Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin.
about
Transmembrane peptides stabilize inverted cubic phases in a biphasic length-dependent manner: implications for protein-induced membrane fusion.The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transitionRecombinant influenza A H3N2 viruses with mutations of HA transmembrane cysteines exhibited altered virological characteristics.The transmembrane homotrimer of ADAM 1 in model lipid bilayers.Viral fusion protein transmembrane domain adopts β-strand structure to facilitate membrane topological changes for virus-cell fusion.Membrane interaction and structure of the transmembrane domain of influenza hemagglutinin and its fusion peptide complex.NMR structures of the second transmembrane domain of the human glycine receptor alpha(1) subunit: model of pore architecture and channel gating.A model membrane protein for binding volatile anesthetics.Class I and class II viral fusion protein structures reveal similar principles in membrane fusion.Two conserved residues are important for inducing highly ordered membrane domains by the transmembrane domain of influenza hemagglutinin.Efficient replication of a paramyxovirus independent of full zippering of the fusion protein six-helix bundle domain.A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion.Reovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion.Modifications of cysteine residues in the transmembrane and cytoplasmic domains of a recombinant hemagglutinin protein prevent cross-linked multimer formation and potency lossComplete dissociation of the HIV-1 gp41 ectodomain and membrane proximal regions upon phospholipid bindingHIV-1 gp41 transmembrane domain interacts with the fusion peptide: implication in lipid mixing and inhibition of virus-cell fusion.The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane StructureCharacterizing a histidine switch controlling pH-dependent conformational changes of the influenza virus hemagglutininMechanism of interaction between the general anesthetic halothane and a model ion channel protein, II: Fluorescence and vibrational spectroscopy using a cyanophenylalanine probeTrimeric transmembrane domain interactions in paramyxovirus fusion proteins: roles in protein folding, stability, and function.Interaction and conformational dynamics of membrane-spanning protein helices.De novo design of conformationally flexible transmembrane peptides driving membrane fusion.New user-friendly approach to obtain an Eisenberg plot and its use as a practical tool in protein sequence analysisHelix-destabilizing, beta-branched, and polar residues in the baboon reovirus p15 transmembrane domain influence the modularity of FAST proteins.Palmitoylation, membrane-proximal basic residues, and transmembrane glycine residues in the reovirus p10 protein are essential for syncytium formation.Structure of the Ebola virus envelope protein MPER/TM domain and its interaction with the fusion loop explains their fusion activity.Isotope-edited FTIR reveals distinct aggregation and structural behaviors of unmodified and pyroglutamylated amyloid β peptides.Lateral distribution of the transmembrane domain of influenza virus hemagglutinin revealed by time-resolved fluorescence imaging.Hemagglutinin of influenza virus partitions into the nonraft domain of model membranes.A cholesterol consensus motif is required for efficient intracellular transport and raft association of a group 2 HA from influenza virus.Co-evolution analysis to predict protein-protein interactions within influenza virus envelope.Trimeric membrane-anchored gp41 inhibits HIV membrane fusion.Reversible immobilization of peptides: surface modification and in situ detection by attenuated total reflection FTIR spectroscopy.The C- and the N-terminal regions of glycoprotein 41 ectodomain fuse membranes enriched and not enriched with cholesterol, respectively.Peptide mimics of the vesicular stomatitis virus G-protein transmembrane segment drive membrane fusion in vitro.Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.
P2860
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P2860
Secondary structure, orientation, oligomerization, and lipid interactions of the transmembrane domain of influenza hemagglutinin.
description
2000 nî lūn-bûn
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2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2000 թվականի հունվարին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Secondary structure, orientati ...... in of influenza hemagglutinin.
@ast
Secondary structure, orientati ...... in of influenza hemagglutinin.
@en
type
label
Secondary structure, orientati ...... in of influenza hemagglutinin.
@ast
Secondary structure, orientati ...... in of influenza hemagglutinin.
@en
prefLabel
Secondary structure, orientati ...... in of influenza hemagglutinin.
@ast
Secondary structure, orientati ...... in of influenza hemagglutinin.
@en
P356
P1433
P1476
Secondary structure, orientati ...... in of influenza hemagglutinin.
@en
P2093
S A Tatulian
P304
P356
10.1021/BI991594P
P407
P577
2000-01-01T00:00:00Z