pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
about
Replication of alphaviruses: a review on the entry process of alphaviruses into cellsPossible future monoclonal antibody (mAb)-based therapy against arbovirus infectionsFormation and characterization of the trimeric form of the fusion protein of Semliki Forest VirusAn epitope of the Semliki Forest virus fusion protein exposed during virus-membrane fusion.Entry and uncoating of enveloped virusesKinetics of endosome acidification detected by mutant and wild-type Semliki Forest virus.Molecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein.The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.Site-Directed Antibodies against the Stem Region Reveal Low pH-Induced Conformational Changes of the Semliki Forest Virus Fusion ProteinThe 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding processSphingolipid-dependent fusion of Semliki Forest virus with cholesterol-containing liposomes requires both the 3-hydroxyl group and the double bond of the sphingolipid backboneCholesterol is required in the exit pathway of Semliki Forest virusCholesterol is required for infection by Semliki Forest virusMembrane fusion process of Semliki Forest virus. I: Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cellsMembrane and protein interactions of a soluble form of the Semliki Forest virus fusion proteinRole of spike protein conformational changes in fusion of Semliki Forest virusRole of ribosomes in Semliki Forest virus nucleocapsid uncoatingMembrane fusion of Semliki Forest virus involves homotrimers of the fusion proteinConformational alteration of Sindbis virion glycoproteins induced by heat, reducing agents, or low pHBiosynthesis, maturation, and acid activation of the Semliki Forest virus fusion proteinMutagenesis of the putative fusion domain of the Semliki Forest virus spike proteinFusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62A conformational change in Sindbis virus glycoproteins E1 and E2 is detected at the plasma membrane as a consequence of early virus-cell interaction.The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturationRole of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion ProteinDifferential Incorporation of Cholesterol by Sindbis Virus Grown in Mammalian or Insect CellsA structural and functional perspective of alphavirus replication and assemblyThe alphaviruses: gene expression, replication, and evolutionMosquito cellular factors and functions in mediating the infectious entry of chikungunya virusStructural plasticity of the Semliki Forest virus glycome upon interspecies transmission.The surface conformation of Sindbis virus glycoproteins E1 and E2 at neutral and low pH, as determined by mass spectrometry-based mappingThe cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependenceLow pH-induced conformational change in herpes simplex virus glycoprotein B.Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular traffickingMembrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein.Alphavirus Entry and Membrane Fusion.Chikungunya virus neutralization antigens and direct cell-to-cell transmission are revealed by human antibody-escape mutants.Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus fusion protein.Vaccinia mature virus fusion regulator A26 protein binds to A16 and G9 proteins of the viral entry fusion complex and dissociates from mature virions at low pHPersistent reovirus infections of L cells select mutations in viral attachment protein sigma1 that alter oligomer stability
P2860
Q21296804-C21F1681-76A0-4529-AA86-7591277681F3Q24289014-4724FFC3-B118-4D37-87F2-0C17CDE75543Q27469686-2E52DCD4-6B64-4902-B5BB-7D55A54FF506Q27469752-37B62D57-C1D0-48BB-B170-FEBFF889A8FFQ27469760-1FBC2BFD-0705-418F-814D-D59CFD0B4D12Q27470014-884BA410-1575-4936-A192-59333BCA13B5Q27472838-B0DF7827-7FA7-43CC-975D-603D2C59834CQ27472848-A2A11A7F-FD3F-4ECE-AE8F-EC1737FC5973Q27477540-90A3FC17-BD10-4923-81A7-592B438F5944Q27478445-7CCFDDAB-8F41-40E4-B13A-1112EC11561CQ27478474-0B912A19-DAE0-4420-BFAA-2F3791FBD1DCQ27482648-77492A46-6C29-4D3E-8116-CE18C5BD9F6EQ27485689-E2C118A3-BBA4-4C1B-976B-A72CC9442EB8Q27485691-BF050C22-7104-4339-85AA-BA1F6C47F009Q27485999-DF09B21E-CA5C-4FD1-AA82-5A9F9E23AE9CQ27486079-B2DD6858-0D90-4975-B08C-D8B57BC46829Q27486197-86B30AC2-6EE0-40DE-A280-B93FD42A8232Q27486203-3222B6DB-C1A8-4E72-8723-BFCB8482A5C0Q27486236-D96D7CFE-32BA-42AB-A778-666F8E124A35Q27486494-0E37212A-7CEF-471C-8DF1-D2C43D9FC81AQ27486542-8470E3D0-7EE2-4121-8C6D-0C9A03C2689CQ27486570-BD488619-2C95-4A15-8F28-FAAC7498EC1EQ27486596-A9A79EA9-5BB4-43C8-906B-5040B17B7362Q27486630-04E6D6CB-FB41-43C5-AA8C-F4858EE9243FQ27488309-A39030A3-7C7D-4890-A996-41BFAA053D83Q27489520-9679C0ED-B214-4F65-A7A6-EA8A7BC6325CQ27490173-9D0DBDF4-2128-4C45-A700-E3A0E9A1B221Q27860954-5A23F1AF-71D8-4F8C-9AB6-A2484E00A0A7Q28486029-FBE30330-6B99-4112-97DE-F900513DCF72Q30358358-5945FD14-E19A-428E-AB9F-9FC00DF5E4DFQ30872909-99501B93-BCB6-46EF-9CFA-DDA5B8BF31E2Q33647933-31B379F7-1BE9-4B06-B0F5-94554DA0810CQ33769277-31EA4776-3F09-4F00-80FC-A8D01BEFBA1BQ33797871-16328261-29D7-4B58-A4AA-1A0A1EBD7A95Q34043702-ED007720-435D-46AF-9B3E-8B6B9328E1B9Q34905189-CEC110A3-369F-45E2-B6C4-41D8930C7D31Q35586877-CC96F62D-C286-46DA-82F7-F133DFA8C037Q35784690-D7B52487-87C2-48A9-B05D-C745C5F9B30CQ35826881-1542FA33-DDD4-4BB5-A0DD-C4EF8E56C65FQ35869465-61A93B4E-625A-462D-8904-C29B17A86CFF
P2860
pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
description
1985 nî lūn-bûn
@nan
1985年の論文
@ja
1985年論文
@yue
1985年論文
@zh-hant
1985年論文
@zh-hk
1985年論文
@zh-mo
1985年論文
@zh-tw
1985年论文
@wuu
1985年论文
@zh
1985年论文
@zh-cn
name
pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
@ast
pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
@en
type
label
pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
@ast
pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
@en
prefLabel
pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
@ast
pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
@en
P2860
P356
P1476
pH-induced alterations in the fusogenic spike protein of Semliki Forest virus
@en
P2093
A Helenius
P2860
P304
P356
10.1083/JCB.101.6.2284
P407
P577
1985-12-01T00:00:00Z