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lectin/lituruohot
Linkki tallennetaan leikepöydälle
Sivu 1 alkaen 123 tuloksia
An Arabidopsis TIR-Lectin Two-Domain Protein Confers Defense Properties against Tetranychus urticae.
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Plant immunity depends on fast and specific transcriptional reprogramming triggered by the perception of biotic stresses. Numerous studies have been conducted to better understand the response of plants to the generalist herbivore two-spotted spider mite (Tetranychus urticae). However, how
Transcriptional profiling of the lectin ArathEULS3 from Arabidopsis thaliana toward abiotic stresses.
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The family of EUL-related lectins groups all proteins with an Euonymus lectin (EUL) domain, a protein motif which is highly conserved throughout the plant kingdom and occurs as part of many chimeric proteins with different domain architectures. The S3 type EUL lectin from Arabidopsis thaliana
Binding properties of the N-acetylglucosamine and high-mannose N-glycan PP2-A1 phloem lectin in Arabidopsis.
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Phloem Protein2 (PP2) is a component of the phloem protein bodies found in sieve elements. We describe here the lectin properties of the Arabidopsis (Arabidopsis thaliana) PP2-A1. Using a recombinant protein produced in Escherichia coli, we demonstrated binding to N-acetylglucosamine oligomers.
Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis thaliana.
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The Euonymus lectin (EUL) domain was recognized as the structural motif for a novel class of putative carbohydrate binding proteins. Confocal microscopy demonstrated that the lectin from Euonymus europaeus (EEA) as well as the EUL protein from Arabidopsis thaliana (ArathEULS3) are located in the
The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion.
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Stress granules are cytoplasmic compartments, which serve as mRNA storage units during stress, therefore regulating translation. The Arabidopsis thaliana lectin ArathEULS3 has been widely described as a stress inducible gene. This study aimed to examine in detail the localization of
The Arabidopsis A4 subfamily of lectin receptor kinases negatively regulates abscisic acid response in seed germination.
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Abscisic acid (ABA) is an important plant hormone for a wide array of growth and developmental processes and stress responses, but the mechanism of ABA signal perception on the plasma membrane remains to be dissected. A previous GeneChip analysis revealed that a member of the A4 subfamily of lectin
The Arabidopsis LECTIN RECEPTOR KINASE-VI.2 is a functional protein kinase and is dispensable for basal resistance to Botrytis cinerea.
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Sensing of microbial pathogens by pathogen-associated molecular patterns (PAMPs) through pattern recognition receptors (PRRs) elicits a defense program known as PAMP-triggered immunity (PTI). Recently, we have shown that the Arabidopsis thaliana L-TYPE LECTIN RECEPTOR KINASE-VI.2 (LecRK-VI.2)
Characterization of the yam tuber storage proteins from Dioscorea batatas exhibiting unique lectin activities.
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Four major proteins designated DB1, DB2, DB3, and DB4 were isolated and characterized from the yam tuber Dioscorea batatas. The ratios of their yields were 20:50:20:10. DB1 was a mannose-binding lectin (20 kDa) consisting of 10-kDa subunits and was classified as the monocot mannose-binding lectin
Expression and purification of a biologically active Phytophthora parasitica cellulose binding elicitor lectin in Pichia pastoris.
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The Phytophthora parasitica cellulose-binding elicitor lectin, (CBEL), is a cell wall-localized protein playing a key role in cell wall organization and adhesion of the mycelium to cellulosic substrates. CBEL is a potent elicitor of plant immune responses and this activity is linked to its ability
Expression of garlic leaf lectin under the control of the phloem-specific promoter Asus1 from Arabidopsis thaliana protects tobacco plants against the tobacco aphid (Myzus nicotianae).
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BACKGROUND
To check for correlation between the insecticidal properties and the specificity of lectins, a comparative study was made of the insecticidal activities of two garlic lectins with different biological activities.
RESULTS
The insecticidal activity of the garlic (Allium sativum L.) leaf
Coccinia indica agglutinin, a 17kDa PP2 like phloem lectin: Affinity purification, primary structure and formation of self-assembled filaments.
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Phloem protein-2 (PP2) is an abundant soluble protein in the sieve elements in plants. Its lectin property was reported in various species. The primary structure of a 17kDa PP2 from Coccinia indica (Coccinia indica agglutinin, CIA17), determined by mass spectrometry, shows extensive homology with
A Nod factor-binding lectin is a member of a distinct class of apyrases that may be unique to the legumes.
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Recent studies from our laboratory have found that a root lectin from the legume Dolichos hifloris is present on the root surface, binds rhizobial Nod factor and has apyrase activity. To assess the broader significance of this lectin/nucleotide phosphohydrolase (Db-LNP), we have cloned a second
A lectin from Sesbania aculeata (Dhaincha) roots and its possible function.
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A lectin was isolated from the roots of Sesbania aculeata. This is a glucose specific lectin having 39 kDa subunit molecular weight. The expression of this lectin was found to be developmentally regulated and observed to be the highest in the second week. The lectin was purified by affinity
A probarley lectin processing enzyme purified from Arabidopsis thaliana seeds.
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An aspartic proteinase was purified from the seeds of Arabidopsis thaliana (ecotype RLD) using affinity chromatography on pepstatin-agarose and ion exchange chromatography. The purified enzyme is optimally active at pH 3.5 and completely inhibited by pepstatin A. The purified Arabidopsis aspartic
miR393 regulation of lectin receptor-like kinases associated with LPS perception in Arabidopsis thaliana.
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microRNAs regulate dynamic aspects of innate immunity in Arabidopsis thaliana in response to lipopolysaccharides. Lectin-domain receptor-like kinases function as surveillance proteins and miR393 targets transcripts of an L-type LecRK (LECRK-V.7, At3g59740). This study investigated miR393 regulation
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