An amphipathic alpha-helix including glutamates 509 and 516 is crucial for membrane translocation of adenylate cyclase toxin and modulates formation and cation selectivity of its membrane channels.
about
Bordetella adenylate cyclase toxin mobilizes its beta2 integrin receptor into lipid rafts to accomplish translocation across target cell membrane in two stepsRTX proteins: a highly diverse family secreted by a common mechanismCalcium influx rescues adenylate cyclase-hemolysin from rapid cell membrane removal and enables phagocyte permeabilization by toxin pores.Translocation-specific conformation of adenylate cyclase toxin from Bordetella pertussis inhibits toxin-mediated hemolysis.Differences in purinergic amplification of osmotic cell lysis by the pore-forming RTX toxins Bordetella pertussis CyaA and Actinobacillus pleuropneumoniae ApxIA: the role of pore size.Delivery of large heterologous polypeptides across the cytoplasmic membrane of antigen-presenting cells by the Bordetella RTX hemolysin moiety lacking the adenylyl cyclase domain.Role of CD11b/CD18 in the process of intoxication by the adenylate cyclase toxin of Bordetella pertussisStimulation of Bordetella pertussis adenylate cyclase toxin intoxication by its hemolysin domainMembrane restructuring by Bordetella pertussis adenylate cyclase toxin, a member of the RTX toxin family.The deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Acyltransferases in bacteria.Bordetella adenylate cyclase toxin: a unique combination of a pore-forming moiety with a cell-invading adenylate cyclase enzyme.Phospholipase A activity of adenylate cyclase toxin mediates translocation of its adenylate cyclase domain.Cyclic AMP-Elevating Capacity of Adenylate Cyclase Toxin-Hemolysin Is Sufficient for Lung Infection but Not for Full Virulence of Bordetella pertussis.Pore-forming and enzymatic activities of Bordetella pertussis adenylate cyclase toxin synergize in promoting lysis of monocytes.Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin.Cell surface binding, uptaking and anticancer activity of L-K6, a lysine/leucine-rich peptide, on human breast cancer MCF-7 cellsThe conserved tyrosine residue 940 plays a key structural role in membrane interaction of Bordetella adenylate cyclase toxin.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes.Understanding the Mechanism of Translocation of Adenylate Cyclase Toxin across Biological Membranes.Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins.Bordetella Pertussis Adenylate Cyclase Toxin Does Not Possess a Phospholipase A Activity; Serine 606 and Aspartate 1079 Residues Are Not Involved in Target Cell Delivery of the Adenylyl Cyclase Enzyme Domain.
P2860
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P2860
An amphipathic alpha-helix including glutamates 509 and 516 is crucial for membrane translocation of adenylate cyclase toxin and modulates formation and cation selectivity of its membrane channels.
description
1999 nî lūn-bûn
@nan
1999 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
An amphipathic alpha-helix inc ...... vity of its membrane channels.
@ast
An amphipathic alpha-helix inc ...... vity of its membrane channels.
@en
type
label
An amphipathic alpha-helix inc ...... vity of its membrane channels.
@ast
An amphipathic alpha-helix inc ...... vity of its membrane channels.
@en
prefLabel
An amphipathic alpha-helix inc ...... vity of its membrane channels.
@ast
An amphipathic alpha-helix inc ...... vity of its membrane channels.
@en
P2093
P1476
An amphipathic alpha-helix inc ...... vity of its membrane channels.
@en
P2093
P304
37644-37650
P407
P577
1999-12-01T00:00:00Z