Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
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Bordetella adenylate cyclase toxin mobilizes its beta2 integrin receptor into lipid rafts to accomplish translocation across target cell membrane in two stepsPertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology toolsRTX 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.Disorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretionCharge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.Albumin, in the Presence of Calcium, Elicits a Massive Increase in Extracellular Bordetella Adenylate Cyclase Toxin.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 pertussisSelective translocation of the Bordetella pertussis adenylate cyclase toxin across the basolateral membranes of polarized epithelial cellsCa2+ influx and tyrosine kinases trigger Bordetella adenylate cyclase toxin (ACT) endocytosis. Cell physiology and expression of the CD11b/CD18 integrin major determinants of the entry route.Calcium, acylation, and molecular confinement favor folding of Bordetella pertussis adenylate cyclase CyaA toxin into a monomeric and cytotoxic formThe deletion of several amino acid stretches of Escherichia coli alpha-hemolysin (HlyA) suggests that the channel-forming domain contains beta-strands.Membrane-Pore Forming Characteristics of the Bordetella pertussis CyaA-Hemolysin Domain.Adenylate cyclase toxin-hemolysin relevance for pertussis vaccines.Bordetella adenylate cyclase toxin: a unique combination of a pore-forming moiety with a cell-invading adenylate cyclase enzyme.Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.Cyclic AMP-Elevating Capacity of Adenylate Cyclase Toxin-Hemolysin Is Sufficient for Lung Infection but Not for Full Virulence of Bordetella pertussis.The conserved tyrosine residue 940 plays a key structural role in membrane interaction of Bordetella adenylate cyclase toxin.Stability, structural and functional properties of a monomeric, calcium-loaded adenylate cyclase toxin, CyaA, from Bordetella pertussis.Structure-Function Relationships Underlying the Capacity of Bordetella Adenylate Cyclase Toxin to Disarm Host Phagocytes.Pore-formation by adenylate cyclase toxoid activates dendritic cells to prime CD8+ and CD4+ T cells.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
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
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name
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
@en
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
@nl
type
label
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
@en
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
@nl
prefLabel
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
@en
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
@nl
P2093
P50
P356
P1433
P1476
Oligomerization is involved in pore formation by Bordetella adenylate cyclase toxin.
@en
P2093
Elke Maier
Jana Vojtova-Vodolanova
Oldrich Benada
Oliver Knapp
P304
P356
10.1096/FJ.09-131250
P407
P577
2009-05-05T00:00:00Z