February 15th, 2017 by Thomas J Gardella
Nature Chemical Biology 13, 247 (2017). doi:10.1038/nchembio.2316
Author: Thomas J Gardella
A new mechanism of functional crosstalk between two distinct G-protein-coupled receptors (GPCRs)—the parathyroid hormone receptor (PTHR) and β2-adrenergic receptor (β2 Ar)—that occurs at the level of G protein βγ subunits and a specific adenylyl cyclase isoform is identified. This crosstalk augments cAMP signaling by the PTHR from endosomes, and thus promotes the actions of PTH ligands in bone target cells.
February 15th, 2017 by Mirella Bucci
Nature Chemical Biology 13, 243 (2017). doi:10.1038/nchembio.2325
Author: Mirella Bucci
February 15th, 2017 by Grant Miura
Nature Chemical Biology 13, 243 (2017). doi:10.1038/nchembio.2322
Author: Grant Miura
February 15th, 2017 by Caitlin Deane
Nature Chemical Biology 13, 243 (2017). doi:10.1038/nchembio.2324
Author: Caitlin Deane
February 15th, 2017 by Fahim Farzadfard
Nature Chemical Biology 13, 245 (2017). doi:10.1038/nchembio.2315
Authors: Fahim Farzadfard & Timothy K Lu
Bioengineers have endowed a consortium of human cells with an artificial sense of smell, enabling the cells to detect, quantify, and remember the presence of gaseous volatile compounds in their environment.
February 15th, 2017 by Joshua M. Finkelstein
Nature Chemical Biology 13, 243 (2017). doi:10.1038/nchembio.2323
Author: Joshua M. Finkelstein
February 15th, 2017 by Amy M Ehrenworth
Nature Chemical Biology 13, 249 (2017). doi:10.1038/nchembio.2308
Authors: Amy M Ehrenworth & Pamela Peralta-Yahya
February 10th, 2017 by Yang Wang, Ralf Heermann and Kirsten Jung
February 2nd, 2017 by pthomas2
Abstract deadline Monday March 20, 2017. In addition to poster sessions, there will be oral sessions for contributed papers from Graduate students and postdocs, Early Career Investigators and Mid-Career Investigators. Speakers for these symposia will be selected from the submitted abstracts. If your abstract is not chosen for an oral presentation, it will be moved to a poster session. Click here to submit abstract.
Structural Basis for the Lesion-scanning Mechanism of the Bacterial MutY DNA Glycosylase [Enzymology]
January 27th, 2017 by Lan Wang, Srinivas Chakravarthy, Gregory L VerdineThe highly mutagenic A:oxoG (8-oxoguanine) base-pair is generated mainly by misreplication of the C:oxoG base-pair, the oxidation product of the C:G base-pair. A:oxoG base-pair is particularly insidious because neither base in it carries faithful information to direct the repair of the other. The bacterial MutY (MUTYH in humans) adenine DNA glycosylase is able to initiate the repair of A:oxoG by selectively cleaving the A base from the A:oxoG base-pair. The difference between faithful repair and wreaking mutagenic havoc on the genome lies in the accurate discrimination between two structurally similar base-pairs: A:oxoG and A:T. Here we present two crystal structures of the MutY N-terminal domain in complex with either undamaged DNA or DNA containing an intrahelical lesion. These structures have captured for the first time, a DNA glycosylase scanning the genome for a damaged base in the very first stage of lesion-recognition and the base-extrusion pathway. The mode of interaction observed here has suggested a common lesion-scanning mechanism across the entire helix-hairpin-helix superfamily to which MutY belongs. In addition, small-angle X-ray scattering (SAXS) studies together with accompanying biochemical assays have suggested a possible role played by the C-terminal oxoG-recognition domain of MutY in lesion-scanning.