The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands.
about
Structural similarities of human and mammalian lipocalins, and their function in innate immunity and allergyCrystal Structure and Computational Analyses Provide Insights into the Catalytic Mechanism of 2,4-Diacetylphloroglucinol Hydrolase PhlG from Pseudomonas fluorescensThe structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteinsIdentification and mechanism of ABA receptor antagonismModulation of Abscisic Acid Signaling in Vivo by an Engineered Receptor-Insensitive Protein Phosphatase Type 2C AlleleStructure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data SetInsight into the Molecular Basis of Aromatic Polyketide Cyclization: Crystal Structure and in Vitro Characterization of WhiE-ORFVIStructural and bioinformatic analysis of the kiwifruit allergen Act d 11, a member of the family of ripening-related proteinsThe Strawberry Pathogenesis-related 10 (PR-10) Fra a Proteins Control Flavonoid Biosynthesis by Binding to Metabolic IntermediatesHuman IgE against the major allergen Bet v 1 - defining an epitope with limited cross-reactivity between different PR-10 family proteinsMechanism of high-affinity abscisic acid binding to PYL9/RCAR1Cross-reactivity of peanut allergens.Structure of ginseng major latex-like protein 151 and its proposed lysophosphatidic acid-binding mechanismPost-translational control of ABA signalling: the roles of protein phosphorylation and ubiquitinationIdentification of olivetolic acid cyclase from Cannabis sativa reveals a unique catalytic route to plant polyketidesLigand Recognition of the Major Birch Pollen Allergen Bet v 1 is Isoform DependentAbscisic acid inhibits type 2C protein phosphatases via the PYR/PYL family of START proteinsEAACI Molecular Allergology User's Guide.High-throughput computational structure-based characterization of protein families: START domains and implications for structural genomicsCrystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response.A new approach to assess and predict the functional roles of proteins across all known structuresAllergens and their role in the allergic immune response.Oak protein profile alterations upon root colonization by an ectomycorrhizal fungus.Enzyme discovery beyond homology: a unique hydroxynitrile lyase in the Bet v1 superfamily.Characterisation of the Vitis vinifera PR10 multigene familySolution structure and function of YndB, an AHSA1 protein from Bacillus subtilisBet v 1 from birch pollen is a lipocalin-like protein acting as allergen only when devoid of iron by promoting Th2 lymphocytes.Chimeras of Bet v 1 and Api g 1 reveal heterogeneous IgE responses in patients with birch pollen allergy.Structural enzymology of polyketide synthases.Vig r 6, the cytokinin-specific binding protein from mung bean (Vigna radiata) sprouts, cross-reacts with Bet v 1-related allergens and binds IgE from birch pollen allergic patients' sera.Identification and characterization of stress resistance related genes of Brassica rapa.Shared functions of plant and mammalian StAR-related lipid transfer (START) domains in modulating transcription factor activity.Glutathione-S-transferase: a minor allergen in birch pollen due to limited release from hydrated pollenAn elm EST database for identifying leaf beetle egg-induced defense genes.Thirsty plants and beyond: structural mechanisms of abscisic acid perception and signaling.Transcriptome Analysis of Early Responsive Genes in Rice during Magnaporthe oryzae Infection.IgE, IgG4 and IgA specific to Bet v 1-related food allergens do not predict oral allergy syndromeThe major birch pollen allergen Bet v 1 induces different responses in dendritic cells of birch pollen allergic and healthy individuals.Evolution of abscisic acid synthesis and signaling mechanismsIdentification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes.
P2860
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P2860
The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands.
description
2008 nî lūn-bûn
@nan
2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
The Bet v 1 fold: an ancient, ...... of large, hydrophobic ligands.
@ast
The Bet v 1 fold: an ancient, ...... of large, hydrophobic ligands.
@en
type
label
The Bet v 1 fold: an ancient, ...... of large, hydrophobic ligands.
@ast
The Bet v 1 fold: an ancient, ...... of large, hydrophobic ligands.
@en
prefLabel
The Bet v 1 fold: an ancient, ...... of large, hydrophobic ligands.
@ast
The Bet v 1 fold: an ancient, ...... of large, hydrophobic ligands.
@en
P2860
P50
P356
P1476
The Bet v 1 fold: an ancient, ...... of large, hydrophobic ligands.
@en
P2860
P2888
P356
10.1186/1471-2148-8-286
P577
2008-10-15T00:00:00Z
P5875
P6179
1051612410