Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity.
about
Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeMembrane accumulation of influenza A virus hemagglutinin triggers nuclear export of the viral genome via protein kinase Calpha-mediated activation of ERK signaling.Avian influenza viruses inhibit the major cellular signalling integrator c-Abl.Recombinant influenza A H3N2 viruses with mutations of HA transmembrane cysteines exhibited altered virological characteristics.Upconversion luminescence resonance energy transfer (LRET)-based biosensor for rapid and ultrasensitive detection of avian influenza virus H7 subtype.Functional significance of the hemadsorption activity of influenza virus neuraminidase and its alteration in pandemic viruses.Vaccination against influenza with recombinant hemagglutinin expressed by Schizochytrium sp. confers protective immunity.Mass spectrometric sequencing and acylation character analysis of C-terminal anchoring segment from Influenza A hemagglutinin.Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virusS acylation of the hemagglutinin of influenza viruses: mass spectrometry reveals site-specific attachment of stearic acid to a transmembrane cysteine.Influenza virus hemagglutinin (H3 subtype) requires palmitoylation of its cytoplasmic tail for assembly: M1 proteins of two subtypes differ in their ability to support assembly.Palmitoylations on murine coronavirus spike proteins are essential for virion assembly and infectivity.The cytoplasmic tail domain of influenza B virus hemagglutinin is important for its incorporation into virions but is not essential for virus replication in cell culture in the presence of compensatory mutations.Higher polymerase activity of a human influenza virus enhances activation of the hemagglutinin-induced Raf/MEK/ERK signal cascade.Hemagglutinin-esterase-fusion (HEF) protein of influenza C virus.Protease activation mutants elicit protective immunity against highly pathogenic avian influenza viruses of subtype H7 in chickens and mice.Protein-lipid interactions critical to replication of the influenza A virus.Palmitoylation of the influenza A virus M2 protein is not required for virus replication in vitro but contributes to virus virulence.Progress toward Understanding Protein S-acylation: Prospective in PlantsAssociation of influenza virus proteins with membrane rafts.Lipid domain association of influenza virus proteins detected by dynamic fluorescence microscopy techniques.Palmitoylation contributes to membrane curvature in Influenza A virus assembly and hemagglutinin-mediated membrane fusion.Two Cytoplasmic Acylation Sites and an Adjacent Hydrophobic Residue, but No Other Conserved Amino Acids in the Cytoplasmic Tail of HA from Influenza A Virus Are Crucial for Virus Replication.Site-specific S-acylation of influenza virus hemagglutinin: the location of the acylation site relative to the membrane border is the decisive factor for attachment of stearate.Mutation of a raft-targeting signal in the transmembrane region retards transport of influenza virus hemagglutinin through the Golgi.Modulation of cell surface transport and lipid raft localization by the cytoplasmic tail of the influenza virus hemagglutinin.The role of stearate attachment to the hemagglutinin-esterase-fusion glycoprotein HEF of influenza C virus.Influenza virus pathogenicity is determined by caspase cleavage motifs located in the viral proteins.A cholesterol consensus motif is required for efficient intracellular transport and raft association of a group 2 HA from influenza virus.Acylation and cholesterol binding are not required for targeting of influenza A virus M2 protein to the hemagglutinin-defined budozone.The carboxy-terminal domain of glycoprotein N of human cytomegalovirus is required for virion morphogenesis.Structural features of fusogenic model transmembrane domains that differentially regulate inner and outer leaflet mixing in membrane fusion.Mass spectrometry analysis of influenza virus reassortant clones does not reveal an influence of other viral proteins on S-acylation of hemagglutinin.Protein Palmitoylation and Its Role in Bacterial and Viral Infections.Recycling of MUC1 is dependent on its palmitoylation.Influenza A Virus Cell Entry, Replication, Virion Assembly and MovementDeep Sequencing of H7N9 Influenza A Viruses from 16 Infected Patients from 2013 to 2015 in Shanghai Reveals Genetic Diversity and Antigenic Drift
P2860
Q27487974-CA665390-4794-4498-A8F2-0B4505916B24Q27863918-BF66708B-F718-432D-973C-567754E2FE1FQ30009343-7100529F-D9B5-4353-969D-97410EADBA2BQ30355996-33E2D5F0-3F77-4345-8349-A411D8B38378Q30359810-4F04487A-EFA0-4712-ACBA-EC01CC423E5CQ30377325-D2C47F57-4F12-4C3C-A4E8-D06679709693Q30429880-EC996E9D-6814-46C3-B3F6-74ABBA7C289EQ33236170-A5BA227C-4457-4652-89B4-6EBEB97EC34FQ33318082-5E9AB0A7-6019-41E1-A4EE-336AFFDAAE90Q33348431-95962A10-F7F4-4ED7-807B-CAD51F2434FBQ34092725-BA1D3FBA-8864-45F1-AB67-96AB9E8468A7Q34302034-76391F5B-A392-4D96-BB6F-799144A9897FQ36363199-AD974702-0EB3-4B1A-9838-4D045C2A443CQ36419847-66474537-1EF0-4626-9238-7B3531D266E4Q36447882-31ADF213-2407-4917-9CFF-C7AF46AF379CQ36778856-919A468E-E83B-4763-8BDD-24985C153509Q37222632-4D3D4106-F0E3-4F12-A2B3-6B8F7A7C24A5Q37333871-2799E723-16AC-4C21-8352-CDAC6C80387BQ37719052-9DF5C07A-1273-4009-8395-D3206C441EFFQ37982058-027D7395-664A-4250-A6DF-F7F0526EE46DQ38051421-44DFA100-DEB4-439C-ADD7-5038435DFD54Q38631745-FF672146-7EB3-4428-A781-5F6B81EE23ADQ38811637-B794BF23-B797-40AD-8664-13E62743E42AQ38944670-30F341CD-F421-4A70-8FC7-7CDB40DAF6D3Q39412349-3D069240-7B99-4FB4-A85C-F7C4198DDD66Q40659443-59349EFD-D1F3-4F95-8967-3F24B4A5E2B0Q41166047-2F9E836C-8387-4459-941D-1754F38C640CQ41841585-A07163DB-3234-4011-B33E-C3C36C26783AQ42183262-FD566454-1D05-48FF-9FB0-50D2B8547328Q42235675-B10E4DC9-9E18-4611-8FF0-A8077BA03873Q42737921-7EF32D41-C038-486C-8878-7BFC5E07811AQ45237236-7A0D926F-3A73-4A76-A194-C3089D2F5006Q45354345-50EED399-A0AC-4F6D-BBC3-002D9F6CDAF3Q49511036-E6445F33-C00F-42E7-B570-D2828CDB4455Q50737955-0FBCCBAE-63B2-462D-BD29-85357DE3E59DQ56981340-494210B7-2AF4-40EC-B599-3B840BCABAEBQ57004711-3F0BDA56-55D5-4486-A9E9-C92AEB502EB9
P2860
Acylation-mediated membrane anchoring of avian influenza virus hemagglutinin is essential for fusion pore formation and virus infectivity.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Acylation-mediated membrane an ...... rmation and virus infectivity.
@en
type
label
Acylation-mediated membrane an ...... rmation and virus infectivity.
@en
prefLabel
Acylation-mediated membrane an ...... rmation and virus infectivity.
@en
P2093
P2860
P1433
P1476
Acylation-mediated membrane an ...... rmation and virus infectivity.
@en
P2093
Astrid Herwig
Nahid Azzouz
Ralf Wagner
P2860
P304
P356
10.1128/JVI.79.10.6449-6458.2005
P407
P577
2005-05-01T00:00:00Z