Membrane restructuring by Bordetella pertussis adenylate cyclase toxin, a member of the RTX toxin family.
about
Bordetella adenylate cyclase toxin mobilizes its beta2 integrin receptor into lipid rafts to accomplish translocation across target cell membrane in two stepsVirulence factor rtx in Legionella pneumophila, evidence suggesting it is a modular multifunctional proteinPertussis toxin and adenylate cyclase toxin provide a one-two punch for establishment of Bordetella pertussis infection of the respiratory tractAdenylate cyclase toxin promotes internalisation of integrins and raft components and decreases macrophage adhesion capacityRole of CD11b/CD18 in the process of intoxication by the adenylate cyclase toxin of Bordetella pertussisOnly two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface.Recruitment of a phospholipase C/sphingomyelinase into non-lamellar lipid droplets during hydrolysis of lipid bilayers.Structural elements of the cholesterol-dependent cytolysins that are responsible for their cholesterol-sensitive membrane interactions.Calpain-Mediated Processing of Adenylate Cyclase Toxin Generates a Cytosolic Soluble Catalytically Active N-Terminal Domain.Ca2+ 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.Membrane organization and ionization behavior of the minor but crucial lipid ceramide-1-phosphate.Membrane association and destabilization by Aggregatibacter actinomycetemcomitans leukotoxin requires changes in secondary structuresTransbilayer (flip-flop) lipid motion and lipid scrambling in membranes.The RTX pore-forming toxin α-hemolysin of uropathogenic Escherichia coli: progress and perspectives.The role of ceramide-1-phosphate in biological functions.Phospholipase A activity of adenylate cyclase toxin mediates translocation of its adenylate cyclase domain.Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.End-product diacylglycerol enhances the activity of PI-PLC through changes in membrane domain structureAsymmetric addition of ceramides but not dihydroceramides promotes transbilayer (flip-flop) lipid motion in membranes.Inhibition of LtxA toxicity by blocking cholesterol binding with peptides.Adenylate Cyclase Toxin promotes bacterial internalisation into non phagocytic cells.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.Aggregatibacter actinomycetemcomitans leukotoxin is post-translationally modified by addition of either saturated or hydroxylated fatty acyl chainsAggregatibacter actinomycetemcomitans leukotoxin cytotoxicity occurs through bilayer destabilization.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.Human ATG3 binding to lipid bilayers: role of lipid geometry, and electric charge.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.The calcium-binding C-terminal domain of Escherichia coli alpha-hemolysin is a major determinant in the surface-active properties of the protein.Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins.
P2860
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P2860
Membrane restructuring by Bordetella pertussis adenylate cyclase toxin, a member of the RTX toxin family.
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@ast
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@en
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@nl
type
label
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@ast
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@en
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@nl
prefLabel
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@ast
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@en
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@nl
P2093
P2860
P1476
Membrane restructuring by Bord ...... ember of the RTX toxin family.
@en
P2093
Félix M Goñi
Helena Ostolaza
Ivo Konopasek
Jiri Masin
M-Asunción Requero
P2860
P304
P356
10.1128/JB.186.12.3760-3765.2004
P407
P577
2004-06-01T00:00:00Z