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Annals of the New York Academy of Sciences, 1970
SUMMARYBlood group specific plant agglutinins (named lectins by the present author) were discovered in 1945, first mentioned in 1947, and described in detail by Renkonen in 1948 and by Boyd in 1949. Similar agglutinins have since been found in some invertebrates. Thousands of species have now been screened for such activity.
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SUMMARYBlood group specific plant agglutinins (named lectins by the present author) were discovered in 1945, first mentioned in 1947, and described in detail by Renkonen in 1948 and by Boyd in 1949. Similar agglutinins have since been found in some invertebrates. Thousands of species have now been screened for such activity.
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Critical Reviews in Biotechnology, 1997
The harmful effects of chemical pesticides on the environment and human health have inspired a search for safer, environmentally-friendly control alternatives. The great advances in biotechnology, supported by basic studies utilizing molecular biology tools, have made biological control (i.e., the use of antagonistic microorganisms, fungi, or bacteria ...
Ilan Chet, Jacob Inbar
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The harmful effects of chemical pesticides on the environment and human health have inspired a search for safer, environmentally-friendly control alternatives. The great advances in biotechnology, supported by basic studies utilizing molecular biology tools, have made biological control (i.e., the use of antagonistic microorganisms, fungi, or bacteria ...
Ilan Chet, Jacob Inbar
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Structural basis of lectin-carbohydrate recognition.
Annual Review of Biochemistry, 1996Lectins are responsible for cell surface sugar recognition in bacteria, animals, and plants. Examples include bacterial toxins; animal receptors that mediate cell-cell interactions, uptake of glycoconjugates, and pathogen neutralization; and plant toxins
W. Weis, K. Drickamer
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Bifunctional properties of lectins: lectins redefined
Trends in Biochemical Sciences, 1988Abstract Both ‘classical' lectins, originally identified as cell agglutinins, and other carbohydrate-binding proteins that were identified by different means, may contain a second type of binding site that is specific for a non-carbohydrate ligand.
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Organic & Biomolecular Chemistry, 2009
Carbohydrate recognition presents a difficult challenge to supramolecular chemists, especially in the natural medium of water. After two decades of research, it has at last been possible to develop biomimetic receptors which perform well in aqueous solution.
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Carbohydrate recognition presents a difficult challenge to supramolecular chemists, especially in the natural medium of water. After two decades of research, it has at last been possible to develop biomimetic receptors which perform well in aqueous solution.
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Journal of Pediatric Gastroenterology and Nutrition, 1983
SummaryLectins are being used increasingly for the study of carbohydrate structures in the small and large intestine. These substances are particularly useful for characterization of normal and abnormal intestinal mucus, but they are also important probes for investigation of epithelial surface changes associated with differentiation and maturation ...
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SummaryLectins are being used increasingly for the study of carbohydrate structures in the small and large intestine. These substances are particularly useful for characterization of normal and abnormal intestinal mucus, but they are also important probes for investigation of epithelial surface changes associated with differentiation and maturation ...
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Lectin Affinity Chromatography
Molecular Biotechnology, 1994Lectins are glycoproteins or proteins that have a selective affinity for a carbohydrate, or a group of carbohydrates. Many purified lectins are readily available and these maybe immobilized to a variety of chromatography supports.
Owen Goldring, Iris West
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Molecular Pharmaceutics, 2014
Here, we report the covalent conjugation of lectin on Fe2O3@Au core@shell nanoparticle (lectin-Fe2O3@Au NP) for T2-weighted magnetic resonance (MR) and X-ray computed tomography (CT) dual-modality imaging. The lectin-Fe2O3@Au NPs are prepared by coupling
Xiuxia He +5 more
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Here, we report the covalent conjugation of lectin on Fe2O3@Au core@shell nanoparticle (lectin-Fe2O3@Au NP) for T2-weighted magnetic resonance (MR) and X-ray computed tomography (CT) dual-modality imaging. The lectin-Fe2O3@Au NPs are prepared by coupling
Xiuxia He +5 more
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Lectins in the unicellular Tetrahymena. I. Lectin detection with FITC-labeled anti-lectins
Acta Histochemica, 1983FITC-labeled antibodies prepared in rabbits to bean, pea, lens, datura, and snail lectin indicated by immunological reaction presence in the Tetrahymena of corresponding lectin-like components. The latter localized partly on the surface, partly inside the body of the unicellular.
György Csaba, Péter Kovács
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Annual Review of Biophysics and Biomolecular Structure, 1995
Lectins comprise a structurally very diverse class of proteins characterized by their ability to bind carbohydrates with considerable specificity. They are found in organisms ranging from viruses and plants to humans and serve to mediate biological recognition events.
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Lectins comprise a structurally very diverse class of proteins characterized by their ability to bind carbohydrates with considerable specificity. They are found in organisms ranging from viruses and plants to humans and serve to mediate biological recognition events.
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