Results 301 to 310 of about 126,085 (349)
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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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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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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.
I, West, O, Goldring
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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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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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Glycomimetics for the inhibition and modulation of lectins
Chemical Society Reviews, 2023, Petra Menova, Elena Shanina
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Multivalent glycosystems for human lectins
Chemical Society Reviews, 2023Macarena Martínez-Bailén +2 more
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