Mutations in the putative fusion peptide of Semliki Forest virus affect spike protein oligomerization and virus assembly.
about
Replication of alphaviruses: a review on the entry process of alphaviruses into cellsCoronavirus particle assembly: primary structure requirements of the membrane protein.An epitope of the Semliki Forest virus fusion protein exposed during virus-membrane fusion.Molecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein.Novel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion proteinFurin Processing and Proteolytic Activation of Semliki Forest VirusFunctions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and AssemblyEffects of anti-E2 monoclonal antibody on sindbis virus replication in AT3 cells expressing bcl-2Role of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion ProteinDifferential Incorporation of Cholesterol by Sindbis Virus Grown in Mammalian or Insect CellsA structural and functional perspective of alphavirus replication and assemblyE1 Mutants Identify a Critical Region in the Trimer Interface of the Semliki Forest Virus Fusion ProteinImaging the alphavirus exit pathway.The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependenceMutations in the E1 hydrophobic domain of rubella virus impair virus infectivity but not virus assembly.Alphavirus Entry and Membrane Fusion.The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusionIntercellular Extensions Are Induced by the Alphavirus Structural Proteins and Mediate Virus TransmissionMechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exitInteractions involved in pH protection of the alphavirus fusion proteinFluorescent Protein-Tagged Sindbis Virus E2 Glycoprotein Allows Single Particle Analysis of Virus Budding from Live Cells.A key interaction between the alphavirus envelope proteins responsible for initial dimer dissociation during fusionThe role of E3 in pH protection during alphavirus assembly and exitfus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunitEffects of mutations in the rubella virus E1 glycoprotein on E1-E2 interaction and membrane fusion activity.Semliki forest virus budding: assay, mechanisms, and cholesterol requirementIn vivo generation and characterization of a soluble form of the Semliki forest virus fusion proteinAcid-induced movements in the glycoprotein shell of an alphavirus turn the spikes into membrane fusion mode.Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion.The nucleocapsid-binding spike subunit E2 of Semliki Forest virus requires complex formation with the E1 subunit for activity.A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion.Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus.An Alphavirus E2 Membrane-Proximal Domain Promotes Envelope Protein Lateral Interactions and Virus Budding.The Alphavirus Exit Pathway: What We Know and What We Wish We Knew.Functional Study of the C-Terminal Part of the Hepatitis C Virus E1 Ectodomain
P2860
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P2860
Mutations in the putative fusion peptide of Semliki Forest virus affect spike protein oligomerization and virus assembly.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Mutations in the putative fusi ...... merization and virus assembly.
@en
Mutations in the putative fusi ...... merization and virus assembly.
@nl
type
label
Mutations in the putative fusi ...... merization and virus assembly.
@en
Mutations in the putative fusi ...... merization and virus assembly.
@nl
prefLabel
Mutations in the putative fusi ...... merization and virus assembly.
@en
Mutations in the putative fusi ...... merization and virus assembly.
@nl
P2093
P2860
P1433
P1476
Mutations in the putative fusi ...... omerization and virus assembly
@en
P2093
M R Klimjack
P Levy-Mintz
W A Duffus
P2860
P304
P407
P577
1995-04-01T00:00:00Z