Comprehensive analysis of ebola virus GP1 in viral entry. - Wikidata - awgldk - TriplyDB

Comprehensive analysis of ebola virus GP1 in viral entry.

Comprehensive analysis of ebola virus GP1 in viral entry.

http://www.wikidata.org/entity/Q33724185

about

T-cell immunoglobulin and mucin domain 1 (TIM-1) is a receptor for Zaire Ebolavirus and Lake Victoria Marburgvirus The Tyro3 receptor kinase Axl enhances macropinocytosis of Zaire ebolavirus Ebola virus entry requires the host-programmed recognition of an intracellular receptor Tyro3 family-mediated cell entry of Ebola and Marburg viruses The organisation of Ebola virus reveals a capacity for extensive, modular polyploidy IFITM3 restricts influenza A virus entry by blocking the formation of fusion pores following virus-endosome hemifusion Neutralizing ebolavirus: structural insights into the envelope glycoprotein and antibodies targeted against it Ebolavirus glycoprotein structure and mechanism of entry Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor Techniques and tactics used in determining the structure of the trimericebolavirusglycoprotein Host-Primed Ebola Virus GP Exposes a Hydrophobic NPC1 Receptor-Binding Pocket, Revealing a Target for Broadly Neutralizing Antibodies Structural and molecular basis for Ebola virus neutralization by protective human antibodies Immune protection of nonhuman primates against Ebola virus with single low-dose adenovirus vectors encoding modified GPs New small molecule entry inhibitors targeting hemagglutinin-mediated influenza a virus fusion Induction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a Trigger Ebolavirus is evolving but not changing: No evidence for functional change in EBOV from 1976 to the 2014 outbreak.Analysis of hemagglutinin-mediated entry tropism of H5N1 avian influenza.A new player in the puzzle of filovirus entry.Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.The primed ebolavirus glycoprotein (19-kilodalton GP1,2): sequence and residues critical for host cell binding.Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein.Cell adhesion promotes Ebola virus envelope glycoprotein-mediated binding and infection.Identification of N-glycans from Ebola virus glycoproteins by matrix-assisted laser desorption/ionisation time-of-flight and negative ion electrospray tandem mass spectrometry.Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity Identification of continuous human B-cell epitopes in the VP35, VP40, nucleoprotein and glycoprotein of Ebola virus Discovery, synthesis, and biological evaluation of a novel group of selective inhibitors of filoviral entry Identification of a small-molecule entry inhibitor for filoviruses.Ebola virion attachment and entry into human macrophages profoundly effects early cellular gene expression.Detection of cell-cell fusion mediated by Ebola virus glycoproteins.A "Trojan horse" bispecific-antibody strategy for broad protection against ebolaviruses Analysis of the highly diverse gene borders in Ebola virus reveals a distinct mechanism of transcriptional regulation.Serological evidence of ebolavirus infection in bats, China A comparative high-throughput screening protocol to identify entry inhibitors of enveloped viruses Inhibition of Ebola virus entry by a C-peptide targeted to endosomes.Structural basis for Marburg virus neutralization by a cross-reactive human antibody.sGP serves as a structural protein in Ebola virus infection.Influences of glycosylation on antigenicity, immunogenicity, and protective efficacy of ebola virus GP DNA vaccines Role of EXT1 and Glycosaminoglycans in the Early Stage of Filovirus Entry.Inhibition of Ebola and Marburg Virus Entry by G Protein-Coupled Receptor Antagonists Novel Small Molecule Entry Inhibitors of Ebola Virus.

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P2860

Comprehensive analysis of ebola virus GP1 in viral entry.

http://www.wikidata.org/entity/Q33724185

description

2005 nî lūn-bûn

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2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2005 թվականի ապրիլին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年論文

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2005年论文

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Comprehensive analysis of ebola virus GP1 in viral entry.

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Comprehensive analysis of ebola virus GP1 in viral entry.

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Comprehensive analysis of ebola virus GP1 in viral entry.

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Journal of Virology

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Comprehensive analysis of ebola virus GP1 in viral entry.

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Balaji Manicassamy

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Haiqing Jiang

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Jizhen Wang

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Lijun Rong

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P2860

C-type lectins DC-SIGN and L-SIGN mediate cellular entry by Ebola virus in cis and in trans

Differential N-linked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR

Human immunodeficiency virus type 1 viral protein R (Vpr) arrests cells in the G2 phase of the cell cycle by inhibiting p34cdc2 activity

Core structure of the envelope glycoprotein GP2 from Ebola virus at 1.9-A resolution

Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

Crystal structure of the Ebola virus membrane fusion subunit, GP2, from the envelope glycoprotein ectodomain

The PSIPRED protein structure prediction server

Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin

Development of a preventive vaccine for Ebola virus infection in primates

Vpr is required for efficient replication of human immunodeficiency virus type-1 in mononuclear phagocytes

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