Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity - Test2 - elhamkhani - TriplyDB

Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity

Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity

http://www.wikidata.org/entity/Q33676579

about

Lectin-dependent enhancement of Ebola virus infection via soluble and transmembrane C-type lectin receptors Intracellular events and cell fate in filovirus infection Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection Identification of a broad-spectrum antiviral small molecule against severe acute respiratory syndrome coronavirus and Ebola, Hendra, and Nipah viruses by using a novel high-throughput screening assay Ebola virus entry requires the host-programmed recognition of an intracellular receptor The organisation of Ebola virus reveals a capacity for extensive, modular polyploidy Antigenic subversion: a novel mechanism of host immune evasion by Ebola virus A shared structural solution for neutralizing ebolaviruses Structural and molecular basis for Ebola virus neutralization by protective human antibodies Principles of Virus Uncoating: Cues and the Snooker Ball Ebola virus: A gap in drug design and discovery - experimental and computational perspective.Anti-Ebola therapies based on monoclonal antibodies: current state and challenges ahead.Mapping of Ebolavirus Neutralization by Monoclonal Antibodies in the ZMapp Cocktail Using Cryo-Electron Tomography and Studies of Cellular Entry Ebola virus and severe acute respiratory syndrome coronavirus display late cell entry kinetics: evidence that transport to NPC1+ endolysosomes is a rate-defining step Induction of Cell-Cell Fusion by Ebola Virus Glycoprotein: Low pH Is Not a Trigger A new player in the puzzle of filovirus entry.Cathepsin cleavage potentiates the Ebola virus glycoprotein to undergo a subsequent fusion-relevant conformational change.Structure of the Ebola virus glycoprotein spike within the virion envelope at 11 Å resolution.Ebola virus glycoprotein needs an additional trigger, beyond proteolytic priming for membrane fusion Cell entry by a novel European filovirus requires host endosomal cysteine proteases and Niemann-Pick C1.Camouflage and misdirection: the full-on assault of ebola virus disease Biological challenges and technological opportunities for respiratory syncytial virus vaccine development.An update on the use of antibodies against the filoviruses.Ebola virus glycoprotein Fc fusion protein confers protection against lethal challenge in vaccinated mice.Inhibition of Ebola virus entry by a C-peptide targeted to endosomes.Structural basis for Marburg virus neutralization by a cross-reactive human antibody.Impact of Ebola mucin-like domain on antiglycoprotein antibody responses induced by Ebola virus-like particles.Ebola virus entry: a curious and complex series of events.Protective mAbs and Cross-Reactive mAbs Raised by Immunization with Engineered Marburg Virus GPs The role of antigen-presenting cells in filoviral hemorrhagic fever: gaps in current knowledge.Filoviruses require endosomal cysteine proteases for entry but exhibit distinct protease preferences Filovirus entry into cells - new insights.Facile Discovery of a Diverse Panel of Anti-Ebola Virus Antibodies by Immune Repertoire Mining.Codon-optimized filovirus DNA vaccines delivered by intramuscular electroporation protect cynomolgus macaques from lethal Ebola and Marburg virus challenges Endocytic pathways involved in filovirus entry: advances, implications and future directions.Cell-cell contact promotes Ebola virus GP-mediated infection.Potent neutralizing monoclonal antibodies against Ebola virus infection Comprehensive functional analysis of N-linked glycans on Ebola virus GP1.Molecular characterization of the monoclonal antibodies composing ZMAb: a protective cocktail against Ebola virus.Assembly of the Marburg virus envelope.

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Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity

http://www.wikidata.org/entity/Q33676579

description

2010 nî lūn-bûn

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2010 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2010 թվականի հունվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年论文

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Biochemical and structural cha ...... viral entry and immunogenicity

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Biochemical and structural cha ...... viral entry and immunogenicity

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Biochemical and structural cha ...... viral entry and immunogenicity

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Biochemical and structural cha ...... viral entry and immunogenicity

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Biochemical and structural cha ...... viral entry and immunogenicity

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Chantelle L Hood

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Jeffrey C Boyington

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Jonathan Abraham

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Kwanyee Leung

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Peter D Kwong

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P2860

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

Tyro3 family-mediated cell entry of Ebola and Marburg viruses

Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor

Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection

Protective immunity to lethal challenge of the 1918 pandemic influenza virus by vaccination.

Alpha5beta1-integrin controls ebolavirus entry by regulating endosomal cathepsins.

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.

Folate receptor-alpha is a cofactor for cellular entry by Marburg and Ebola viruses.

Comprehensive analysis of ebola virus GP1 in viral entry.

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2972-2982

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10.1128/JVI.02151-09

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6

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84

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2010-01-06T00:00:00Z

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20053739

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2826059

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