The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Characterization of the alpha 1A-adrenoceptors of guinea pig liver membranes: studies using 5-[3H]methylurapidil.

Binding of 5-[3H]methylurapidil to guinea pig liver membranes was rapid, saturable, and reversible. Scatchard analysis of saturation isotherms indicated a single class of binding sites with a Kd of 0.86 nM and a Bmax of 36 fmol/mg of protein. Preincubation of the membranes with chlorethylclonidine did not alter significantly the binding parameters for 5-[3H]methylurapidil. Binding competition experiments were performed, and the order of potency for agonists was oxymetazoline > epinephrine > norepinephrine >> methoxamine; for antagonists, the potency order was (+)-niguldipine > or = 5-methylurapidil = prazosin = WB4101 > benoxathian > or = phentolamine > or = (-)-niguldipine. The binding affinity for epinephrine was modulated by the hydrolysis-resistant GTP analogue guanosine-5'-(beta, gamma-imido)triphosphate. The pharmacological profile of the 5-[3H]methylurapidil binding sites of guinea pig liver differs markedly from those of the cloned alpha 1-adrenoceptors (i.e., alpha 1B-, alpha 1C-, and alpha 1A/D-adrenoceptors) and resembles that of the classical alpha 1A receptor subtype.[1]


WikiGenes - Universities