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Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein BHerpes simplex virus type 1 entry is inhibited by the cobalt chelate complex CTC-96Multiple peptides homologous to herpes simplex virus type 1 glycoprotein B inhibit viral infectionLow pH-induced conformational change in herpes simplex virus glycoprotein B.Herpes simplex virus type 1 glycoprotein B requires a cysteine residue at position 633 for folding, processing, and incorporation into mature infectious virus particles.Herpes simplex virus glycoprotein B binds to cell surfaces independently of heparan sulfate and blocks virus entryThe Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Anti-glycoprotein D antibodies that permit adsorption but block infection by herpes simplex virus 1 prevent virion-cell fusion at the cell surface.Mapping regions of Epstein-Barr virus (EBV) glycoprotein B (gB) important for fusion function with gH/gL.Glycoprotein B of herpes simplex virus type 1 oligomerizes through the intermolecular interaction of a 28-amino-acid domainCross-linking of glycoprotein oligomers during herpes simplex virus type 1 entry.Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins.Exploitation of Cellular Cytoskeletons and Signaling Pathways for Cell Entry by Kaposi's Sarcoma-Associated Herpesvirus and the Closely Related Rhesus Rhadinovirus.Glycoprotein C of herpes simplex virus type 1 plays a principal role in the adsorption of virus to cells and in infectivityDifferential rates of processing and transport of herpes simplex virus type 1 glycoproteins gB and gC.Oligomer formation of the gB glycoprotein of herpes simplex virus type 1.Two distinct trimeric conformations of natively membrane-anchored full-length herpes simplex virus 1 glycoprotein B.A herpes simplex virus mutant in which glycoprotein D sequences are replaced by beta-galactosidase sequences binds to but is unable to penetrate into cells.Amino-terminal sequence, synthesis, and membrane insertion of glycoprotein B of herpes simplex virus type 1.Analysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesisHerpes simplex virus type 1 glycoprotein K and the UL20 protein are interdependent for intracellular trafficking and trans-Golgi network localizationHerpes simplex virus type 1 gK is required for gB-mediated virus-induced cell fusion, while neither gB and gK nor gB and UL20p function redundantly in virion de-envelopmentOvine Herpesvirus 2 Glycoproteins B, H, and L Are Sufficient for, and Viral Glycoprotein Ov8 Can Enhance, Cell-Cell Membrane Fusion.Assembly and organization of glycoproteins B, C, D, and H in herpes simplex virus type 1 particles lacking individual glycoproteins: No evidence for the formation of a complex of these molecules.Restoration of function of carboxy-terminally truncated pseudorabies virus glycoprotein B by point mutations in the ectodomain.Proteolytic processing of human cytomegalovirus glycoprotein B is dispensable for viral growth in culture.Oligomeric structure of glycoproteins in herpes simplex virus type 1.Disulfide bonds of herpes simplex virus type 2 glycoprotein gB.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.Identification and characterization of a novel structural glycoprotein in pseudorabies virus, gL.Effects of deletions in the carboxy-terminal hydrophobic region of herpes simplex virus glycoprotein gB on intracellular transport and membrane anchoring.Synthesis and processing of the Marek's disease herpesvirus B antigen glycoprotein complex.The pseudorabies virus gII gene is closely related to the gB glycoprotein gene of herpes simplex virus.Mildly Acidic pH Triggers an Irreversible Conformational Change in the Fusion Domain of Herpes Simplex Virus 1 Glycoprotein B and Inactivation of Viral Entry.Engineering glycoprotein B of bovine herpesvirus 1 to function as transporter for secreted proteins: a new protein expression approach.Binding of herpes simplex virus glycoprotein B (gB) to paired immunoglobulin-like type 2 receptor alpha depends on specific sialylated O-linked glycans on gB
P2860
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P2860
description
1986 nî lūn-bûn
@nan
1986 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1986 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
name
Oligomerization of herpes simplex virus glycoprotein B.
@ast
Oligomerization of herpes simplex virus glycoprotein B.
@en
type
label
Oligomerization of herpes simplex virus glycoprotein B.
@ast
Oligomerization of herpes simplex virus glycoprotein B.
@en
prefLabel
Oligomerization of herpes simplex virus glycoprotein B.
@ast
Oligomerization of herpes simplex virus glycoprotein B.
@en
P2860
P1433
P1476
Oligomerization of herpes simplex virus glycoprotein B.
@en
P2093
L Claesson-Welsh
P2860
P304
P407
P577
1986-11-01T00:00:00Z