Functional interaction between paramyxovirus fusion and attachment proteins.
about
Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggeringMeasles Virus Fusion Protein: Structure, Function and InhibitionStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeStructure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion proteinStructure and Mutagenesis of the Parainfluenza Virus 5 Hemagglutinin-Neuraminidase Stalk Domain Reveals a Four-Helix Bundle and the Role of the Stalk in Fusion PromotionStructure of the parainfluenza virus 5 (PIV5) hemagglutinin-neuraminidase (HN) ectodomainMorbillivirus Experimental Animal Models: Measles Virus Pathogenesis Insights from Canine Distemper VirusSequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion processStructural basis of efficient contagion: measles variations on a theme by parainfluenza viruses.Measles virus entry inhibitors: a structural proposal for mechanism of action and the development of resistance.Structural and mechanistic studies of measles virus illuminate paramyxovirus entry.Measles virus-induced suppression of immune responses.Paramyxovirus glycoprotein incorporation, assembly and budding: a three way dance for infectious particle production.Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry.Probing the functions of the paramyxovirus glycoproteins F and HN with a panel of synthetic antibodies.Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptorsCanine distemper virus envelope protein interactions modulated by hydrophobic residues in the fusion protein globular head.Canine distemper virus infects canine keratinocytes and immune cells by using overlapping and distinct regions located on one side of the attachment proteinTiming is everything: Fine-tuned molecular machines orchestrate paramyxovirus entry.Emerging paramyxoviruses: molecular mechanisms and antiviral strategiesThe paramyxovirus fusion protein C-terminal region: mutagenesis indicates an indivisible protein unit.Ephrin-B2 and ephrin-B3 as functional henipavirus receptorsParamyxovirus fusion and entry: multiple paths to a common endStructural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusion.Adaptation of human parainfluenza virus to airway epithelium reveals fusion properties required for growth in host tissue.Cysteines in the stalk of the nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation.Type II integral membrane protein, TM of J paramyxovirus promotes cell-to-cell fusion.Base of the measles virus fusion trimer head receives the signal that triggers membrane fusion.Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.The human metapneumovirus fusion protein mediates entry via an interaction with RGD-binding integrins.New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk.Triggering the measles virus membrane fusion machinery.Individual N-glycans added at intervals along the stalk of the Nipah virus G protein prevent fusion but do not block the interaction with the homologous F protein.Envelope protein dynamics in paramyxovirus entry.A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F)Measles virus attachment proteins with impaired ability to bind CD46 interact more efficiently with the homologous fusion proteinHydrophobic and charged residues in the central segment of the measles virus hemagglutinin stalk mediate transmission of the fusion-triggering signal.Mutagenesis of Paramyxovirus Hemagglutinin-Neuraminidase Membrane-Proximal Stalk Region Influences Stability, Receptor Binding, and Neuraminidase Activity.Mutations in the parainfluenza virus 5 fusion protein reveal domains important for fusion triggering and metastability.
P2860
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P2860
Functional interaction between paramyxovirus fusion and attachment proteins.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Functional interaction between paramyxovirus fusion and attachment proteins.
@en
Functional interaction between paramyxovirus fusion and attachment proteins.
@nl
type
label
Functional interaction between paramyxovirus fusion and attachment proteins.
@en
Functional interaction between paramyxovirus fusion and attachment proteins.
@nl
prefLabel
Functional interaction between paramyxovirus fusion and attachment proteins.
@en
Functional interaction between paramyxovirus fusion and attachment proteins.
@nl
P2093
P2860
P356
P1476
Functional interaction between paramyxovirus fusion and attachment proteins.
@en
P2093
James P Snyder
Richard K Plemper
Tanja Paal
P2860
P304
16561-16572
P356
10.1074/JBC.M801018200
P407
P577
2008-04-21T00:00:00Z