Results 291 to 300 of about 30,089 (322)
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Nucleocytoplasmic plant lectins
Biochimica et Biophysica Acta (BBA) - General Subjects, 2010During the last decade it was unambiguously shown that plants synthesize minute amounts of carbohydrate-binding proteins upon exposure to stress situations like drought, high salt, hormone treatment, pathogen attack or insect herbivory. In contrast to the 'classical' plant lectins, which are typically found in storage vacuoles or in the extracellular ...
Els J.M. Van Damme, Nausicaä Lannoo
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Antitumor effect of plant lectins
Natural Toxins, 1997AbstractThis review examines the literature data concerning the biological activity of plant lectins. Numerous studies have reported that these substances possess toxic, cytotoxic, antitumor, and anticarcinogenic properties. A brief description of the biological properties of plant lectins, as well as the effect of plant lectins on normal and malignant
Elvira González de Mejı́a+1 more
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Subunit assembly of plant lectins
Current Opinion in Structural Biology, 2007Lectins are a structurally diverse group of carbohydrate recognizing proteins that are involved in various biological processes and exhibit substantial structural diversity. Interestingly, in spite of having varied carbohydrate-binding specificities, they show modest variation in their secondary and tertiary structure.
Sinha, Sharmistha+3 more
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The role of lectins in plant defence
The Histochemical Journal, 1995Recent progress in the search for the physiological role of plant lectins supports the idea that some of these proteins are involved in the defence mechanisms of the plant. To place the evidence in favour of such a defensive role in a broad perspective, a short overview is given of the most important plant pathogens and predators.
J. Van Damme, Willy J. Peumans
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Antinutritional properties of plant lectins
Toxicon, 2004Lectins are carbohydrate binding (glyco)proteins which are ubiquitous in nature. In plants, they are distributed in various families and hence ingested daily in appreciable amounts by both humans and animals. One of the most nutritionally important features of plant lectins is their ability to survive digestion by the gastrointestinal tract of ...
Jose T.A. Oliveira, Ilka M. Vasconcelos
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Ribosome-inactivating lectins of plants [PDF]
A heterogeneous group of plant proteins are capable of enzymatically inactivating ribosomes by depurination of the invariant adenine in the 28S rRNA. Some of these proteins are heterodimers, containing a lectin subunit joined to an enzymatic subunit via a disulfide bond.
O. J. Sudarkina+2 more
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Review: The multiple roles of plant lectins
Plant Science, 2021For decades, the biological roles of plant lectins remained obscure and subject to speculation. With the advent of technological and scientific progress, researchers have compiled a vast amount of information regarding the structure, biological activities and functionality of hundreds of plant lectins.
Tibo De Coninck, Els J.M. Van Damme
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Current Opinion in Structural Biology, 1997
Among the crystal structures of lectins determined recently, three--snowdrop lectin, jacalin and amaranthin--represent new lectin families. Their polypeptide folds share remarkably similar features and consist exclusively of beta structure. Autonomously folded beta-sheet subdomains, inter-related by a pseudothreefold symmetry, assemble to form beta ...
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Among the crystal structures of lectins determined recently, three--snowdrop lectin, jacalin and amaranthin--represent new lectin families. Their polypeptide folds share remarkably similar features and consist exclusively of beta structure. Autonomously folded beta-sheet subdomains, inter-related by a pseudothreefold symmetry, assemble to form beta ...
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Recombinant Plant Lectins and Their Mutants
2003Publisher Summary This chapter focuses on recombinant plant lectins, especially those that have been investigated by mutagenesis. Cloning and expression of plant lectins have developed into powerful tools in aiding investigations of the structure–function relationships in their lectins.
Nathan Sharon, Hansjörg Streicher
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