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Bordetella pertussis toxin

Bordetella pertussis Toxin Borer Sol Boroethane Boron Bromide Boron Chloride Boron Fluoride Boron Hydride Boron Tribromide Boron Trichloride Boron Trifluoride Botox... [Pg.636]

Fig. 2. Minimal components of the G protein-coupling cycle in a schematic chemotaxis pathway. (A) Chemotaxis G protein-coupled receptors reside in the plasma membrane associated with specific heterotrimeric G proteins. (B) Upon binding of a chemoattractant such as fMLF, the receptor catalyzes the exchange of GTP for GDP in the a subunit of the G protein, thereby dissociating the GTP-bound a subunit from the (3 subunit complex. Chemotaxis GPCRs typically utilize the a isoform of the a subunit. (C) Subsequently the dissociated GTP-bound a subunit and the j3 subunit complex each dock to effectors elsewhere in the cell. (D) The a subunit possesses intrinsic GTPase activity that hydrolyzes the bound GTP to GDP, thereby regenerating the GDP-bound Oj subunit that reassociates with the / 7 subunit complex and with the receptor. Bordetella pertussis toxin covalently and specifically modifies the isoform of the a subunit and prevents its association with receptor (see text for additional discussion and references). Fig. 2. Minimal components of the G protein-coupling cycle in a schematic chemotaxis pathway. (A) Chemotaxis G protein-coupled receptors reside in the plasma membrane associated with specific heterotrimeric G proteins. (B) Upon binding of a chemoattractant such as fMLF, the receptor catalyzes the exchange of GTP for GDP in the a subunit of the G protein, thereby dissociating the GTP-bound a subunit from the (3 subunit complex. Chemotaxis GPCRs typically utilize the a isoform of the a subunit. (C) Subsequently the dissociated GTP-bound a subunit and the j3 subunit complex each dock to effectors elsewhere in the cell. (D) The a subunit possesses intrinsic GTPase activity that hydrolyzes the bound GTP to GDP, thereby regenerating the GDP-bound Oj subunit that reassociates with the / 7 subunit complex and with the receptor. Bordetella pertussis toxin covalently and specifically modifies the isoform of the a subunit and prevents its association with receptor (see text for additional discussion and references).
Moss J, Stanley SJ, Watkins PA et al. (1986) Stimulation of the thiol-dependent ADP-ribosyltransferase and NAD glycohydrolase activities of Bordetella pertussis toxin by adenine nucleotides, phospholipids, and detergents. In Biochemistry 25 2720-2725... [Pg.61]

Fig. 4. Sequence homology between subunits S2 and S3 of Bordetella pertussis toxin and the selectins. Identical residues are underscored. Gaps have been introduced for optimal alignment. (Modified from ref. [123].)... Fig. 4. Sequence homology between subunits S2 and S3 of Bordetella pertussis toxin and the selectins. Identical residues are underscored. Gaps have been introduced for optimal alignment. (Modified from ref. [123].)...
Bordetella pertussis (toxin) Rabbit Lung Lactose, anti-Le antibody [166]... [Pg.496]

Moss J, Stanley SJ, Burns DL et al. Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of bordetella pertussis toxin (islet-activating protein). J Biol Chem 1983 238(19) 11879-11882. [Pg.10]

Watkins PA, Moss J, Burns DL, Hewlett EL, Vaughan M (1984) Inhibition of bovine rod outer segment GTPase by Bordetella pertussis. Toxin 259 1378-1381... [Pg.81]

Tummuru MK, Sharma SA, Blaser MJ (1995) Helicobacter pylori cag C, a homolog of the Bordetella pertussis toxin secretion protein, is required for induction of IL-8 in gastric epithelial cells. Gastroenterology A2A6... [Pg.188]

See other pages where Bordetella pertussis toxin is mentioned: [Pg.113]    [Pg.396]    [Pg.371]    [Pg.4]    [Pg.396]    [Pg.20]    [Pg.204]    [Pg.694]    [Pg.73]    [Pg.15]    [Pg.132]   
See also in sourсe #XX -- [ Pg.396 , Pg.397 ]

See also in sourсe #XX -- [ Pg.396 , Pg.397 ]



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Bordetella Toxin

Pertussis

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