about
Rab 5 is required for the cellular entry of dengue and West Nile virusesProteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes)Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomesFormation 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.Kinetics 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.Functions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and AssemblyAlphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomesCholesterol is required in the exit pathway of Semliki Forest virusUbiquitin Depletion and Dominant-Negative VPS4 Inhibit Rhabdovirus Budding without Affecting Alphavirus BuddingCholesterol is required for infection by Semliki Forest virusMembrane and protein interactions of a soluble form of the Semliki Forest virus fusion proteinRole of spike protein conformational changes in fusion of Semliki Forest virusBiosynthesis, maturation, and acid activation of the Semliki Forest virus fusion proteinMutagenesis of the putative fusion domain of the Semliki Forest virus spike proteinA conformational change in Sindbis virus glycoproteins E1 and E2 is detected at the plasma membrane as a consequence of early virus-cell interaction.Role of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion ProteinStructure of the St. Louis Encephalitis Virus Postfusion Envelope TrimerThe alphaviruses: gene expression, replication, and evolutionDengue virus ensures its fusion in late endosomes using compartment-specific lipids.The surface conformation of Sindbis virus glycoproteins E1 and E2 at neutral and low pH, as determined by mass spectrometry-based mappingSindbis virus glycoprotein E1 is divided into two discrete domains at amino acid 129 by disulfide bridge connections.The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependenceBiochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusionHuman dendritic cell activity against Histoplasma capsulatum is mediated via phagolysosomal fusionAlphavirus Entry and Membrane Fusion.The interaction of alphavirus E1 protein with exogenous domain III defines stages in virus-membrane fusionBST2/tetherin inhibition of alphavirus exit.Transmembrane signaling: an ion-flux-independent model for signal transduction by complexed Fc receptorspH-induced alterations in the fusogenic spike protein of Semliki Forest virusRole for adenosine triphosphate in regulating the assembly and transport of vesicular stomatitis virus G protein trimers.Acidification of endosome subpopulations in wild-type Chinese hamster ovary cells and temperature-sensitive acidification-defective mutants.Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exitMembrane fusion process of Semliki Forest virus. II: Cleavage-dependent reorganization of the spike protein complex controls virus entryLipidomics of host-pathogen interactions.Variant influenza virus hemagglutinin that induces fusion at elevated pHReceptor-mediated entry of diphtheria toxin into monkey kidney (Vero) cells: electron microscopic evaluationHost cell factors and functions involved in vesicular stomatitis virus entry.
P2860
Q24683001-4430CC87-0898-4AAA-9EBA-A2FA913B235DQ24800750-91BA8797-10F2-44AC-BE07-AD1AD1B86727Q24810483-403CF241-FB47-4796-A9CB-31D1DFD345ADQ27469686-B3C74318-1534-451F-86E4-73D07CAB86EFQ27469752-F90FA7C8-4189-497F-802F-4779404577B6Q27470014-A6C36565-B40B-4218-8D6A-21D7E07C7029Q27472838-A8CAA05E-5E91-49D1-B8CE-B8AFDDE2A5A9Q27477615-21DB3B44-C93A-4C65-85A0-7AFF490E45BAQ27482419-71097868-B9D2-404C-A35D-7CFC378A41DCQ27482648-DE1D01D2-D3F3-486F-AC09-E27B25D0F9F8Q27485001-4AB15692-CEEA-47E9-9171-743476C2465FQ27485689-1B08CFD0-9629-4432-B9A2-08CE387A306EQ27485999-ABBAFDF9-01AC-4D03-A967-5E13EB88263BQ27486079-C18973FD-03B7-46CC-A8EE-3AB90046BB69Q27486494-D939D54C-85AF-4608-8BFC-A489412F14D9Q27486542-72AFE90B-111E-4F4A-92A5-A31D91B44E4EQ27486596-D1C6B852-0B0E-4EBC-96CC-EF3DA4953BBBQ27488309-94889E20-65C9-44C9-B39E-A58B2E7F4145Q27674868-692B444A-FB12-463F-8CAB-CB3AEC3A2261Q27860954-985352A2-8A40-4442-8E07-96D1C7982140Q28475709-C4058F29-8788-43EC-9BFA-C48B481F6267Q30872909-5E041391-640F-48C7-8A83-A453910BBAE4Q33605141-79F58E26-853A-463A-972A-02150356DDD8Q33647933-C545D16F-6A6C-45F8-8860-183D78B419DBQ33797087-D7CD2AC2-B02C-4AE7-8451-20C7B800ED56Q34033498-56F88A77-3B14-427F-8704-85267495F089Q34905189-CAA63C44-F08A-4428-832C-4904E10EC0ECQ35531595-F3766632-F171-4293-823B-D566D6850139Q35544442-41C5A8FD-9981-4246-9E48-D124186E02A0Q36212014-CC3947FC-5DE9-4FC2-9AF5-DA2922B3E529Q36214003-47D5FF45-8F60-4ACA-ABE5-50432D304C6BQ36217751-2BD866BF-540F-4871-87DD-D37DD5380985Q36220457-BE4FC70A-5DF3-4FA7-9A68-2C38847C6795Q36237272-22ECDA2D-26D6-4A54-9C3C-D17A4988317FQ36254866-FE12A534-DD8B-44EE-82AA-09E23B1F724DQ36530818-0D78CC46-3ECB-463D-B6A8-98A9A7AE1D63Q36543297-872272CB-A46F-4435-A911-F6C0589DEA74Q36857895-37DBC2ED-A1E8-4B22-9716-3DCAB65583CAQ37031488-EAB93734-C554-4A71-B352-ECE37405F6FDQ37033185-B8438D6D-EBF1-4BDA-9896-C94AC9F48C31
P2860
description
1984 nî lūn-bûn
@nan
1984年の論文
@ja
1984年論文
@yue
1984年論文
@zh-hant
1984年論文
@zh-hk
1984年論文
@zh-mo
1984年論文
@zh-tw
1984年论文
@wuu
1984年论文
@zh
1984年论文
@zh-cn
name
Membrane fusion mutants of Semliki Forest virus
@ast
Membrane fusion mutants of Semliki Forest virus
@en
type
label
Membrane fusion mutants of Semliki Forest virus
@ast
Membrane fusion mutants of Semliki Forest virus
@en
prefLabel
Membrane fusion mutants of Semliki Forest virus
@ast
Membrane fusion mutants of Semliki Forest virus
@en
P2093
P2860
P356
P1476
Membrane fusion mutants of Semliki Forest virus
@en
P2093
Helenius A
Kielian MC
Kääriäinen L
P2860
P304
P356
10.1083/JCB.98.1.139
P407
P577
1984-01-01T00:00:00Z