Measles virus (MV) hemagglutinin: evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head.
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Crystal structure of measles virus hemagglutinin provides insight into effective vaccinesMeasles Virus Hemagglutinin Protein Epitopes: The Basis of Antigenic StabilityStructure of the measles virus hemagglutinin bound to the CD46 receptorStructure of the measles virus hemagglutinin bound to its cellular receptor SLAMStructure of measles virus hemagglutinin bound to its epithelial receptor nectin-4Phylodynamic analysis of the canine distemper virus hemagglutinin gene.Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategiesPrevention of measles virus infection by intranasal delivery of fusion inhibitor peptidesGenetic characterization of the hemagglutinin genes of wild-type measles virus circulating in china, 1993-2009Molecular evolution of haemagglutinin (H) gene in measles virus.Measles virus, immune control, and persistence.Lentiviral vectors displaying modified measles virus gp overcome pre-existing immunity in in vivo-like transduction of human T and B cells.A human lung carcinoma cell line supports efficient measles virus growth and syncytium formation via a SLAM- and CD46-independent mechanism.Paramyxoviruses: different receptors - different mechanisms of fusion.Henipavirus receptor usage and tropism.Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150).Glycoprotein interactions in paramyxovirus fusion.Identification of Hendra virus G glycoprotein residues that are critical for receptor binding.Multiple amino acid substitutions in hemagglutinin are necessary for wild-type measles virus to acquire the ability to use receptor CD46 efficiently.The heads of the measles virus attachment protein move to transmit the fusion-triggering signal.Morbillivirus receptors and tropism: multiple pathways for infection.Mutations in the H, F, or M Proteins Can Facilitate Resistance of Measles Virus to Neutralizing Human Anti-MV Sera.Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model.Previously unrecognized amino acid substitutions in the hemagglutinin and fusion proteins of measles virus modulate cell-cell fusion, hemadsorption, virus growth, and penetration rate.Nearby clusters of hemagglutinin residues sustain SLAM-dependent canine distemper virus entry in peripheral blood mononuclear cells.Canine distemper viruses expressing a hemagglutinin without N-glycans lose virulence but retain immunosuppression.Crystallization and preliminary crystallographic analysis of the measles virus hemagglutinin in complex with the CD46 receptor.Amino Acid substitutions in matrix, fusion and hemagglutinin proteins of wild measles virus for adaptation to vero cells.Isolation and complete nucleotide sequence of the measles virus IMB-1 strain in China.Measles Vaccine.Hemagglutinin-specific neutralization of subacute sclerosing panencephalitis viruses.Computational Analysis of the Interaction Energies between Amino Acid Residues of the Measles Virus Hemagglutinin and Its Receptors.
P2860
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P2860
Measles virus (MV) hemagglutinin: evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
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2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
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2004年學術文章
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2004年學術文章
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name
Measles virus (MV) hemagglutin ...... overlap on the globular head.
@en
Measles virus
@nl
type
label
Measles virus (MV) hemagglutin ...... overlap on the globular head.
@en
Measles virus
@nl
prefLabel
Measles virus (MV) hemagglutin ...... overlap on the globular head.
@en
Measles virus
@nl
P2093
P2860
P1433
P1476
Measles virus (MV) hemagglutin ...... overlap on the globular head.
@en
P2093
Benjamin Néel
Johannes P M Langedijk
Michelle Ainouze
Nicolas Massé
Robin Buckland
T Fabian Wild
P2860
P304
P356
10.1128/JVI.78.17.9051-9063.2004
P407
P577
2004-09-01T00:00:00Z