Results 201 to 210 of about 45,451 (256)
AquIRE reveals the mechanisms of clinically induced RNA damage and the conservation and dynamics of glycoRNAs. [PDF]
Nucleic Acids ResZhang Z +20 more
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LeLISA: A New Lectin-Based Immunoassay for Evaluation of Mucinous and Serous Content in Pancreatic Cystic Neoplasms. [PDF]
Dig Dis SciHauge T +5 more
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Current Opinion in Structural Biology, 1999
Lectins - carbohydrate-binding proteins involved in a variety of recognition processes - exhibit considerable structural diversity. Three new lectin folds and further elaborations of known folds have been described recently. Large variability in quaternary association resulting from small alterations in essentially the same tertiary structure is a ...
Vijayan, M, Chandra, Nagasuma
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Lectins - carbohydrate-binding proteins involved in a variety of recognition processes - exhibit considerable structural diversity. Three new lectin folds and further elaborations of known folds have been described recently. Large variability in quaternary association resulting from small alterations in essentially the same tertiary structure is a ...
Vijayan, M, Chandra, Nagasuma
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Vox Sanguinis, 1963
SummaryPlant agglutinins are described which act more strongly as temperature is decreased. Crotalaria mucronata as well as variants of Phaseolus lunatus contain pronounced cold agglutinins against B cells while their action on A1‐cells is not enhanced with decreasing temperature.
F, OTTENSOOSER, M, SATO
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SummaryPlant agglutinins are described which act more strongly as temperature is decreased. Crotalaria mucronata as well as variants of Phaseolus lunatus contain pronounced cold agglutinins against B cells while their action on A1‐cells is not enhanced with decreasing temperature.
F, OTTENSOOSER, M, SATO
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Biochimica et Biophysica Acta (BBA) - General Subjects, 2004
This review summarizes studies on lectins that have been documented to be in the cytoplasm and nucleus of cells. Of these intracellular lectins, the most extensively studied are members of the galectin family. Galectin-1 and galectin-3 have been identified as pre-mRNA splicing factors in the nucleus, in conjunction with their interacting ligand, Gemin4.
John L, Wang +3 more
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This review summarizes studies on lectins that have been documented to be in the cytoplasm and nucleus of cells. Of these intracellular lectins, the most extensively studied are members of the galectin family. Galectin-1 and galectin-3 have been identified as pre-mRNA splicing factors in the nucleus, in conjunction with their interacting ligand, Gemin4.
John L, Wang +3 more
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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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