The oligomerization reaction of the Semliki Forest virus membrane protein subunits
about
Replication of alphaviruses: a review on the entry process of alphaviruses into cellsA CRISPR screen defines a signal peptide processing pathway required by flavivirusesFunctional characterization of intracellular and secreted forms of a truncated hepatitis C virus E2 glycoproteinAdaptive mutations in Sindbis virus E2 and Ross River virus E1 that allow efficient budding of chimeric virusesFormation and characterization of the trimeric form of the fusion protein of Semliki Forest VirusMolecular genetic study of the interaction of Sindbis virus E2 with Ross River virus E1 for virus budding.Folding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulumOligomerization-dependent folding of the membrane fusion protein of Semliki Forest virusVisualization of membrane protein domains by cryo-electron microscopy of dengue virus4.4 Å cryo-EM structure of an enveloped alphavirus Venezuelan equine encephalitis virusThe role of the hepatitis C virus glycoproteins in infection.In vitro evolution of high-titer, virus-like vesicles containing a single structural protein.Assembly of alphavirus replication complexes from RNA and protein components in a novel trans-replication system in mammalian cells.Interactions between PE2, E1, and 6K required for assembly of alphaviruses studied with chimeric viruses.Role of conserved cysteines in the alphavirus E3 proteinDual split protein-based fusion assay reveals that mutations to herpes simplex virus (HSV) glycoprotein gB alter the kinetics of cell-cell fusion induced by HSV entry glycoproteinsMutational analysis, using a full-length rubella virus cDNA clone, of rubella virus E1 transmembrane and cytoplasmic domains required for virus release.Lectin-mediated retention of p62 facilitates p62-E1 heterodimerization in endoplasmic reticulum of Semliki Forest virus-infected cells.The nucleocapsid-binding spike subunit E2 of Semliki Forest virus requires complex formation with the E1 subunit for activity.The dynamic envelope of a fusion class II virus. E3 domain of glycoprotein E2 precursor in Semliki Forest virus provides a unique contact with the fusion protein E1.Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin.Prefusion rearrangements resulting in fusion Peptide exposure in Semliki forest virus.The Alphavirus Exit Pathway: What We Know and What We Wish We Knew.
P2860
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P2860
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
description
1995 nî lūn-bûn
@nan
1995 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
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
name
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@ast
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@en
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@nl
type
label
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@ast
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@en
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@nl
prefLabel
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@ast
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@en
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@nl
P2093
P2860
P3181
P356
P1476
The oligomerization reaction of the Semliki Forest virus membrane protein subunits
@en
P2093
P2860
P304
P3181
P356
10.1083/JCB.128.3.283
P407
P577
1995-02-01T00:00:00Z