The E2 signal sequence of rubella virus remains part of the capsid protein and confers membrane association in vitro
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.Rubella virus replication and links to teratogenicityGERp95, a membrane-associated protein that belongs to a family of proteins involved in stem cell differentiationStructure-function relation of the NH2-terminal domain of the Semliki Forest virus capsid proteinProcessing and membrane topology of the spike proteins G1 and G2 of Uukuniemi virusSpike protein-nucleocapsid interactions drive the budding of alphavirusesRubella virus capsid protein structure and its role in virus assembly and infectionMonoclonal antibody-defined epitope map of expressed rubella virus protein domains.Assembly, maturation and three-dimensional helical structure of the teratogenic rubella virus.The Rubella virus capsid is an anti-apoptotic protein that attenuates the pore-forming ability of Bax.Short self-interacting N-terminal region of rubella virus capsid protein is essential for cooperative actions of capsid and nonstructural p150 proteins.Cryo-electron tomography of rubella virus.Analyses of phosphorylation events in the rubella virus capsid protein: role in early replication eventsIdentification of domains in rubella virus genomic RNA and capsid protein necessary for specific interactionInfluenza C virus CM2 integral membrane glycoprotein is produced from a polypeptide precursor by cleavage of an internal signal sequence.Alphavirus spike-nucleocapsid interaction and network antibodiesRubella virus E2 signal peptide is required for perinuclear localization of capsid protein and virus assembly.Phosphorylation of rubella virus capsid regulates its RNA binding activity and virus replication.Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion.Rubella virus capsid protein interacts with poly(a)-binding protein and inhibits translation.Incorporation of homologous and heterologous proteins into the envelope of Moloney murine leukemia virus.Immunoaffinity purification of baculovirus-expressed rubella virus E1 for diagnostic purposes.Membrane proteins organize a symmetrical virus.Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding.
P2860
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P2860
The E2 signal sequence of rubella virus remains part of the capsid protein and confers membrane association in vitro
description
1990 nî lūn-bûn
@nan
1990 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
The E2 signal sequence of rube ...... membrane association in vitro
@ast
The E2 signal sequence of rube ...... membrane association in vitro
@en
The E2 signal sequence of rube ...... membrane association in vitro
@nl
type
label
The E2 signal sequence of rube ...... membrane association in vitro
@ast
The E2 signal sequence of rube ...... membrane association in vitro
@en
The E2 signal sequence of rube ...... membrane association in vitro
@nl
prefLabel
The E2 signal sequence of rube ...... membrane association in vitro
@ast
The E2 signal sequence of rube ...... membrane association in vitro
@en
The E2 signal sequence of rube ...... membrane association in vitro
@nl
P2093
P2860
P1433
P1476
The E2 signal sequence of rube ...... membrane association in vitro
@en
P2093
P2860
P304
P577
1990-11-01T00:00:00Z