Functional and structural interactions between measles virus hemagglutinin and CD46
about
Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virusMembrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins.Crystal structure of two CD46 domains reveals an extended measles virus-binding surfaceA 3D model for the measles virus receptor CD46 based on homology modeling, Monte Carlo simulations, and hemagglutinin binding studiesApplications of flow cytometry to clinical microbiology.Clinical isolates of measles virus use CD46 as a cellular receptor.Multiple antiviral activities of cyanovirin-N: blocking of human immunodeficiency virus type 1 gp120 interaction with CD4 and coreceptor and inhibition of diverse enveloped viruses.Complement Evasion Strategies of Viruses: An Overview.Moesin is not a receptor for measles virus entry into mouse embryonic stem cells.Long-term sterilizing immunity to rinderpest in cattle vaccinated with a recombinant vaccinia virus expressing high levels of the fusion and hemagglutinin glycoproteinsCell entry by measles virus: long hybrid receptors uncouple binding from membrane fusionOncolysis by paramyxoviruses: multiple mechanisms contribute to therapeutic efficiency.Cell type-specific fusion cofactors determine human immunodeficiency virus type 1 tropism for T-cell lines versus primary macrophages.N-linked glycans with similar location in the fusion protein head modulate paramyxovirus fusion.Targeted strategies for henipavirus therapeuticsClinical testing of engineered oncolytic measles virus strains in the treatment of cancer: an overview.A target site for template-based design of measles virus entry inhibitors.Functional interaction between paramyxovirus fusion and attachment proteins.Oncolytic measles virus retargeting by ligand displayRecovery and characterization of a chimeric rinderpest virus with the glycoproteins of peste-des-petits-ruminants virus: homologous F and H proteins are required for virus viability.Octamerization enables soluble CD46 receptor to neutralize measles virus in vitro and in vivo.Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization.CD46 expression does not overcome the intracellular block of measles virus replication in transgenic rats.The CD46 transmembrane domain is required for efficient formation of measles-virus-mediated syncytium
P2860
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P2860
Functional and structural interactions between measles virus hemagglutinin and CD46
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Functional and structural interactions between measles virus hemagglutinin and CD46
@ast
Functional and structural interactions between measles virus hemagglutinin and CD46
@en
Functional and structural interactions between measles virus hemagglutinin and CD46
@nl
type
label
Functional and structural interactions between measles virus hemagglutinin and CD46
@ast
Functional and structural interactions between measles virus hemagglutinin and CD46
@en
Functional and structural interactions between measles virus hemagglutinin and CD46
@nl
prefLabel
Functional and structural interactions between measles virus hemagglutinin and CD46
@ast
Functional and structural interactions between measles virus hemagglutinin and CD46
@en
Functional and structural interactions between measles virus hemagglutinin and CD46
@nl
P2093
P2860
P1433
P1476
Functional and structural interactions between measles virus hemagglutinin and CD46
@en
P2093
P2860
P304
P407
P577
1995-06-01T00:00:00Z