ArticleBiophysical journal2014
Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Structural Characterization of Food Allergens by Nuclear Magnetic Resonance Spectroscopy.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Structural Basis of the Immunological Cross-Reactivity between Kiwi and Birch Pollen.Foods (Basel, Switzerland) · 2023Article
- The History and Science of the Major Birch Pollen Allergen Bet v 1.Biomolecules · 2023Review
- Review
- Ascorbylation of a Reactive Cysteine in the Major Apple Allergen Mal d 1.Foods (Basel, Switzerland) · 2022Article
- The Structural Flexibility of PR-10 Food Allergens.International journal of molecular sciences · 2022Article
- Combined 3D-QSAR, molecular docking and dynamics simulations studies to model and design TTK inhibitors.Frontiers in chemistry · 2022Article
- Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1.Foods (Basel, Switzerland) · 2021Article
- Structure and Zeatin Binding of the Peach AllergenJournal of agricultural and food chemistry · 2021Article
- Inverse relation between structural flexibility and IgE reactivity of Cor a 1 hazelnut allergens.Scientific reports · 2021Article
- Structural Bases for the Allergenicity of Fra a 1.02 in Strawberry Fruits.Journal of agricultural and food chemistry · 2020Article
- Ligand Binding of PR-10 Proteins with a Particular Focus on the Bet v 1 Allergen Family.Current allergy and asthma reports · 2020Review
- Modeling to Understand Plant Protein Structure-Function Relationships-Implications for Seed Storage Proteins.Molecules (Basel, Switzerland) · 2020Review
- Dynamics Rationalize Proteolytic Susceptibility of the Major Birch Pollen Allergen Bet v 1.Frontiers in molecular biosciences · 2020Article
- Multiple roles of Bet v 1 ligands in allergen stabilization and modulation of endosomal protease activity.Allergy · 2019Article
- Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1.Scientific reports · 2018Article
- Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms.International journal of molecular sciences · 2017Article
- Influence of protein fold stability on immunogenicity and its implications for vaccine design.Expert review of vaccines · 2017Review
- Structure of the Major Apple Allergen Mal d 1.Journal of agricultural and food chemistry · 2017Article
- Measurement of Ligand-Target Residence Times byJournal of medicinal chemistry · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
Pathogenesis-related plant proteins of class-10 (PR-10) are essential for storage and transport of small molecules. A prominent member of the PR-10 family, the major birch pollen allergen Bet v 1, is the main cause of spring pollinosis in the temperate climate zone of the northern hemisphere. Bet v 1 binds various ligand molecules to its internal cavity, and immunologic effects of the presence of ligand have been discussed. However, the mechanism of binding has remained elusive. In this study, we show that in solution Bet v 1.0101 is conformationally heterogeneous and cannot be represented by a single structure. NMR relaxation data suggest that structural dynamics are fundamental for ligand access to the protein interior. Complex formation then leads to significant rigidification of the protein along with a compaction of its 3D structure. The data presented herein provide a structural basis for understanding the immunogenic and allergenic potential of ligand binding to Bet v 1 allergens.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.