Isoforms of Bet v 1, the major birch pollen allergen, analyzed by liquid chromatography, mass spectrometry, and cDNA cloning.
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Characterization of PR-10 genes from eight Betula species and detection of Bet v 1 isoforms in birch pollenCurrent overview of allergens of plant pathogenesis related protein familiesCrystallographically Mapped Ligand Binding Differs in High and Low IgE Binding Isoforms of Birch Pollen Allergen Bet v 1A pathogenesis related protein, VpPR-10.1, from Vitis pseudoreticulata: an insight of its mode of antifungal activityLigand Recognition of the Major Birch Pollen Allergen Bet v 1 is Isoform DependentTree pollen allergens-an update from a molecular perspectiveMolecular characteristics and biochemical functions of VpPR10s from Vitis pseudoreticulata associated with biotic and abiotic stresses.Protease recognition sites in Bet v 1a are cryptic, explaining its slow processing relevant to its allergenicity.Molecular characterization of recombinant T1, a non-allergenic periwinkle (Catharanthus roseus) protein, with sequence similarity to the Bet v 1 plant allergen familyQuality Control of Biomedicinal Allergen Products - Highly Complex Isoallergen Composition Challenges Standard MS Database Search and Requires Manual Data Analyses.Airborne house dust particles and diesel exhaust particles as allergen carriers.Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding.Birch pollen-related food allergy to legumes: identification and characterization of the Bet v 1 homologue in mungbean (Vigna radiata), Vig r 1.Seven different genes encode a diverse mixture of isoforms of Bet v 1, the major birch pollen allergen.Comparative genomics of fungal allergens and epitopes shows widespread distribution of closely related allergen and epitope orthologues.Purification and characterization of the major oak pollen allergen Que a 1 for component-resolved diagnostics using ImmunoCAP.The influence of recombinant production on the immunologic behavior of birch pollen isoallergens.Genetically engineered and synthetic allergen derivatives: candidates for vaccination against type I allergy.Comparing Proteolytic Fingerprints of Antigen-Presenting Cells during Allergen ProcessingAntigen aggregation decides the fate of the allergic immune response.Glycoproteomic analysis of seven major allergenic proteins reveals novel post-translational modifications.Isolation and characterization of a pathogenesis-related protein 10 gene (GmPR10) with induced expression in soybean (Glycine max) during infection with Phytophthora sojae.Computational tools for the study of allergens.Allergen databases.Allergy vaccines--new approaches to an old concept.Dissection of immunoglobulin E and T lymphocyte reactivity of isoforms of the major birch pollen allergen Bet v 1: potential use of hypoallergenic isoforms for immunotherapy.Expression in Escherichia coli, purification, and spectroscopic characterization of two mutant Bet v 1 proteins.Structural and functional aspects of PR-10 proteins.Innate affairs of allergens.AllergenOnline: A peer-reviewed, curated allergen database to assess novel food proteins for potential cross-reactivity.Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms.Proteomics for Allergy: from Proteins to the Patients.The role of Foxp3+ T cells in long-term efficacy of prophylactic and therapeutic mucosal tolerance induction in mice.Conversion of the major birch pollen allergen, Bet v 1, into two nonanaphylactic T cell epitope-containing fragments: candidates for a novel form of specific immunotherapyCharacterization of the T cell response to the major hazelnut allergen, Cor a 1.04: evidence for a relevant T cell epitope not cross-reactive with homologous pollen allergens.NMR solution structure of Ole e 6, a major allergen from olive tree pollen.Preserved epitope-specific T cell activation by recombinant Bet v 1-MBP fusion proteins.Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.Value of eight-amino-acid matches in predicting the allergenicity status of proteins: an empirical bioinformatic investigationLocalization of Millisecond Dynamics: Dihedral Entropy from Accelerated MD.
P2860
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P2860
Isoforms of Bet v 1, the major birch pollen allergen, analyzed by liquid chromatography, mass spectrometry, and cDNA cloning.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Isoforms of Bet v 1, the major ...... pectrometry, and cDNA cloning.
@ast
Isoforms of Bet v 1, the major ...... pectrometry, and cDNA cloning.
@en
type
label
Isoforms of Bet v 1, the major ...... pectrometry, and cDNA cloning.
@ast
Isoforms of Bet v 1, the major ...... pectrometry, and cDNA cloning.
@en
prefLabel
Isoforms of Bet v 1, the major ...... pectrometry, and cDNA cloning.
@ast
Isoforms of Bet v 1, the major ...... pectrometry, and cDNA cloning.
@en
P2093
P2860
P356
P1476
Isoforms of Bet v 1, the major ...... spectrometry, and cDNA cloning
@en
P2093
E Pittenauer
F Ferreira
H Breiteneder
O Scheiner
P2860
P304
P356
10.1074/JBC.270.6.2607
P407
P577
1995-02-01T00:00:00Z