Strength of envelope protein interaction modulates cytopathicity of measles virus.
about
Modes of paramyxovirus fusion: a Henipavirus perspectiveBimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggeringNonnucleoside inhibitor of measles virus RNA-dependent RNA polymerase complex activityUnity in diversity: shared mechanism of entry among paramyxovirusesHenipavirus mediated membrane fusion, virus entry and targeted therapeuticsStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemePotent host-directed small-molecule inhibitors of myxovirus RNA-dependent RNA-polymerasesSequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion processFunctional and structural characterization of neutralizing epitopes of measles virus hemagglutinin protein.Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.Measles virus entry inhibitors: a structural proposal for mechanism of action and the development of resistance.Design of a small-molecule entry inhibitor with activity against primary measles virus strains.Activation of paramyxovirus membrane fusion and virus entryStructural and mechanistic studies of measles virus illuminate paramyxovirus entry.Measles virus-induced suppression of immune responses.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry.Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.Identification of a second major site for CD46 binding in the hemagglutinin protein from a laboratory strain of measles virus (MV): potential consequences for wild-type MV infection.Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein-containing complexes.The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein.Canine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head.Electron cryotomography of measles virus reveals how matrix protein coats the ribonucleocapsid within intact virions.Timing is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Mechanism of fusion triggering by human parainfluenza virus type III: communication between viral glycoproteins during entryParamyxovirus fusion and entry: multiple paths to a common endTunable and reversible drug control of protein production via a self-excising degron.Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein.Incorporation of functional HN-F glycoprotein-containing complexes into newcastle disease virus is dependent on cholesterol and membrane lipid raft integrityFusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.The human metapneumovirus fusion protein mediates entry via an interaction with RGD-binding integrins.Interacting domains of the HN and F proteins of newcastle disease virus.Mechanism for active membrane fusion triggering by morbillivirus attachment protein.N-linked glycans with similar location in the fusion protein head modulate paramyxovirus fusion.Residues in the stalk domain of the hendra virus g glycoprotein modulate conformational changes associated with receptor bindingParamyxoviruses: different receptors - different mechanisms of fusion.A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F)Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion proteinIdentification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation.Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability.
P2860
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P2860
Strength of envelope protein interaction modulates cytopathicity of measles virus.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Strength of envelope protein interaction modulates cytopathicity of measles virus.
@en
Strength of envelope protein interaction modulates cytopathicity of measles virus.
@nl
type
label
Strength of envelope protein interaction modulates cytopathicity of measles virus.
@en
Strength of envelope protein interaction modulates cytopathicity of measles virus.
@nl
prefLabel
Strength of envelope protein interaction modulates cytopathicity of measles virus.
@en
Strength of envelope protein interaction modulates cytopathicity of measles virus.
@nl
P2093
P2860
P1433
P1476
Strength of envelope protein interaction modulates cytopathicity of measles virus.
@en
P2093
Adele K Fielding
Anthea L Hammond
Richard K Plemper
P2860
P304
P356
10.1128/JVI.76.10.5051-5061.2002
P407
P577
2002-05-01T00:00:00Z