Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.
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Fold stability during endolysosomal acidification is a key factor for allergenicity and immunogenicity of the major birch pollen allergenLeaf-specific pathogenesis-related 10 homolog, PgPR-10.3, shows in silico binding affinity with several biologically important moleculesInformation flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms.Allergen immunotherapy for birch pollen-allergic patients: recent advances.Influence of protein fold stability on immunogenicity and its implications for vaccine design.Measurement of Ligand-Target Residence Times by 1H Relaxation Dispersion NMR Spectroscopy.Localization of Millisecond Dynamics: Dihedral Entropy from Accelerated MD.Structure of the Major Apple Allergen Mal d 1Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1.
P2860
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P2860
Ligand binding modulates the structural dynamics and compactness of the major birch pollen allergen.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
2014年论文
@zh
2014年论文
@zh-cn
name
Ligand binding modulates the s ...... e major birch pollen allergen.
@en
type
label
Ligand binding modulates the s ...... e major birch pollen allergen.
@en
prefLabel
Ligand binding modulates the s ...... e major birch pollen allergen.
@en
P2093
P2860
P50
P1433
P1476
Ligand binding modulates the s ...... he major birch pollen allergen
@en
P2093
Julian E Fuchs
Marium Bibi
Martin Tollinger
Sarina Grutsch
Stefan Kofler
P2860
P304
P356
10.1016/J.BPJ.2014.10.062
P407
P577
2014-12-01T00:00:00Z