The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
about
Role of rubella virus glycoprotein domains in assembly of virus-like particles.Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria.Interactions between rubella virus capsid and host protein p32 are important for virus replication.Rubella virus replication and links to teratogenicityIntracellular localization of Crimean-Congo Hemorrhagic Fever (CCHF) virus glycoproteins.Envelopment of varicella-zoster virus: targeting of viral glycoproteins to the trans-Golgi networkInvolvement of the endoplasmic reticulum in the assembly and envelopment of African swine fever virusRole of glycoprotein PE2 in formation and maturation of the Sindbis virus spikeFormation and rearrangement of disulfide bonds during maturation of the Sindbis virus E1 glycoproteinAssembly, maturation and three-dimensional helical structure of the teratogenic rubella virus.The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers.Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport.Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal.The paramyxovirus simian virus 5 hemagglutinin-neuraminidase glycoprotein, but not the fusion glycoprotein, is internalized via coated pits and enters the endocytic pathway.Rubella virus capsid protein: a small protein with big functions.Class II enveloped viruses.Characterization of Borna disease virus p56 protein, a surface glycoprotein involved in virus entry.Effects of mutations in the rubella virus E1 glycoprotein on E1-E2 interaction and membrane fusion activity.Rubella virus E2 signal peptide is required for perinuclear localization of capsid protein and virus assembly.Characterization of the Golgi retention motif of Rift Valley fever virus G(N) glycoprotein.Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication.Characterization of an endoplasmic reticulum retention signal in the rubella virus E1 glycoprotein.Rubella virus capsid protein interacts with poly(a)-binding protein and inhibits translation.The protein-tyrosine phosphatase CD45 reaches the cell surface via golgi-dependent and -independent pathways.Cell-permeable ceramides preferentially inhibit coated vesicle formation and exocytosis in Chinese hamster ovary compared with Madin-Darby canine kidney cells by preventing the membrane association of ADP-ribosylation factor.The rubella virus capsid protein inhibits mitochondrial import.Requirement of the N-terminal region of orthobunyavirus nonstructural protein NSm for virus assembly and morphogenesis.
P2860
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P2860
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
description
1993 nî lūn-bûn
@nan
1993 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1993年の論文
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1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
name
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@ast
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@en
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@nl
type
label
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@ast
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@en
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@nl
prefLabel
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@ast
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@en
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@nl
P2093
P2860
P356
P1476
The rubella virus E2 and E1 spike glycoproteins are targeted to the Golgi complex
@en
P2093
L Woodward
M G Farquhar
T C Hobman
P2860
P304
P356
10.1083/JCB.121.2.269
P407
P577
1993-04-01T00:00:00Z