In vivo generation and characterization of a soluble form of the Semliki forest virus fusion protein
about
Effects of membrane potential and sphingolipid structures on fusion of Semliki Forest virus.Novel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion proteinFurin Processing and Proteolytic Activation of Semliki Forest VirusFunctions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and AssemblyUbiquitin Depletion and Dominant-Negative VPS4 Inhibit Rhabdovirus Budding without Affecting Alphavirus BuddingRole of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion ProteinAn in vivo transfection approach elucidates a role for Aedes aegypti thioester-containing proteins in flaviviral infection.Alphavirus Entry and Membrane Fusion.Enhanced production of Chikungunya virus-like particles using a high-pH adapted spodoptera frugiperda insect cell line.An alphavirus temperature-sensitive capsid mutant reveals stages of nucleocapsid assemblyA specific domain of the Chikungunya virus E2 protein regulates particle formation in human cells: implications for alphavirus vaccine design.Class II fusion protein of alphaviruses drives membrane fusion through the same pathway as class I proteins.A key interaction between the alphavirus envelope proteins responsible for initial dimer dissociation during fusionA conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion.An Alphavirus E2 Membrane-Proximal Domain Promotes Envelope Protein Lateral Interactions and Virus Budding.The Alphavirus Exit Pathway: What We Know and What We Wish We Knew.
P2860
Q27472911-7DCF7BBF-EC92-4623-85D5-6EB652E6CF9AQ27472923-8B524CE5-5BF1-4FAF-80FB-593662197112Q27473344-8874CD23-187C-4A63-906A-A5F3FDB65DC0Q27477615-66C3F2CB-480C-4027-8D9D-5A97F8BA0CA3Q27485001-E6809D1B-C110-4BE1-87BA-0175BD16CE80Q27488309-61F8891A-3F2D-46CD-A3E0-2E08B56D224BQ33983448-6AAF824F-9D8A-4D0F-8C80-A10866382451Q34905189-4646F3C8-7375-43EC-8870-E8A9C5897143Q35142715-7E507F4C-D768-45BE-BCCF-C2D8782749BBQ36052886-57D5C95B-C452-4013-B452-1452A42E6261Q36171996-000F792F-E1B6-4FE5-9AAF-CF0164392114Q36321675-F62A0F32-C838-46B7-B450-7247BB2C5735Q36759804-2BC40246-43C7-4A10-B851-D726453CE959Q40487953-2BEF99F9-7A35-453C-9D5F-BD3940EAA48FQ44843596-CAA3B8CC-4CD2-4636-8DE8-E4D28392714FQ54268571-7783CCF1-5C8A-4ADB-B314-CBCDE01C423A
P2860
In vivo generation and characterization of a soluble form of the Semliki forest virus fusion protein
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
2001年论文
@zh
2001年论文
@zh-cn
name
In vivo generation and charact ...... ki forest virus fusion protein
@en
In vivo generation and charact ...... i forest virus fusion protein.
@nl
type
label
In vivo generation and charact ...... ki forest virus fusion protein
@en
In vivo generation and charact ...... i forest virus fusion protein.
@nl
prefLabel
In vivo generation and charact ...... ki forest virus fusion protein
@en
In vivo generation and charact ...... i forest virus fusion protein.
@nl
P2093
P2860
P1433
P1476
In vivo generation and charact ...... ki forest virus fusion protein
@en
P2093
P2860
P304
P356
10.1128/JVI.75.17.8329-8339.2001
P407
P577
2001-09-01T00:00:00Z