The small envelope glycoprotein (GS) of equine arteritis virus folds into three distinct monomers and a disulfide-linked dimer

The small envelope glycoprotein (GS) of equine arteritis virus folds into three distinct monomers and a disulfide-linked dimer

Item
http://www.wikidata.org/entity/Q35839725
Coronavirus particle assembly: primary structure requirements of the membrane protein.Identification of the leader-body junctions for the viral subgenomic mRNAs and organization of the simian hemorrhagic fever virus genome: evidence for gene duplication during arterivirus evolution.Characterization of the coronavirus mouse hepatitis virus strain A59 small membrane protein E.Identification of a novel structural protein of arteriviruses.An unconventional role for cytoplasmic disulfide bonds in vaccinia virus proteins.Expression cloning and humoral immune response to the nucleocapsid and membrane proteins of equine arteritis virus.The two major envelope proteins of equine arteritis virus associate into disulfide-linked heterodimers.Structural protein requirements in equine arteritis virus assembly.Monoclonal antibodies directed against conserved epitopes on the nucleocapsid protein and the major envelope glycoprotein of equine arteritis virus.A subset of porcine reproductive and respiratory syndrome virus GP3 glycoprotein is released into the culture medium of cells as a non-virion-associated and membrane-free (soluble) form.Characterization of two new structural glycoproteins, GP(3) and GP(4), of equine arteritis virusFormation of disulfide-linked complexes between the three minor envelope glycoproteins (GP2b, GP3, and GP4) of equine arteritis virus.Biosynthesis of glycoproteins E and I of feline herpesvirus: gE-gI interaction is required for intracellular transport.Complex interactions between the major and minor envelope proteins of equine arteritis virus determine its tropism for equine CD3+ T lymphocytes and CD14+ monocytes.Intra- and intermolecular disulfide bonds of the GP2b glycoprotein of equine arteritis virus: relevance for virus assembly and infectivity.Folding and oligomerization of the gp2b/gp3/gp4 spike proteins of equine arteritis virus in vitro.Co-translational processing of glycoprotein 3 from equine arteritis virus: N-glycosylation adjacent to the signal peptide prevents cleavage.
P2860

The small envelope glycoprotein (GS) of equine arteritis virus folds into three distinct monomers and a disulfide-linked dimer

Item
http://www.wikidata.org/entity/Q35839725
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
The small envelope glycoprotei ...... s and a disulfide-linked dimer
@ast
The small envelope glycoprotei ...... s and a disulfide-linked dimer
@en
type
label
The small envelope glycoprotei ...... s and a disulfide-linked dimer
@ast
The small envelope glycoprotei ...... s and a disulfide-linked dimer
@en
prefLabel
The small envelope glycoprotei ...... s and a disulfide-linked dimer
@ast
The small envelope glycoprotei ...... s and a disulfide-linked dimer
@en
P1433
P1476
P2093
P2860
P304
P31
P407
P433
P478
P577
P698
P932
P1433
P1476
The small envelope glycoprotei ...... s and a disulfide-linked dimer
@en
P2093
P2860
P304
P31
P407
P433
P478
P577
P698
P932