about
Herpes simplex virus glycoprotein B associates with target membranes via its fusion loopsStructure of a trimeric variant of the Epstein-Barr virus glycoprotein BAntigenic and mutational analyses of herpes simplex virus glycoprotein B reveal four functional regionsRetargeting Strategies for Oncolytic Herpes Simplex VirusesPrinciples of virus structural organizationRandom linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein BA Virus-Encoded Cell–Cell Fusion Machine Dependent on Surrogate AdhesinsStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeThe Structure of Herpesvirus Fusion Glycoprotein B-Bilayer Complex Reveals the Protein-Membrane and Lateral Protein-Protein InteractionNative 3D intermediates of membrane fusion in herpes simplex virus 1 entry.Turning of the receptor-binding domains opens up the murine leukaemia virus Env for membrane fusion.Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.Structural basis of nectin-1 recognition by pseudorabies virus glycoprotein DCapturing the herpes simplex virus core fusion complex (gB-gH/gL) in an acidic environment.Crystal structure of herpes simplex virus 2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.Differential effects on cell fusion activity of mutations in herpes simplex virus 1 glycoprotein B (gB) dependent on whether a gD receptor or a gB receptor is overexpressedThe Engineering of a Novel Ligand in gH Confers to HSV an Expanded Tropism Independent of gD Activation by Its ReceptorsCell-cell membrane fusion induced by p15 fusion-associated small transmembrane (FAST) protein requires a novel fusion peptide motif containing a myristoylated polyproline type II helix.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.Alternative entry receptors for herpes simplex virus and their roles in diseaseAnalysis of Epstein-Barr virus glycoprotein B functional domains via linker insertion mutagenesisPrimary B-cell infection with a deltaBALF4 Epstein-Barr virus comes to a halt in the endosomal compartment yet still elicits a potent CD4-positive cytotoxic T-cell response.Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein.The Ig-like v-type domain of paired Ig-like type 2 receptor alpha is critical for herpes simplex virus type 1-mediated membrane fusion.Engineered disulfide bonds in herpes simplex virus type 1 gD separate receptor binding from fusion initiation and viral entry.Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL in part through the C-terminal profusion domain.Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H.DNA vaccine expressing herpes simplex virus 1 glycoprotein C and D protects mice against herpes simplex keratitis.
P2860
Q24644405-A1EE6C17-3F40-4F58-B159-3DA04722DE93Q24645959-D47E7E5C-E55A-4C66-8D35-5371E181EF76Q24672176-C65CA4DF-9F1D-44AA-B6AF-4E0EC0D3317BQ26765439-09191747-4780-4F12-9BDF-DBDBAC6F42A0Q27021684-4D625FEF-3C39-445F-AF3A-8B7AD8E56BC4Q27480974-F0698E63-6C3D-499D-8E91-ED5F55012F90Q27485479-AB1BD6F5-AA20-4310-B585-7C4BA73EFF39Q27487974-635BE4A2-2987-446A-AF11-5BD1CE5275C5Q27679070-6C2DD61B-36F7-4FFF-9495-BA327CAC52BDQ30482898-C0A26679-03E2-49F7-820F-7E767E68C574Q30483804-C93CFBC7-F805-418D-9FF9-346C27462F5AQ33621028-083690BB-B884-415A-8383-112F1A1DF0F8Q33752109-195DE5F6-94B9-4077-ACC2-82F5E7BE6936Q34179684-1C94CA08-F4BA-446D-932C-88BCCDFD5D8BQ34594121-664303A1-B8B7-423B-9AE6-92FD08A9682DQ34982160-BF206F34-8652-4476-A97D-6B44E8BBD5AEQ35638350-3B566BD9-119C-4F32-BB95-E645B6787DB5Q35728426-0D8876DE-26EC-48C6-B229-6E99398D1947Q35948061-582B9D26-95EA-4AFA-90ED-5412B4DD82E5Q36154255-ACF6E5EE-4B5C-45B0-AC91-734D43C4DF6AQ37033353-76FCABF2-25B6-4515-ACDC-E3C6D5741999Q39879585-C2E7E0D1-3C84-4FB3-BD7C-FD19DB04AF4FQ40099372-A6289ADF-A275-4507-B51E-3F78586A5034Q41836765-15A04ED1-70E5-497D-9DA7-38725DA8CEB4Q41914603-4932B096-6C38-4F39-AF94-A068765B06FAQ42675409-BC876023-E373-43D7-ABDA-E7AD80819B82Q42736704-D7914666-5CE1-4104-85FE-3A39A631794DQ45324169-1933561D-793A-4156-8DED-0AA2D373DE56
P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Molecular gymnastics at the herpesvirus surface.
@ast
Molecular gymnastics at the herpesvirus surface.
@en
type
label
Molecular gymnastics at the herpesvirus surface.
@ast
Molecular gymnastics at the herpesvirus surface.
@en
prefLabel
Molecular gymnastics at the herpesvirus surface.
@ast
Molecular gymnastics at the herpesvirus surface.
@en
P2860
P356
P1433
P1476
Molecular gymnastics at the herpesvirus surface.
@en
P2860
P304
P356
10.1038/SJ.EMBOR.7400807
P50
P577
2006-10-01T00:00:00Z