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Maackia amurensis seed lectin structure and sequence comparison with other M. amurensis lectins. [PDF]
J Biol ChemNayak AR +7 more
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Engineering glycosyltransferases into glycan binding proteins using a mammalian surface display platform. [PDF]
Nat CommunHombu R +4 more
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Glycosylation in neuroinflammation: mechanisms, implications, and therapeutic strategies for neurodegenerative diseases. [PDF]
Transl NeurodegenerCheng S, Xiao B, Luo Z.
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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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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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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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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.
openaire +2 more sources