pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.
about
The central proline of an internal viral fusion peptide serves two important rolesA specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotypeProtein stability induced by ligand binding correlates with changes in protein flexibility.Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion.How to lose a kink and gain a helix: pH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers.Delay of influenza hemagglutinin refolding into a fusion-competent conformation by receptor binding: a hypothesisReversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusionStructural and functional properties of an unusual internal fusion peptide in a nonenveloped virus membrane fusion protein.Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37 degrees C either by soluble murine CEACAM1 receptors or by pH 8.Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion.Membrane fusion mediated by coiled coils: a hypothesis.pH-dependence of intermediate steps of membrane fusion induced by the influenza fusion peptide.The influenza fusion peptide promotes lipid polar head intrusion through hydrogen bonding with phosphates and N-terminal membrane insertion depth.Membrane perturbation and fusion pore formation in influenza hemagglutinin-mediated membrane fusion. A new model for fusion.Environmental pH modulates inerolysin activity via post-binding blockade.
P2860
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P2860
pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
pH-induced conformational chan ...... fect on target lipid bilayers.
@ast
pH-induced conformational chan ...... fect on target lipid bilayers.
@en
type
label
pH-induced conformational chan ...... fect on target lipid bilayers.
@ast
pH-induced conformational chan ...... fect on target lipid bilayers.
@en
prefLabel
pH-induced conformational chan ...... fect on target lipid bilayers.
@ast
pH-induced conformational chan ...... fect on target lipid bilayers.
@en
P2860
P356
P1433
P1476
pH-induced conformational chan ...... fect on target lipid bilayers.
@en
P2860
P304
P356
10.1002/PRO.5560071113
P577
1998-11-01T00:00:00Z