lines, the adherent and non-adherent EAT cells, have been studied. The adherent EAT (a-EAT) cells grow in monolayer in vitro in the presence of fetal bovine serum. The

Binding of a natural anthocyanin inhibitor to influenza neuraminidase by mass spectrometry.

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The binding of a natural anthocyanin to influenza neuraminidase has been studied employing mass spectrometry and molecular docking. Derived from a black elderberry extract, cyanidin-3-sambubiocide has been found to be a potent inhibitor of sialidase activity. This study reveals the molecular basis

Wild-type and cultured Ehrlich ascites tumour cells differ in tumorigenicity, lectin binding patterns and binding to basement membranes.

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Three different variants of the Ehrlich ascites tumour (EAT) cell were derived and the lectin surface reactivities, as well as the malignant characteristics of each variant, were studied. Wild-type cells (EAT-wt) were selected for growth on basement membranes and tissue culture plastic to give EAT-c

Use of Spectroscopic Techniques to Reveal the Nature of the Interactions of Two Sialic Acid Specific Lectins with Gold Nanoparticles.

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From UV-vis absorption, steady state and time resolved fluorescence measurements coupled with circular dichroism (CD) spectral studies, it was revealed that among the two lectins: Sambucus nigra agglutinin (SNA) and Saraca indica (saracin II), SNA forms stronger binding complex in the ground state
Three variants of the classical Ehrlich ascites tumor (EAT) cell have been studied by quantitative, sialic acid-specific, lectin-gold ultrastructural cytochemistry. Electron microscopic examination revealed pronounced differences in the surface morphology of the three cell variants. The wild-type
Human influenza viruses are more efficiently isolated by inoculating patient samples into the amniotic rather than the allantoic cavity of embryonated chicken eggs. This type of cultivation selects virus variants with mutations around the hemagglutinin (HA) receptor binding site. To understand the

Reduced α-2,6 sialylation regulates cell migration in endometriosis.

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Is endometriosis associated with aberrant sialylation patterns and what is the potential impact of such anomalies on cell migratory properties?The reduced α-2,6 sialylation patterns in the peritoneal fluid of endometriosis-affected women and in stromal and

Toxoplasma gondii: uptake of fetuin and identification of a 15-kDa fetuin-binding protein.

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Lectin-binding studies demonstrated the presence of a 68-kDa glycoprotein in tachyzoites of Toxoplasma gondii harvested from P388D1 macrophage cell cultures but not in tachyzoites maintained in peritoneal cavities of NMRI mice. This protein was identified as the embryonic protein fetuin that

Sialoglycoproteins and penultimate sugar expression pattern in developing murine olfactory and respiratory mucosa.

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Sialic acid residues are constant constituents of the glycoproteins of the airways in all species. Sialoglycoproteins are the main acidic glycoprotein and their functions are to mediate cell adherence, to control the viscoelasticity of mucus and to serve as receptor sites for the binding of
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