X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy - Wikidata - awgldk - TriplyDB

X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

http://www.wikidata.org/entity/Q27734077

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Do lipids influence the allergic sensitization process?Current overview of allergens of plant pathogenesis related protein families Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1 Major venom allergen of yellow jackets, Ves v 5: structural characterization of a pathogenesis-related protein superfamily Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure Crystal structure and functional analysis of tetracenomycin ARO/CYC: Implications for cyclization specificity of aromatic polyketides Cytokinin-induced structural adaptability of a Lupinus luteus PR-10 protein Structures of twoArabidopsis thalianamajor latex proteins represent novel helix-grip folds Structural mechanism of abscisic acid binding and signaling by dimeric PYR1.Der p 5 Crystal Structure Provides Insight into the Group 5 Dust Mite Allergens Solution structure of the strawberry allergen Fra a 1 Crystallographically Mapped Ligand Binding Differs in High and Low IgE Binding Isoforms of Birch Pollen Allergen Bet v 1 The Strawberry Pathogenesis-related 10 (PR-10) Fra a Proteins Control Flavonoid Biosynthesis by Binding to Metabolic Intermediates Stabilization of the Dimeric Birch Pollen Allergen Bet v 1 Impacts Its Immunological Properties Structure and function of the peanut panallergen Ara h 8.Human IgE against the major allergen Bet v 1 - defining an epitope with limited cross-reactivity between different PR-10 family proteins Likelihood-based molecular-replacement solution for a highly pathological crystal with tetartohedral twinning and sevenfold translational noncrystallographic symmetry Development and evaluation of a sublingual tablet based on recombinant Bet v 1 in birch pollen-allergic patients Structure of ginseng major latex-like protein 151 and its proposed lysophosphatidic acid-binding mechanism Solution structure of Der f 2, the major mite allergen for atopic diseases Probing the molecular basis of allergy. three-dimensional structure of the bovine lipocalin allergen Bos d 2 Immunological mechanisms of allergen-specific immunotherapy A pathogenesis related protein, VpPR-10.1, from Vitis pseudoreticulata: an insight of its mode of antifungal activity Ligand Recognition of the Major Birch Pollen Allergen Bet v 1 is Isoform Dependent Multiple Patterns of Regulation and Overexpression of a Ribonuclease-Like Pathogenesis-Related Protein Gene, OsPR10a, Conferring Disease Resistance in Rice and Arabidopsis NMR resonance assignments of the major apple allergen Mal d 1 Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergen EAACI Molecular Allergology User's Guide.100 Years later: Celebrating the contributions of x-ray crystallography to allergy and clinical immunology.Six years of INSTAND e. V. sIgE proficiency testing: An evaluation of in vitro allergy diagnostics High-throughput computational structure-based characterization of protein families: START domains and implications for structural genomics Expression and secondary structure determination by NMR methods of the major house dust mite allergen Der p 2.Molecular characterization of recombinant T1, a non-allergenic periwinkle (Catharanthus roseus) protein, with sequence similarity to the Bet v 1 plant allergen family Biologically active recombinant forms of a major house dust mite group 1 allergen Der f 1 with full activities of both cysteine protease and IgE binding.Identification of a villin-related tobacco protein as a novel cross-reactive plant allergen.The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands.Soluble CD36 ectodomain binds negatively charged diacylglycerol ligands and acts as a co-receptor for TLR2.The influence of recombinant production on the immunologic behavior of birch pollen isoallergens.Transient dimers of allergens.A gate-latch-lock mechanism for hormone signalling by abscisic acid receptors.

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P2860

X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

http://www.wikidata.org/entity/Q27734077

description

1996 nî lūn-bûn

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1996 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

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1996 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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1996年の論文

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年学术文章

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1996年學術文章

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name

X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy

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C Schou

http://www.w3.org/2001/XMLSchema#string

F M Poulsen

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H Ipsen

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H Løwenstein

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M D Spangfort

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P Osmark

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R J Joost van Neerven

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Protein structure comparison by alignment of distance matrices

The P-loop--a common motif in ATP- and GTP-binding proteins

SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions

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1040-5

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scholarly article

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1051935

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10.1038/NSB1296-1040

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12

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3

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Michael Gajhede

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8946858

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