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Single Amino Acid Polymorphisms of Pertussis Toxin Subunit S2 (PtxB) Affect Protein FunctionIdentification of amino acid residues essential for the enzymatic activities of pertussis toxin.Mapping of linear B-cell epitopes of the S2 subunit of pertussis toxin.Epitopes on the S1 subunit of pertussis toxin recognized by monoclonal antibodiesEngineering of genetically detoxified pertussis toxin analogs for development of a recombinant whooping cough vaccine.Site-specific alterations in the B oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin.Specific lung mucosal and systemic immune responses after oral immunization of mice with Salmonella typhimurium aroA, Salmonella typhi Ty21a, and invasive Escherichia coli expressing recombinant pertussis toxin S1 subunit.Identification of linear B-cell determinants of pertussis toxin associated with the receptor recognition site of the S3 subunit.Construction of minitransposons for constitutive and inducible expression of pertussis toxin in bvg-negative Bordetella bronchisepticaLethal infection by Bordetella pertussis mutants in the infant mouse model.Inhibition of pertussis toxin binding to model receptors by antipeptide antibodies directed at an antigenic domain of the S2 subunit.Activities of complete and truncated forms of pertussis toxin subunits S1 and S2 synthesized by Escherichia coli.Nucleotide sequence homology to pertussis toxin gene in Bordetella bronchiseptica and Bordetella parapertussis.Effect of monoclonal antibody to pertussis toxin on toxin activity.Anaphylaxis or so-called encephalopathy in mice sensitized to an antigen with the aid of pertussigen (pertussis toxin)Detection of subunits of pertussis toxin in Tn5-induced Bordetella mutants deficient in toxin biological activityExpression of the S-1 catalytic subunit of pertussis toxin in Escherichia coli.Construction and characterization of Bordetella pertussis toxin mutants.Reduced glutathione is required for pertussis toxin secretion by Bordetella pertussis.Roles of the disulfide bond and the carboxy-terminal region of the S1 subunit in the assembly and biosynthesis of pertussis toxin.Expression of pertussis toxin in Bordetella bronchiseptica and Bordetella parapertussis carrying recombinant plasmids.Cloning, partial sequence, expression, and antigenic analysis of the filamentous hemagglutinin gene of Bordetella pertussis.The type III secreted protein BopD in Bordetella bronchiseptica is complexed with BopB for pore formation on the host plasma membrane.The BvgAS virulence control system regulates type III secretion in Bordetella bronchiseptica.Protein-chemical analysis of pertussis toxin reveals homology between the subunits S2 and S3, between S1 and the A chains of enterotoxins of Vibrio cholerae and Escherichia coli and identifies S2 as the haptoglobin-binding subunit.Progress with a recombinant whooping cough vaccine: a review.
P2860
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P2860
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年論文
@yue
1986年論文
@zh-hant
1986年論文
@zh-hk
1986年論文
@zh-mo
1986年論文
@zh-tw
1986年论文
@wuu
1986年论文
@zh
1986年论文
@zh-cn
name
Molecular cloning of pertussis toxin genes.
@ast
Molecular cloning of pertussis toxin genes.
@en
type
label
Molecular cloning of pertussis toxin genes.
@ast
Molecular cloning of pertussis toxin genes.
@en
prefLabel
Molecular cloning of pertussis toxin genes.
@ast
Molecular cloning of pertussis toxin genes.
@en
P2093
P2860
P356
P1476
Molecular cloning of pertussis toxin genes.
@en
P2093
Barstad PA
Coligan JE
P2860
P304
P356
10.1093/NAR/14.8.3251
P407
P577
1986-04-01T00:00:00Z