Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state
about
Magic angle spinning NMR of virusesFolded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external regionMultiple locations of peptides in the hydrocarbon core of gel-phase membranes revealed by peptide (13)C to lipid (2)H rotational-echo double-resonance solid-state nuclear magnetic resonance.Conditional trimerization and lytic activity of HIV-1 gp41 variants containing the membrane-associated segments.Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.Complete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid bindingMolecular basis for epitope recognition by non-neutralizing anti-gp41 antibody F240Membrane insertion of fusion peptides from Ebola and Marburg viruses studied by replica-exchange molecular dynamics simulations.Structural Study of a New HIV-1 Entry Inhibitor and Interaction with the HIV-1 Fusion Peptide in Dodecylphosphocholine Micelles.Solid-state NMR Study of the YadA Membrane-Anchor Domain in the Bacterial Outer Membrane.Transmembrane Interactions of Full-length Mammalian Bitopic Cytochrome-P450-Cytochrome-b5 Complex in Lipid Bilayers Revealed by Sensitivity-Enhanced Dynamic Nuclear Polarization Solid-state NMR Spectroscopy.Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization.pH-dependent vesicle fusion induced by the ectodomain of the human immunodeficiency virus membrane fusion protein gp41: Two kinetically distinct processes and fully-membrane-associated gp41 with predominant β sheet fusion peptide conformation.Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain.Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity.Sample Preparation for Membrane Protein Structural Studies by Solid-State NMR.Festkörper-NMR-Studien an der Membrananker-Domäne von YadA in der bakteriellen Außenmembran
P2860
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P2860
Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Solid-state NMR spectroscopy o ...... e final six-helix bundle state
@en
Solid-state NMR spectroscopy o ...... e final six-helix bundle state
@nl
type
label
Solid-state NMR spectroscopy o ...... e final six-helix bundle state
@en
Solid-state NMR spectroscopy o ...... e final six-helix bundle state
@nl
prefLabel
Solid-state NMR spectroscopy o ...... e final six-helix bundle state
@en
Solid-state NMR spectroscopy o ...... e final six-helix bundle state
@nl
P2093
P2860
P1476
Solid-state NMR spectroscopy o ...... e final six-helix bundle state
@en
P2093
David P Weliky
Kelly Sackett
Matthew J Nethercott
Zhaoxiong Zheng
P2860
P304
P356
10.1016/J.JMB.2013.11.010
P407
P577
2013-11-16T00:00:00Z