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注意：仅列出部分参考文献，下载原文获取全部文献信息。PILRα is a herpes simplex virus-1 entry coreceptor that associates with glycoprotein B
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Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein
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Intracellular trafficking and maturation of herpes simplex virus type 1 gB and virus egress require functional biogenesis of multivesicular bodies
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Binding-site interactions between Epstein-Barr virus fusion proteins gp42 and gH/gL reveal a peptide that inhibits both epithelial and B-Cell membrane fusion
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Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane
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Separation of receptor-binding and profusogenic domains of glycoprotein D of herpes simplex virus 1 into distinct interacting proteins
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Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B
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The multipartite system that mediates entry of herpes simplex virus into the cell
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Molecular gymnastics at the herpesvirus surface
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Hydrophobic α-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion
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Crystal structure of glycoprotein B from herpes simplex virus 1
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Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
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Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B
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Heptad repeat 2 in herpes simplex virus 1 gH interacts with heptad repeat 1 and is critical for virus entry and fusion
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Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry
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Fusogenic domains in herpes simplex virus type 1 glycoprotein H
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The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors
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A heptad repeat in herpes simplex virus 1 gH, located downstream of the α-helix with attributes of a fusion peptide, is critical for virus entry and fusion
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JOURNAL OF VIROLOGY (2005)
Herpes simplex virus entry mediator associates in infected cells in a complex with viral proteins gD and at least gH
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The ectodomain of herpes simplex virus glycoprotein h contains a membrane α-helix with attributes of an internal fusion peptide, positionally conserved in the Herpesviridae family
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Simple and highly efficient BAC recombineering using gaIK selection
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The herpes simplex virus JMP mutant enters receptor-negative J cells through a novel pathway independent of the known receptors nectin1, HveA, and nectin2
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The soluble ectodomain of herpes simplex virus gD contains a membrane-proximal pro-fusion domain and suffices to mediate virus entry
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Herpes simplex virus: receptors and ligands for cell entry
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Herpes simplex virus glycoprotein K, but not its syncytial allele, inhibits cell-cell fusion mediated by the four fusogenic glycoproteins, gD, gB, gH, and gL
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Analysis of the role of the membrane-spanning and cytoplasmic tail domains of herpes simplex virus type 1 glycoprotein D in membrane fusion
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Critical residues in the CC′ ridge of the human nectin1 receptor V domain enable herpes simplex virus entry into the cell and act synergistically with the downstream region
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Herpes simplex virus glycoprotein D bound to the human receptor HveA
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Cell fusion induced by herpes simplex virus glycoproteins gB, gD, and gH-gL requires a gD receptor but not necessarily heparan sulfate
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Glycoprotein D or J delivered in trans blocks apoptosis in SK-N-SH cells induced by a herpes simplex virus 1 mutant lacking intact genes expressing both glycoproteins
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DNA vaccination against rat Her-2/neu p185 more effectively inhibits carcinogenesis than transplantable carcinomas in transgenic BALB/c mice
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