Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent. - sprookjes - yvandenbroek - TriplyDB

Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent.

Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent.

http://www.wikidata.org/entity/Q46677504

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Virulence factor rtx in Legionella pneumophila, evidence suggesting it is a modular multifunctional protein RTX proteins: a highly diverse family secreted by a common mechanism Alpha-hemolysin from Escherichia coli uses endogenous amplification through P2X receptor activation to induce hemolysis.Python erythrocytes are resistant to α-hemolysin from Escherichia coli.Mannheimia haemolytica leukotoxin binds to lipid rafts in bovine lymphoblastoid cells and is internalized in a dynamin-2- and clathrin-dependent manner.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Pore forming activity of the potent RTX-toxin produced by pediatric pathogen Kingella kingae: Characterization and comparison to other RTX-family members.RTX cytotoxins recognize beta2 integrin receptors through N-linked oligosaccharides Uropathogenic Escherichia coli-Associated Exotoxins Knockdown of the MAPK p38 pathway increases the susceptibility of Chilo suppressalis larvae to Bacillus thuringiensis Cry1Ca toxin.Pore-forming bacterial toxins and antimicrobial peptides as modulators of ADAM function.F199E substitution reduced toxicity of Clostridium perfringens epsilon toxin by depriving the receptor binding capability.Sialic acid residues are essential for cell lysis mediated by leukotoxin from Aggregatibacter actinomycetemcomitans.Brief heat treatment causes a structural change and enhances cytotoxicity of the Escherichia coli α-hemolysin.Bordetella adenylate cyclase toxin promotes calcium entry into both CD11b+ and CD11b- cells through cAMP-dependent L-type-like calcium channels.Putative identification of an amphipathic alpha-helical sequence in hemolysin of Escherichia coli (HlyA) involved in transmembrane pore formation.Acylation Enhances, but Is Not Required for, the Cytotoxic Activity of Mannheimia haemolytica Leukotoxin in Bighorn Sheep The calcium-binding C-terminal domain of Escherichia coli alpha-hemolysin is a major determinant in the surface-active properties of the protein.Functional Consequences of Calcium Influx Promoted by Bacterial Pore-Forming Toxins

P2860

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P2860

Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent.

http://www.wikidata.org/entity/Q46677504

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

Binding of Escherichia coli he ...... lls is not receptor-dependent.

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Binding of Escherichia coli he ...... lls is not receptor-dependent.

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Binding of Escherichia coli he ...... lls is not receptor-dependent.

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Binding of Escherichia coli he ...... lls is not receptor-dependent.

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Binding of Escherichia coli he ...... lls is not receptor-dependent.

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Binding of Escherichia coli he ...... lls is not receptor-dependent.

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P1433

Journal of Biological Chemistry

P1476

Binding of Escherichia coli he ...... lls is not receptor-dependent.

@en

P2093

Angela Valeva

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

Fatima Boukhallouk

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Helene Kemmer

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Isabel Siegel

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Ivan Walev

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

Silvia Weis

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Sucharit Bhakdi

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Triantafyllos Chavakis

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Trudy M Wassenaar

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P2860

Integrin leukocyte function-associated antigen-1-mediated cell binding can be activated by clustering of membrane rafts

Interaction of Escherichia coli hemolysin with biological membranes. A study using cysteine scanning mutagenesis.

Respiratory burst in human neutrophils.

Mannheimia haemolytica leukotoxin activates a nonreceptor tyrosine kinase signaling cascade in bovine leukocytes, which induces biological effects.

Membrane interaction of Escherichia coli hemolysin: flotation and insertion-dependent labeling by phospholipid vesicles.

Escherichia coli hemolysin is a potent inductor of phosphoinositide hydrolysis and related metabolic responses in human neutrophils.

RTX toxins recognize a beta2 integrin on the surface of human target cells.

Reversible adsorption and nonreversible insertion of Escherichia coli alpha-hemolysin into lipid bilayers.

Potent leukocidal action of Escherichia coli hemolysin mediated by permeabilization of target cell membranes.

Acylation of lysine 983 is sufficient for toxin activity of Bordetella pertussis adenylate cyclase. Substitutions of alanine 140 modulate acylation site selectivity of the toxin acyltransferase CyaC.

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36657-36663

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scholarly article

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10.1074/JBC.M507690200

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P433

44

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280

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2005-08-30T00:00:00Z

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P698

16131494

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