Pertussis toxin has eukaryotic-like carbohydrate recognition domains - Wikidata - awgldk - TriplyDB

Pertussis toxin has eukaryotic-like carbohydrate recognition domains

Pertussis toxin has eukaryotic-like carbohydrate recognition domains

http://www.wikidata.org/entity/Q36759213

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Comparative genomics of the classical Bordetella subspecies: the evolution and exchange of virulence-associated diversity amongst closely related pathogens Primary cilia utilize glycoprotein-dependent adhesion mechanisms to stabilize long-lasting cilia-cilia contacts.Pertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology tools Bacterial Toxins as Pathogen Weapons Against Phagocytes The fourth immunoglobulin-like domain of NCAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth.Heparin-inhibitable lectin activity of the filamentous hemagglutinin adhesin of Bordetella pertussis Role of pertussis toxin A subunit in neutrophil migration and vascular permeability.Progress in high resolution atomic force microscopy in biology.Characterization of pertussis toxin analogs containing mutations in B-oligomer subunits Exploring novel vaccines against Helicobacter pylori: protective and therapeutic immunization.Aerolysin and pertussis toxin share a common receptor-binding domain Role of Bordetella pertussis virulence factors in adherence to epithelial cell lines derived from the human respiratory tract Role of ADP-ribosyltransferase activity of pertussis toxin in toxin-adhesin redundancy with filamentous hemagglutinin during Bordetella pertussis infection Identification and characterization of the carbohydrate ligands recognized by pertussis toxin via a glycan microarray and surface plasmon resonance.Investigation in a murine model of possible mechanisms of enhanced local reactions to post-primary diphtheria-tetanus toxoid boosters in recipients of acellular pertussis-diphtheria-tetanus vaccine.G(i/o) protein-dependent and -independent actions of Pertussis Toxin (PTX).Mechanistic insight into pertussis toxin and lectin signaling using T cells engineered to express a CD8α/CD3ζ chimeric receptor.Consequences of microbial attachment: directing host cell functions with adhesins.Antibody-mediated neutralization of pertussis toxin-induced mitogenicity of human peripheral blood mononuclear cells.Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells.Site-specific alterations in the B oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin.Prokaryotic peptides that block leukocyte adherence to selectins Bordetella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18).The B-oligomer of pertussis toxin deactivates CC chemokine receptor 5 and blocks entry of M-tropic HIV-1 strains Adhesion of Bordetella pertussis to eukaryotic cells requires a time-dependent export and maturation of filamentous hemagglutinin Properties of pertussis toxin B oligomer assembled in vitro from recombinant polypeptides produced by Escherichia coli.Interaction of pertussis toxin with human T lymphocytes.Significance of glycosphingolipid fatty acid chain length on membrane microdomain-mediated signal transduction.Pertussis: a matter of immune modulation.The ins and outs of pertussis toxin.Membrane microdomains in immunity: glycosphingolipid-enriched domain-mediated innate immune responses.Immunity to the respiratory pathogen Bordetella pertussis.The virulence factors of Bordetella pertussis: talented modulators of host immune response.The 70-kilodalton pertussis toxin-binding protein in Jurkat cells.Animal lectins as self/non-self recognition molecules. Biochemical and genetic approaches to understanding their biological roles and evolution.Intracellular delivery of a cytolytic T-lymphocyte epitope peptide by pertussis toxin to major histocompatibility complex class I without involvement of the cytosolic class I antigen processing pathway.Reversal of the CD4(+)/CD8(+) T-cell ratio in lymph node cells upon in vitro mitogenic stimulation by highly purified, water-soluble S3-S4 dimer of pertussis toxin.Role of carbohydrate recognition domains of pertussis toxin in adherence of Bordetella pertussis to human macrophages.Identification of a carbohydrate recognition domain in filamentous hemagglutinin from Bordetella pertussis.Binding of pertussis toxin to lipid vesicles containing glycolipids.

P2860

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P2860

Pertussis toxin has eukaryotic-like carbohydrate recognition domains

http://www.wikidata.org/entity/Q36759213

description

1992 nî lūn-bûn

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1992年の論文

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1992年論文

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1992年論文

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1992年論文

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1992年論文

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1992年論文

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1992年论文

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1992年论文

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1992年论文

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name

Pertussis toxin has eukaryotic-like carbohydrate recognition domains

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Pertussis toxin has eukaryotic-like carbohydrate recognition domains

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type

label

Pertussis toxin has eukaryotic-like carbohydrate recognition domains

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Pertussis toxin has eukaryotic-like carbohydrate recognition domains

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prefLabel

Pertussis toxin has eukaryotic-like carbohydrate recognition domains

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Pertussis toxin has eukaryotic-like carbohydrate recognition domains

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Pertussis toxin has eukaryotic-like carbohydrate recognition domains

@en

P2093

E I Tuomanen

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

H R Masure

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

K Saukkonen

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

V L Mar

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W N Burnette

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P2860

Cloning and sequencing of the pertussis toxin genes: operon structure and gene duplication

Pertussis toxin gene: nucleotide sequence and genetic organization

Identification of a region in the S1 subunit of pertussis toxin that is required for enzymatic activity and that contributes to the formation of a neutralizing antigenic determinant.

Legume lectins--a large family of homologous proteins.

Pertussis holotoxoid formed in vitro with a genetically deactivated S1 subunit.

The PapG protein is the alpha-D-galactopyranosyl-(1----4)-beta-D-galactopyranose-binding adhesin of uropathogenic Escherichia coli

Mapping of linear B-cell epitopes of the S2 subunit of pertussis toxin.

Mechanism of pertussis toxin B oligomer-mediated protection against Bordetella pertussis respiratory infection.

Integrin-mediated localization of Bordetella pertussis within macrophages: role in pulmonary colonization

Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein

P304

118-122

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scholarly article

P356

10.1073/PNAS.89.1.118

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P407

P433

1

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P478

89

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P577

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P5875

21425464

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P698

1729677

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P932

48187

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