Naturally processed T cell-activating peptides of the major birch pollen allergen.
about
T Cell Epitope Peptide Therapy for Allergic DiseasesImmunoregulatory T cell epitope peptides: the new frontier in allergy therapyNitration of the pollen allergen bet v 1.0101 enhances the presentation of bet v 1-derived peptides by HLA-DR on human dendritic cellsSensitization prevalence, antibody cross-reactivity and immunogenic peptide profile of Api g 2, the non-specific lipid transfer protein 1 of celeryAssessing protein immunogenicity with a dendritic cell line-derived endolysosomal degradomeFold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergenCD4+ T-cell epitope prediction using antigen processing constraintsBet v 1 from birch pollen is a lipocalin-like protein acting as allergen only when devoid of iron by promoting Th2 lymphocytes.Comparing Proteolytic Fingerprints of Antigen-Presenting Cells during Allergen ProcessingComprehensive analysis of contributions from protein conformational stability and major histocompatibility complex class II-peptide binding affinity to CD4+ epitope immunogenicity in HIV-1 envelope glycoprotein.Association of HLA-DR1 with the allergic response to the major mugwort pollen allergen: molecular background.Interaction of allergens, major histocompatibility complex molecules, and T cell receptors: a 'ménage à trois' that opens new avenues for therapeutic intervention in type I allergy.Structural and functional aspects of PR-10 proteins.Immunoproteomic analysis of house dust mite antigens reveals distinct classes of dominant T cell antigens according to function and serological reactivity.Deciphering the MHC-associated peptidome: a review of naturally processed ligand data.Correlation of sensitizing capacity and T-cell recognition within the Bet v 1 family.Kinetics, cross-reactivity, and specificity of Bet v 1-specific IgG4 antibodies induced by immunotherapy with birch pollen.Conformational instability governed by disulfide bonds partitions the dominant from subdominant helper T-cell responses specific for HIV-1 envelope glycoprotein gp120.Endolysosomal Degradation of Allergenic Ole e 1-Like Proteins: Analysis of Proteolytic Cleavage Sites Revealing T Cell Epitope-Containing Peptides.HLA-DR-presented peptide repertoires derived from human monocyte-derived dendritic cells pulsed with blood coagulation factor VIII.Characterization of the T-cell response to Dau c 1, the Bet v 1-homolog in carrot.Differential activation of dendritic cells by toll-like receptors causes diverse differentiation of naïve CD4+ T cells from allergic patients.Reshaping the Bet v 1 fold modulates T(H) polarization.Determination of a Predictive Cleavage Motif for Eluted Major Histocompatibility Complex Class II Ligands
P2860
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P2860
Naturally processed T cell-activating peptides of the major birch pollen allergen.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
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name
Naturally processed T cell-activating peptides of the major birch pollen allergen.
@en
Naturally processed T cell-activating peptides of the major birch pollen allergen.
@nl
type
label
Naturally processed T cell-activating peptides of the major birch pollen allergen.
@en
Naturally processed T cell-activating peptides of the major birch pollen allergen.
@nl
prefLabel
Naturally processed T cell-activating peptides of the major birch pollen allergen.
@en
Naturally processed T cell-activating peptides of the major birch pollen allergen.
@nl
P2093
P50
P1476
Naturally processed T cell-activating peptides of the major birch pollen allergen
@en
P2093
Anette Karle
Anne B Vogt
Gottfried F Fischer
Sonja Mutschlechner
P304
711-8, 718.e1-718.e2
P356
10.1016/J.JACI.2009.10.052
P407
P577
2010-02-04T00:00:00Z