Free-energy simulations reveal that both hydrophobic and polar interactions are important for influenza hemagglutinin antibody binding.
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An induced pocket for the binding of potent fusion inhibitor CL-385319 with H5N1 influenza virus hemagglutininAdvances in Antibody DesignBio-mimicking of proline-rich motif applied to carbon nanotube reveals unexpected subtleties underlying nanoparticle functionalization.Molecular dynamics analysis of antibody recognition and escape by human H1N1 influenza hemagglutinin.Free Energy Perturbation Calculation of Relative Binding Free Energy between Broadly Neutralizing Antibodies and the gp120 Glycoprotein of HIV-1.Comprehensive interrogation of natural TALE DNA-binding modules and transcriptional repressor domains.Large domain motions in Ago protein controlled by the guide DNA-strand seed region determine the Ago-DNA-mRNA complex recognition processSelecting vaccine strains for H3N2 human influenza A virus.EPI-peptide designer: a tool for designing peptide ligand libraries based on epitope-paratope interactions.Investigating Substitutions in Antibody-Antigen Complexes Using Molecular Dynamics: A Case Study with Broad-spectrum, Influenza A Antibodies.The complex and specific pMHC interactions with diverse HIV-1 TCR clonotypes reveal a structural basis for alterations in CTL function.Theoretical studies of the interaction between influenza virus hemagglutinin and its small molecule ligands.Longitudinal Surveillance of Porcine Rotavirus B Strains from the United States and Canada and In Silico Identification of Antigenically Important Sites.
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P2860
Free-energy simulations reveal that both hydrophobic and polar interactions are important for influenza hemagglutinin antibody binding.
description
2012 nî lūn-bûn
@nan
2012 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մարտին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Free-energy simulations reveal ...... emagglutinin antibody binding.
@ast
Free-energy simulations reveal ...... emagglutinin antibody binding.
@en
type
label
Free-energy simulations reveal ...... emagglutinin antibody binding.
@ast
Free-energy simulations reveal ...... emagglutinin antibody binding.
@en
prefLabel
Free-energy simulations reveal ...... emagglutinin antibody binding.
@ast
Free-energy simulations reveal ...... emagglutinin antibody binding.
@en
P2093
P2860
P1433
P1476
Free-energy simulations reveal ...... emagglutinin antibody binding.
@en
P2093
Ruhong Zhou
Seung-gu Kang
Tien Huynh
P2860
P304
P356
10.1016/J.BPJ.2012.01.043
P407
P577
2012-03-20T00:00:00Z