Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation.
about
Structural and Mechanistic Insights into the Tropism of Epstein-Barr VirusHerpesvirus gB: A Finely Tuned Fusion MachineExtensive Mutagenesis of the HSV-1 gB Ectodomain Reveals Remarkable Stability of Its Postfusion FormMembrane deformation and scission by the HSV-1 nuclear egress complex.The Epstein-Barr virus (EBV) glycoprotein B cytoplasmic C-terminal tail domain regulates the energy requirement for EBV-induced membrane fusion.Modulation of Epstein-Barr virus glycoprotein B (gB) fusion activity by the gB cytoplasmic tail domainEnhanced expression of full-length human cytomegalovirus fusion protein in non-swelling baculovirus-infected cells with a minimal fed-batch strategy.Rapid genome assembly and comparison decode intrastrain variation in human alphaherpesviruses.The membrane-proximal region (MPR) of herpes simplex virus gB regulates association of the fusion loops with lipid membranes.An immunoreceptor tyrosine-based inhibition motif in varicella-zoster virus glycoprotein B regulates cell fusion and skin pathogenesis.Regulation of herpes simplex virus gB-induced cell-cell fusion by mutant forms of gH/gL in the absence of gD and cellular receptors.Dual split protein-based fusion assay reveals that mutations to herpes simplex virus (HSV) glycoprotein gB alter the kinetics of cell-cell fusion induced by HSV entry glycoproteinsRegulation of HSV glycoprotein induced cascade of events governing cell-cell fusion.The Glycoprotein B Cytoplasmic Domain Lysine Cluster Is Critical for Varicella-Zoster Virus Cell-Cell Fusion Regulation and InfectionMechanism of neutralization of herpes simplex virus by antibodies directed at the fusion domain of glycoprotein B.Syncytial Mutations Do Not Impair the Specificity of Entry and Spread of a Glycoprotein D Receptor-Retargeted Herpes Simplex Virus.Mutations in Pseudorabies Virus Glycoproteins gB, gD, and gH Functionally Compensate for the Absence of gL.Novel mutations in gB and gH circumvent the requirement for known gD Receptors in herpes simplex virus 1 entry and cell-to-cell spread.The UL21 Tegument Protein of Herpes Simplex Virus 1 Is Differentially Required for the Syncytial Phenotype.Mapping sites of herpes simplex virus type 1 glycoprotein D that permit insertions and impact gD and gB receptors usage.Interplay between the Herpes Simplex Virus 1 gB Cytodomain and the gH Cytotail during Cell-Cell Fusion.Epstein-Barr virus fusion with epithelial cells triggered by gB is restricted by a gL glycosylation site.Herpes simplex virus 1 glycoprotein M and the membrane-associated protein UL11 are required for virus-induced cell fusion and efficient virus entryMutations in the cytoplasmic tail of herpes simplex virus 1 gH reduce the fusogenicity of gB in transfected cells.Functional relevance of the transmembrane domain and cytoplasmic tail of the pseudorabies virus glycoprotein H for membrane fusion.
P2860
Q26752331-6DABD105-6347-45FA-BDA0-0D29CEBAA11FQ26774203-C1B5BA25-D34C-4400-8A88-CA7434479A3CQ27676847-6ADE5549-350C-4C0D-80C4-CE7B0825F16DQ30584459-A244320E-BD2A-488E-9B6F-F88D43A202F4Q34261421-7F8DC370-EAA9-4DF9-9CF5-88B2A46457F8Q34557882-878B3656-67DF-403F-A304-167AD3356666Q35111320-CB0D8C4C-E629-4682-A6DA-005FF626B490Q35677486-28FA607F-0509-4CB3-8B6A-27201D829A9FQ36432018-0E0F04A6-6C32-415F-A314-EEECEBCCA7A7Q36583285-79B52DE9-557B-4E71-9AF5-C16D5267C56AQ36647949-22D2B135-8B8D-44FB-AB74-75B6E32AE455Q37252695-67977CB2-3D37-482B-B89A-C7C0417299F1Q37415391-DED7704B-18ED-4A5E-AF2D-BF78E27DCB1FQ37512919-F4C188B4-7950-464C-B0A2-13E951E937F6Q37644037-262D7341-C735-425A-9060-180EB0D3840CQ38735164-FABD92D5-B516-46BF-A882-863C7AA93F90Q38812527-724D5115-0FDD-449B-99E0-71517FA96433Q39244734-3C0745C0-A3DA-42A8-A167-7A1F87A2596EQ40088691-DB25E210-C9B1-4EF6-AA2C-E4E8F4BE536EQ40310537-49AFDBAD-B412-46FF-8158-0BF6A12551E6Q40984579-C34924C6-E306-4B97-A764-AA3E6F9A5876Q41928813-C15470EA-703F-4646-8DB7-DBC4A33CA347Q42020749-A2A85D22-A2A5-4620-B5F7-ECB4116318BCQ42284668-BE36A943-FFE9-4DC6-B3D9-F97429AA37CBQ52331818-26975DBA-07BD-430D-8AF6-F6D8B8962778
P2860
Membrane requirement for folding of the herpes simplex virus 1 gB cytodomain suggests a unique mechanism of fusion regulation.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Membrane requirement for foldi ...... echanism of fusion regulation.
@en
Membrane requirement for foldi ...... echanism of fusion regulation.
@nl
type
label
Membrane requirement for foldi ...... echanism of fusion regulation.
@en
Membrane requirement for foldi ...... echanism of fusion regulation.
@nl
prefLabel
Membrane requirement for foldi ...... echanism of fusion regulation.
@en
Membrane requirement for foldi ...... echanism of fusion regulation.
@nl
P2093
P2860
P356
P1433
P1476
Membrane requirement for foldi ...... echanism of fusion regulation.
@en
P2093
David S King
Ekaterina E Heldwein
Jessica L Silverman
Neil G Greene
P2860
P304
P356
10.1128/JVI.00932-12
P407
P577
2012-05-23T00:00:00Z