Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.
about
Structural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretionDisorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretionThe Bordetella adenylate cyclase repeat-in-toxin (RTX) domain is immunodominant and elicits neutralizing antibodies.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.Interaction of nuclease colicins with membranes: insertion depth correlates with bilayer perturbation.Calpain-Mediated Processing of Adenylate Cyclase Toxin Generates a Cytosolic Soluble Catalytically Active N-Terminal Domain.Calcium, acylation, and molecular confinement favor folding of Bordetella pertussis adenylate cyclase CyaA toxin into a monomeric and cytotoxic formBordetella 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.Bordetella Adenylate Cyclase-Hemolysin Toxins.Adenylate cyclase toxin-mediated delivery of the S1 subunit of pertussis toxin into mammalian cells.Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin.Stability, structural and functional properties of a monomeric, calcium-loaded adenylate cyclase toxin, CyaA, from Bordetella pertussis.Molecular Basis of Membrane Association by the Phosphatidylinositol Mannosyltransferase PimA Enzyme from Mycobacteria.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.Identification and in silico analysis of helical lipid binding regions in proteins belonging to the amphitropic protein family.Understanding the Mechanism of Translocation of Adenylate Cyclase Toxin across Biological Membranes.Phosphoproteomics of cAMP signaling of Bordetella adenylate cyclase toxin in mouse dendritic cells.Membrane-Active Properties of an Amphitropic Peptide from the CyaA Toxin Translocation Region.The catalytic domains of Clostridium sordellii lethal toxin and related large clostridial glucosylating toxins specifically recognize the negatively charged phospholipids phosphatidylserine and phosphatidic acid.Calmodulin fishing with a structurally disordered bait triggers CyaA catalysis.
P2860
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P2860
Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
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2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
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name
Identification of a region tha ...... rdetella pertussis CyaA toxin.
@en
Identification of a region tha ...... rdetella pertussis CyaA toxin.
@nl
type
label
Identification of a region tha ...... rdetella pertussis CyaA toxin.
@en
Identification of a region tha ...... rdetella pertussis CyaA toxin.
@nl
prefLabel
Identification of a region tha ...... rdetella pertussis CyaA toxin.
@en
Identification of a region tha ...... rdetella pertussis CyaA toxin.
@nl
P2093
P2860
P50
P356
P1476
Identification of a region tha ...... ordetella pertussis CyaA toxin
@en
P2093
Johanna C Karst
Marcus J Swann
Marilyne Davi
Stephen J Roser
P2860
P304
P356
10.1074/JBC.M111.316166
P407
P577
2012-01-12T00:00:00Z