Results 111 to 120 of about 175,144 (193)

Structural-functional aspects of the Bordetella pertussis adenylate cyclase toxin

open access: yes, 2023
Whooping cough (pertussis) is a highly infectious respiratory disease caused by the Gram-negative bacterium Bordetella pertussis. Even though the vaccination rate of the population is high, pertussis is one of the most widespread vaccine-preventable ...
Březinová, Karolína
core  

Bordetella Adenylate Cyclase Toxin Elicits Airway Mucin Secretion through Activation of the cAMP Response Element Binding Protein. [PDF]

open access: yesInt J Mol Sci, 2021
Malandra A   +8 more
europepmc   +1 more source

WR-2721 inhibits parathyroid adenylate cyclase

open access: yes, 1987
WR-2721 [S-2-(3-aminopropylamino)ethylphosphorothioic acid] is a chemoprotective and radioprotective agent that has been shown to lower serum calcium in dogs and in humans.
E. Slatopolsky   +5 more
core   +1 more source

Intranasal application of a bifunctional pertactin-RTX fusion antigen elicits protection of mouse airway mucosa against Bordetella pertussis colonization

open access: yesmSphere
The adenylate cyclase toxin (ACT, AC-Hly, or CyaA) plays a key role in airway infections by Bordetella pertussis and ablates the oxidative burst and opsonophagocytic capacity of sentinel phagocytes.
Carlos Espinosa-Vinals   +6 more
doaj   +1 more source

Dissociation by cooling of hormone and cholera toxin activation of adenylate cyclase in intact cells.

open access: yes, 1979
Cholera toxin, through adenylate cyclase activation reproduced cyclic AMP-mediated effects of thyroid-stimulating hormone (TSH) in dog thyroid slices, i.e. protein iodination, [1-14C]glucose-oxidation and hormone secretion.
Dumont, Jacques Emile   +2 more
core  

Susceptibility of Human Airway Tissue Models Derived From Different Anatomical Sites to Bordetella pertussis and Its Virulence Factor Adenylate Cyclase Toxin. [PDF]

open access: yesFront Cell Infect Microbiol, 2021
Sivarajan R   +7 more
europepmc   +1 more source

Almost half of the RTX domain is dispensable for complement receptor 3 binding and cell-invasive activity of the Bordetella adenylate cyclase toxin. [PDF]

open access: yesJ Biol Chem, 2021
Espinosa-Vinals CA   +7 more
europepmc   +1 more source

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