about
Fusion of Enveloped Viruses in Endosomes.Anti-Viral Properties of Amyloid-β Peptides.Insertion of a ligand to HER2 in gB retargets HSV tropism and obviates the need for activation of the other entry glycoproteins.Peptides Derived from Glycoproteins H and B of Herpes Simplex Virus Type 1 and Herpes Simplex Virus Type 2 Are Capable of Blocking Herpetic Infection in vitro.B Virus (Macacine Herpesvirus 1) Divergence: Variations in Glycoprotein D from Clinical and Laboratory Isolates Diversify Virus Entry Strategies.Ex vivo 2D and 3D HSV-2 infection model using human normal vaginal epithelial cells.Protective capacity of neutralizing and non-neutralizing antibodies against glycoprotein B of cytomegalovirus.Functional Relevance of the N-Terminal Domain of Pseudorabies Virus Envelope Glycoprotein H and Its Interaction with Glycoprotein L.Assembly and Egress of an Alphaherpesvirus Clockwork.A comparative review of viral entry and attachment during large and giant dsDNA virus infections.Structure-Based Mutations in the Herpes Simplex Virus 1 Glycoprotein B Ectodomain Arm Impart a Slow-Entry Phenotype.Epstein-Barr virus fusion with epithelial cells triggered by gB is restricted by a gL glycosylation site.The neutralizing linear epitope of human herpesvirus-6A glycoprotein B does not affect virus infectivity.Importin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.Two classes of protective antibodies against Pseudorabies virus variant glycoprotein B: Implications for vaccine design.Functional role of N-linked glycosylation in pseudorabies virus glycoprotein gH.Functional relevance of the transmembrane domain and cytoplasmic tail of the pseudorabies virus glycoprotein H for membrane fusion.The HSV-1 mechanisms of cell-to-cell spread and fusion are critically dependent on host PTP1B.A new era in cytomegalovirus vaccinology: considerations for rational design of next-generation vaccines to prevent congenital cytomegalovirus infection
P2860
Q28073406-569535AC-F409-44FB-AF32-7CD309E0D885Q30390299-4472C977-8753-453B-A447-69E95827DC69Q33621028-F74C527D-DA68-4A77-9235-B0DDAC6773BFQ36318677-537E396B-3EC2-4DF3-88D6-3B109262D37DQ37300411-06D120BD-FE0A-4FA9-AA32-EEC752A448B8Q37716535-38EA58B9-3592-4052-9036-0800197BA147Q38602178-991C6AED-4BCF-45DD-A21F-601E88408824Q38715323-22CD86C3-26FD-4B93-93DA-FB03DE95F152Q39320358-6E1A14AD-EAA0-4B7B-B672-88E9D300B50FQ40060063-84FF40F3-D820-49E7-B696-E7DE6E4252E1Q40198848-FA0A4005-9029-49BA-9F78-29075668AE88Q41928813-35A8F44F-183D-478A-AC8A-E10B6D5668D7Q45323694-4F04E2F5-736E-443E-968A-8B1EDA35D7C0Q47205447-5AD5E6E8-D33D-4010-B60A-2F4DFAD38639Q47562844-9502F3DD-1910-4B14-A287-5A2E798DCE38Q50043291-26DBF56C-7F46-4121-837F-DF02F96A1382Q52331818-0AE13533-7E3D-466E-A2CC-6D18D273012FQ54217211-280B7230-54C0-47B1-B977-B274863BB5D5Q57072187-2E5F648A-F57E-426C-B399-A9E465A20D42
P2860
description
2015 nî lūn-bûn
@nan
2015 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Herpesvirus gB: A Finely Tuned Fusion Machine
@ast
Herpesvirus gB: A Finely Tuned Fusion Machine
@en
Herpesvirus gB: A Finely Tuned Fusion Machine
@nl
type
label
Herpesvirus gB: A Finely Tuned Fusion Machine
@ast
Herpesvirus gB: A Finely Tuned Fusion Machine
@en
Herpesvirus gB: A Finely Tuned Fusion Machine
@nl
prefLabel
Herpesvirus gB: A Finely Tuned Fusion Machine
@ast
Herpesvirus gB: A Finely Tuned Fusion Machine
@en
Herpesvirus gB: A Finely Tuned Fusion Machine
@nl
P2860
P921
P356
P1433
P1476
Herpesvirus gB: A Finely Tuned Fusion Machine
@en
P2093
Rebecca S Cooper
P2860
P304
P356
10.3390/V7122957
P407
P577
2015-12-11T00:00:00Z