The export pathway of the pseudorabies virus gB homolog gII involves oligomer formation in the endoplasmic reticulum and protease processing in the Golgi apparatus.
about
Accumulation of virion tegument and envelope proteins in a stable cytoplasmic compartment during human cytomegalovirus replication: characterization of a potential site of virus assembly.Human cytomegalovirus pp28 (UL99) localizes to a cytoplasmic compartment which overlaps the endoplasmic reticulum-golgi-intermediate compartment.A wide extent of inter-strain diversity in virulent and vaccine strains of alphaherpesviruses.A heterologous heparin-binding domain can promote functional attachment of a pseudorabies virus gC mutant to cell surfaces.Characterization of cell-binding properties of bovine herpesvirus 1 glycoproteins B, C, and D: identification of a dual cell-binding function of gB.Postoligomerization folding of human cytomegalovirus glycoprotein B: identification of folding intermediates and importance of disulfide bonding.The receptor-binding domain of pseudorabies virus glycoprotein gC is composed of multiple discrete units that are functionally redundant.The amino-terminal one-third of pseudorabies virus glycoprotein gIII contains a functional attachment domain, but this domain is not required for the efficient penetration of Vero cells.Oligomerization of the human cytomegalovirus major envelope glycoprotein complex gB (gp55-116).Characterization and sequence analyses of antibody-selected antigenic variants of herpes simplex virus show a conformationally complex epitope on glycoprotein H.A cellular function is required for pseudorabies virus envelope glycoprotein processing and virus egress.Expression of the Marek's disease virus homolog of herpes simplex virus glycoprotein B in Escherichia coli and its identification as B antigenOligomer formation of the gB glycoprotein of herpes simplex virus type 1.Cleavage of Epstein-Barr virus glycoprotein B is required for full function in cell-cell fusion with both epithelial and B cells.Herpes simplex virus type 1 glycoprotein K and the UL20 protein are interdependent for intracellular trafficking and trans-Golgi network localizationStructure-based functional analyses of domains II and III of pseudorabies virus glycoprotein H.Glycoproteins M and N of pseudorabies virus form a disulfide-linked complex.The attenuated pseudorabies virus strain Bartha fails to package the tegument proteins Us3 and VP22.Glycoprotein gB (gII) of pseudorabies virus can functionally substitute for glycoprotein gB in herpes simplex virus type 1.Proteolytic cleavage of bovine herpesvirus 1 (BHV-1) glycoprotein gB is not necessary for its function in BHV-1 or pseudorabies virus.Pseudorabies virus mutants lacking the essential glycoprotein gII can be complemented by glycoprotein gI of bovine herpesvirus 1.Effect of brefeldin A on alphaherpesvirus membrane protein glycosylation and virus egress.Pseudorabies virus envelope glycoproteins gp50 and gII are essential for virus penetration, but only gII is involved in membrane fusion.Protection of mice and swine from pseudorabies virus conferred by vaccinia virus-based recombinants.Overexpression in bacterial and identification in infected cells of the pseudorabies virus protein homologous to herpes simplex virus type 1 ICP18.5.Mutations in the C-terminal hydrophobic domain of pseudorabies virus gIII affect both membrane anchoring and protein export.
P2860
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P2860
The export pathway of the pseudorabies virus gB homolog gII involves oligomer formation in the endoplasmic reticulum and protease processing in the Golgi apparatus.
description
1990 nî lūn-bûn
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1990年の論文
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1990年学术文章
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1990年学术文章
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1990年学术文章
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1990年学术文章
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1990年學術文章
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1990年學術文章
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1990年學術文章
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name
The export pathway of the pseu ...... essing in the Golgi apparatus.
@en
type
label
The export pathway of the pseu ...... essing in the Golgi apparatus.
@en
prefLabel
The export pathway of the pseu ...... essing in the Golgi apparatus.
@en
P2093
P2860
P1433
P1476
The export pathway of the pseu ...... essing in the Golgi apparatus.
@en
P2093
P2860
P304
P407
P577
1990-05-01T00:00:00Z