Structural basis for paramyxovirus-mediated membrane fusion
about
Genetic variability of the envelope gene of Type D simian retrovirus-2 (SRV-2) subtypes associated with SAIDS-related retroperitoneal fibromatosis in different macaque speciesEntry of parainfluenza virus into cells as a target for interrupting childhood respiratory diseaseEphrin-B2 ligand is a functional receptor for Hendra virus and Nipah virusRole of the hemagglutinin-neuraminidase protein in the mechanism of paramyxovirus-cell membrane fusion.Poliovirus cell entry: common structural themes in viral cell entry pathwaysSecond sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusionInhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein.Measles Virus Fusion Protein: Structure, Function and InhibitionCell entry of enveloped virusesConformational reorganization of the SARS coronavirus spike following receptor binding: implications for membrane fusionThe central proline of an internal viral fusion peptide serves two important rolesFormation and characterization of the trimeric form of the fusion protein of Semliki Forest VirusMembrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusionMutational Evidence for an Internal Fusion Peptide in Flavivirus Envelope Protein EAttenuation of Murray Valley encephalitis virus by site-directed mutagenesis of the hinge and putative receptor-binding regions of the envelope protein.The Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core ComplexStructural basis of viral invasion: lessons from paramyxovirus FFunctional Analysis of the Transmembrane Domain in Paramyxovirus F Protein-Mediated Membrane FusionN- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coilStructural characterization of the human respiratory syncytial virus fusion protein coreThe trimer-of-hairpins motif in membrane fusion: Visna virusMutations that destabilize the gp41 core are determinants for stabilizing the simian immunodeficiency virus-CPmac envelope glycoprotein complexStructure of the dengue virus envelope protein after membrane fusionStructure of the HIV-1 gp41 Membrane-Proximal Ectodomain Region in a Putative Prefusion Conformation † , ‡Structure of the Newcastle disease virus F protein in the post-fusion conformationMembrane fusion machines of paramyxoviruses: capture of intermediates of fusionStudies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusionChSeq: A database of chameleon sequences.Role of sequence and structure of the Hendra fusion protein fusion peptide in membrane fusion.A bundling of viral fusion mechanisms.Studies of the "chain reversal regions" of the avian sarcoma/leukosis virus (ASLV) and ebolavirus fusion proteins: analogous residues are important, and a His residue unique to EnvA affects the pH dependence of ASLV entry.Cysteines flanking the internal fusion peptide are required for the avian sarcoma/leukosis virus glycoprotein to mediate the lipid mixing stage of fusion with high efficiency.Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusionFatal measles virus infection prevented by brain-penetrant fusion inhibitors.Probing the paramyxovirus fusion (F) protein-refolding event from pre- to postfusion by oxidative footprinting.Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR.Mode of action of an antiviral peptide from HIV-1. Inhibition at a post-lipid mixing stage.Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy.Residues in the heptad repeat a region of the fusion protein modulate the virulence of Sendai virus in mice
P2860
Q21093217-AC076661-2597-49C6-9296-31A378D6077BQ24530163-383A5816-90E8-4F32-AF7B-7CAE94BE48C9Q24532042-6B4DA12F-1724-4036-8058-D217F30DEB45Q24538786-112E1BFC-5B09-416C-A71E-8E96363A4A16Q24550839-B16B027A-94D3-4385-9968-B27F5160329DQ24600140-F41F5D41-D06A-4035-BA2D-71B7047B09EDQ24814238-E00F3920-299C-44CF-AFBB-DE7C4E7C6398Q26750552-8E1FCBCB-2C63-48AD-A00A-95C7BDC9C533Q26863682-8F7C28FA-17F5-4098-A5C8-C16882C10BE9Q27302420-140086E2-21B9-4DF6-A774-F490A3F82182Q27469628-AAFB088C-BECD-4F85-A455-91A1B7FB57FAQ27469686-C9BB73FE-0D8B-4409-BD26-9D0830DD8AFBQ27469690-0653287C-2FCE-4C47-9533-18A41ABB4885Q27469788-5F4CD959-8626-44AC-A565-25F900D4DD51Q27469932-069DBCB6-DE69-4589-977D-B4EB4034FFBDQ27477706-C960793E-6A24-4C39-A0BD-3F0F8C4920C7Q27481675-E06E1A52-CA14-429A-A85E-1DB9D04ECF3BQ27489741-DA9FCC6E-C489-4287-A0CA-C3D1A9434DDEQ27619272-186CAE5A-82B5-4F51-98DE-65CC6E85EEA1Q27628799-E32A37D6-7B4E-4C05-AA03-E9703C98E72FQ27633137-4F1685CC-DDF3-4B73-8B18-339277F0E6A8Q27637675-566B1EFB-0D47-4DC3-B2F5-8CACA20E6CA3Q27643009-8B80FA50-36C6-482E-BDA1-AE4BD050AE05Q27653846-4E970534-8C09-4F2F-97F0-7D53A678ACFEQ27661271-B1720178-8B2B-408E-86C4-85F27D0AE063Q28345073-C05545AC-5A95-4D8B-BB2B-6F53BF0F87B7Q28345849-CEC78A2E-A5F0-4854-9F15-EECE3B176523Q28646673-A144C738-2567-4628-AED0-196DBBE36784Q30374636-66AEF01F-6C19-427E-854C-46EE9A0624F5Q30417577-FB49FC66-1E4A-4906-B782-82EDB4711B13Q30430768-7AA21E29-39B5-4911-B098-6CBFD1EB29F8Q30434014-D5F14D66-3B0B-44A1-89C5-49BAFFDEA492Q30441449-53C15D00-5C03-42D3-803A-51D0140C2CA9Q30498517-494E9479-8A87-4777-A384-F3EBDB3CEB63Q30557599-A4210EC5-FC1B-4017-863F-8AB3EF103ECFQ30582350-2D88EA52-C2B9-4055-8588-5B3E5DB15530Q30734301-33E70CAA-7B1F-49A7-9035-F2A079329847Q31454800-254F6B24-DFC9-451C-B21A-A44B1C1CF16DQ33263085-21647F36-9CCE-4DD1-85A4-CDA3933E6129Q33558419-E4446737-7108-4500-B9C1-AAD7E9FAD5C5
P2860
Structural basis for paramyxovirus-mediated membrane fusion
description
1999 nî lūn-bûn
@nan
1999 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի մարտին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Structural basis for paramyxovirus-mediated membrane fusion
@ast
Structural basis for paramyxovirus-mediated membrane fusion
@en
Structural basis for paramyxovirus-mediated membrane fusion
@nl
type
label
Structural basis for paramyxovirus-mediated membrane fusion
@ast
Structural basis for paramyxovirus-mediated membrane fusion
@en
Structural basis for paramyxovirus-mediated membrane fusion
@nl
prefLabel
Structural basis for paramyxovirus-mediated membrane fusion
@ast
Structural basis for paramyxovirus-mediated membrane fusion
@en
Structural basis for paramyxovirus-mediated membrane fusion
@nl
P2093
P3181
P1433
P1476
Structural basis for paramyxovirus-mediated membrane fusion
@en
P2093
T S Jardetzky
P304
P3181
P356
10.1016/S1097-2765(00)80458-X
P577
1999-03-01T00:00:00Z