Titlebook: Receptor Signal Transduction Protocols; R. A. J. Challiss Book 1997 Springer Science+Business Media New York 1997

百靈鳥(niǎo)

Covalent Modification of G Proteins by Affinity Labeling identified a large array of closely related receptors (R), G protein subunits (G), and effecters (E). Currently, an important research goal is to understand the factors that, at each step of the cascade, link R to G to E, govern signal transfer, and signal integration following activation of a spec

細(xì)節(jié)

AND

dapper

Use of Antisense-Generating Plasmids to Probe the Function of Signal Transduction Proteins in Primarheir inaccessibility, but also by the lack of specific tools. The problem is particularly acute when the effect of interest must be measured at the single cell level, for example, receptor modulation of ion channels. Assignment of different G protein subunits to roles in ion channel modulation by re

離開(kāi)可分裂

Protocols Employed in the Investigation of G Protein-Coupled Receptor Phosphorylationcoupled receptor subtypes that have been demonstrated to undergo agonist-dependent phosphorylation (.). In fact, of the receptor subtypes studied, only three—namely the α.C4-adrenoceptor (.), β.-adrenoceptor (.), and the gonadotrophin-releasing hormone receptor (.—are thought not to undergo agonist-

Initiative

粗鄙的人

Radioligand Binding Measurement of Receptor Sequestration in Intact and Permeabilized Cellssequestered into a cell compartment to which hydrophilic ligands have only a limited access (.–.). Although receptor sequestration has frequently been documented, its physiological significance and underlying mechanism(s) remain obscure. This is largely the result of the routine use of intact cells

勤勉

Junction

978-1-4899-4283-8Springer Science+Business Media New York 1997

PRE

Receptor Signal Transduction Protocols978-1-59259-567-9Series ISSN 1064-3745 Series E-ISSN 1940-6029