A monoclonal antibody to Bacillus anthracis protective antigen defines a neutralizing epitope in domain 1 - Wikidata - wikimedia - TriplyDB

A monoclonal antibody to Bacillus anthracis protective antigen defines a neutralizing epitope in domain 1

A monoclonal antibody to Bacillus anthracis protective antigen defines a neutralizing epitope in domain 1

http://www.wikidata.org/entity/Q34721109

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Crystal Structure of the Engineered Neutralizing Antibody M18 Complexed to Domain 4 of the Anthrax Protective Antigen Isolation and chimerization of a highly neutralizing antibody conferring passive protection against lethal Bacillus anthracis infection Immunogenicity of Bacillus anthracis protective antigen domains and efficacy of elicited antibody responses depend on host genetic background.Neutralizing monoclonal antibodies directed against defined linear epitopes on domain 4 of anthrax protective antigen CD1d-dependent B-cell help by NK-like T cells leads to enhanced and sustained production of Bacillus anthracis lethal toxin-neutralizing antibodies.Neutralizing monoclonal antibody to edema toxin and its effect on murine anthrax.Select human anthrax protective antigen epitope-specific antibodies provide protection from lethal toxin challenge.Regulation of anthrax toxin-specific antibody titers by natural killer T cell-derived IL-4 and IFNγ.A requirement for FcγR in antibody-mediated bacterial toxin neutralization.Bacillus anthracis produces membrane-derived vesicles containing biologically active toxins.Identification of peptide sequences as a measure of Anthrax vaccine stability during storage.Mechanism of lethal toxin neutralization by a human monoclonal antibody specific for the PA(20) region of Bacillus anthracis protective antigen.Antibodies against anthrax: mechanisms of action and clinical applications.Functional analysis of neutralizing antibodies against Clostridium perfringens epsilon-toxin Analysis of epitope information related to Bacillus anthracis and Clostridium botulinum.Immunization of Mice with Anthrax Protective Antigen Limits Cardiotoxicity but Not Hepatotoxicity Following Lethal Toxin Challenge Monoclonal antibodies and toxins--a perspective on function and isotype.Rapid generation of an anthrax immunotherapeutic from goats using a novel non-toxic muramyl dipeptide adjuvant.MHC class II and non-MHC class II genes differentially influence humoral immunity to Bacillus anthracis lethal factor and protective antigen.Enhancement of antibody responses to Bacillus anthracis protective antigen domain IV by use of calreticulin as a chimeric molecular adjuvant Stochastic humoral immunity to Bacillus anthracis protective antigen: identification of anti-peptide IgG correlating with seroconversion to Lethal Toxin neutralization Disease-enhancing antibodies improve the efficacy of bacterial toxin-neutralizing antibodies Combinations of monoclonal antibodies to anthrax toxin manifest new properties in neutralization assays.In vitro evaluation, biodistribution and scintigraphic imaging in mice of radiolabeled anthrax toxins Galactoxylomannan-mediated immunological paralysis results from specific B cell depletion in the context of widespread immune system damage.Identification of linear epitopes in Bacillus anthracis protective antigen bound by neutralizing antibodies.Anthrax, toxins and vaccines: a 125-year journey targeting Bacillus anthracis.Radiolabeled antibodies to Bacillus anthracis toxins are bactericidal and partially therapeutic in experimental murine anthrax.Platelet-activating factor contributes to Bacillus anthracis lethal toxin-associated damage.Radioimmunotherapy of fungal diseases: the therapeutic potential of cytocidal radiation delivered by antibody targeting fungal cell surface antigens.Human serum contains a protease that protects against cytotoxic activity of Bacillus anthracis lethal toxin in vitro.Serum-Mediated Cleavage of Bacillus anthracis Protective Antigen Is a Two-Step Process That Involves a Serum Carboxypeptidase.

P2860

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P2860

A monoclonal antibody to Bacillus anthracis protective antigen defines a neutralizing epitope in domain 1

http://www.wikidata.org/entity/Q34721109

description

2006 nî lūn-bûn

@nan

2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հուլիսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

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name

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@ast

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@en

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@nl

type

label

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@ast

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@en

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@nl

prefLabel

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@ast

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@en

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@nl

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Infection and Immunity

P1476

A monoclonal antibody to Bacil ...... utralizing epitope in domain 1

@en

P2093

Antonio Nakouzi

http://www.w3.org/2001/XMLSchema#string

David Goldman

http://www.w3.org/2001/XMLSchema#string

Ekaterina Dadachova

http://www.w3.org/2001/XMLSchema#string

Ekaterina Revskaya

http://www.w3.org/2001/XMLSchema#string

Johanna Rivera

http://www.w3.org/2001/XMLSchema#string

Nareen Abboud

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of a complex between anthrax toxin and its host cell receptor

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Anthrax protective antigen forms oligomers during intoxication of mammalian cells

PA63 channel of anthrax toxin: an extended beta-barrel.

Enhancement of anthrax lethal toxin cytotoxicity: a subset of monoclonal antibodies against protective antigen increases lethal toxin-mediated killing of murine macrophages

Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers.

Clostridium perfringens iota-toxin: mapping of receptor binding and Ia docking domains on Ib.

Pathophysiological manifestations in mice exposed to anthrax lethal toxin.

A recombinant carboxy-terminal domain of the protective antigen of Bacillus anthracis protects mice against anthrax infection.

Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis.

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4149-4156

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scholarly article

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10.1128/IAI.00150-06

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7

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P478

74

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Arturo Casadevall

R. John Collier

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2006-07-01T00:00:00Z

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16790789

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1489699

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