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Abstract Altered regulation of cell cycle, DNA repair, and apoptosis may not be the only ways that loss of p53 contributes to tumorigenesis. Roux and colleagues describe how the tumor suppressor protein p53 can regulate Cdc42-dependent (but neither RhoA- nor Rac-dependent) effects on cell...
Abstract The posttranslational modification of proteins—phosphorylation or dephosphorylation of serine and threonine residues—is usually considered essential for the initiation and maintenance of long-term potentiation (LTP) and long-term depression (LTD) in neural plasticity. Pelkey et al....
Abstract Ma et al. have reported that different G protein-regulated inwardly rectifying K + (GIRK) channels composed of combinations of Kir3.1-Kir3.2-Kir3.3-Kir3.4 are localized to different subcellular compartments. Kir3.3 seems to target Kir3.1-containing channels to lysosomes, whereas...
Abstract John Daly describes his career as “four decades as a chemist at a biomedical institute.” The term certainly fits: Daly speaks fluent organic chemistry, recounting reaction mechanisms that he has been involved with, among them landmark findings such as the “NIH shift” (first...
Abstract Receptor mutations that elicit loss of function are sometimes equated with defects that ablate receptor-ligand binding or receptor-effector interactions. Similarly, mutationally defective enzymes and ion channels are often viewed as compromised in substrate or ion recognition,...
Abstract GAF domains represent one of the largest families of small-molecule binding units present in nature. The first mammalian GAF domains discovered were the cGMP-binding regulatory domains of several cyclic nucleotide phosphodiesterases (PDEs). The crystal structure of the PDE2A GAF domains...
Abstract Cunningham and colleagues have reported that the unfolded protein response (UPR) stimulates cellular influx of calcium, thereby activating calcium-dependent proteins such as calcineurin and calmodulin, and that this activation may be important for UPR. However, the authors have more...
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