Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus.
about
Early Events in Chikungunya Virus Infection-From Virus Cell Binding to Membrane FusionExposure of epitope residues on the outer face of the chikungunya virus envelope trimer determines antibody neutralizing efficacyProteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes)Reversible Acid-Induced Inactivation of the Membrane Fusion Protein of Semliki Forest VirusSite-Directed Antibodies against the Stem Region Reveal Low pH-Induced Conformational Changes of the Semliki Forest Virus Fusion ProteinFunctions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and AssemblyStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeRole of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion ProteinE1 Mutants Identify a Critical Region in the Trimer Interface of the Semliki Forest Virus Fusion ProteinDealing with low pH: entry and exit of alphaviruses and flavivirusesA Stable Prefusion Intermediate of the Alphavirus Fusion Protein Reveals Critical Features of Class II Membrane FusionVirus membrane-fusion proteins: more than one way to make a hairpinFusogenic properties of the ectodomains of hepatitis C virus envelope proteins.The transmembrane domain and acidic lipid flip-flop regulates voltage-dependent fusion mediated by class II and III viral proteins.Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.Atypical fusion peptide of Nelson Bay virus fusion-associated small transmembrane proteinPseudorevertants of a Semliki forest virus fusion-blocking mutation reveal a critical interchain interaction in the core trimerAlphavirus Entry and Membrane Fusion.Chikungunya virus emergence is constrained in Asia by lineage-specific adaptive landscapes.Residue-level resolution of alphavirus envelope protein interactions in pH-dependent fusion.Chikungunya virus adaptation to Aedes albopictus mosquitoes does not correlate with acquisition of cholesterol dependence or decreased pH threshold for fusion reaction.The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusionIdentification of a specific region in the e1 fusion protein involved in zinc inhibition of semliki forest virus fusion.Mutational evidence of internal fusion loops in herpes simplex virus glycoprotein BClass 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 fusionFusion induced by a class II viral fusion protein, semliki forest virus E1, is dependent on the voltage of the target cell.A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion.Post-imaging fiducial markers aid in the orientation determination of complexes with mixed or unknown symmetry.
P2860
Q24701760-5B6058D7-BE9E-440B-93F1-0349FC301957Q24701766-5A554AB2-8B2E-4EE3-8003-0632A017DA7EQ24800750-6BD1EC21-2A4F-4373-BB27-AE2B13D95BDFQ27469816-45B7FC5F-9036-4531-A49F-A117CAEE084EQ27477540-0480E853-0DA0-45DA-88DC-C751F5807AA4Q27477615-414C2A72-6F73-4C2D-895D-D7C5A4827645Q27487974-DC7295DD-526F-4B78-A46E-E8D9910E4C0FQ27488309-0380555D-6518-4945-960A-E9AE42579FBDQ27490331-5B13D7C3-4E7C-4D64-BD5F-8E54231ED32EQ27490433-30220D08-6319-44CA-9EFE-0EC76755B36AQ27490513-E3B9E5B0-6F9E-4173-B812-AFCDCBE0AF8CQ29620769-4489E311-14AD-4303-B45E-DEC98F6A4C2EQ30360986-B8D0F96B-28BB-4879-933B-711029C6EAD8Q30416826-0C601669-A422-4126-BF40-20181B7E9EA2Q30426228-94A1CDAD-5366-467B-88AA-7F25AFC0BF65Q33716645-29007643-9D36-436A-BA18-400EC00B8304Q34295892-FF0D2509-791E-409E-B159-6EF0DD6A48BDQ34905189-A6D835FC-BB9A-4FAC-A2ED-C4B4C9800ABBQ34977748-4B0FBBF0-6475-42CB-8600-99E32C544E93Q35128812-06F89277-D5ED-4F80-8666-AB9AC86ACBB5Q35183277-2C7EA64C-1B4D-4E37-9E51-EB9A7AE4625DQ35531595-556A82E7-B2B7-419F-B739-ECBF015D50F8Q35826908-6B7263F8-B46A-428F-986D-CEA31F00B347Q35857450-D4F9BBC6-B23E-477D-BCFB-3BBB38BA4B5BQ36321675-A86FBF6B-C0AC-49AE-83E7-3DBDDAFDF493Q36759804-23E1F14F-0416-4FEE-AB7A-FBFFBFB162BBQ40096466-79E51678-77B7-49BA-8FB2-81542171F026Q40487953-5304F2D0-7E48-4D2C-9E3C-11FC23E7E5B7Q40898449-C57A9D44-D9D6-4B08-B5FF-E3E417788560
P2860
Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus.
@en
type
label
Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus.
@en
prefLabel
Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus.
@en
P2093
P2860
P1433
P1476
Multistep regulation of membrane insertion of the fusion peptide of Semliki Forest virus.
@en
P2093
Don L Gibbons
Lena Hammar
Maofu Liao
R Holland Cheng
P2860
P304
P356
10.1128/JVI.78.7.3312-3318.2004
P407
P577
2004-04-01T00:00:00Z