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A chemical switch for inhibitor-sensitive alleles of any protein kinase
A chemical genetic strategy for sensitizing protein kinases to cell-permeable molecules that do not inhibit wild-type kinases is described, allowing for rapid functional characterization of members of this important gene family. Expand
Metformin suppresses gluconeogenesis by inhibiting mitochondrial glycerophosphate dehydrogenase
It is shown that metformin non-competitively inhibits the redox shuttle enzyme mitochondrial glycerophosphate dehydrogenase, resulting in an altered hepatocellular redox state, reduced conversion of lactate and glycerol to glucose, and decreased hepatic gluconeogenesis. Expand
Identifying the proteins to which small-molecule probes and drugs bind in cells
- S. Ong, M. Schenone, +14 authors S. Carr
- Biology, Medicine
- Proceedings of the National Academy of Sciences
- 24 March 2009
A powerful method combining quantitative proteomics (SILAC) with affinity enrichment is described to provide unbiased, robust and comprehensive identification of the proteins that bind to small-molecule probes and drugs. Expand
An aminoacyl-tRNA synthetase that specifically activates pyrrolysine.
- C. Polycarpo, A. Ambrogelly, +5 authors D. Söll
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 24 August 2004
In vitro data suggest that Methanosarcina cells have two pathways for acylating the suppressor tRNA(Pyl), which would ensure efficient translation of the in-frame UAG codon in case of pyrrolysine deficiency and safeguard the biosynthesis of the proteins whose genes contain this special codon. Expand
Autoregulation of Cell-specific MAP Kinase Control of the Tryptophan Hydroxylase Promoter*
Using the serotonergic neuron-like CA77 cell line, it is demonstrated that treatment with a 5-hydroxytryptamine autoreceptor agonist can lower TPH mRNA levels and promoter activity and suggest a model for the autoregulation of serotonin biosynthesis by repression of MAP kinase stimulation of the TPH promoter. Expand
Detoxication of cyanide by cystine.
Radioactivity measurements showed that the iminothiazolidinecarboxylic acid was produced from cystine, while the thiocyanate chiefly was formed from other sources of sulfur, which constitutes an independent pathway for detoxi- cabion of cyanide. Expand
The cystathionase-rhodanese system.
Cystathionase and rhodanese have been combined to form a coupled enzyme system which is capable of utilizing cysteine sulfur for transsulfuration and utilizes thiocystine as a substrate more efficiently than it does thiosulfate. Expand
The metabolism of thiocyanate in the rat and its inhibition by propylthiouracil.
Their results could not be taken as unequivocal evidence for the metabolism of thiocyanate by the body because, as the authors have observed, thiOCyanate breaks down spontaneously in aqueous solution to yield sulfate, but the study did indicate that the processes which might occur in biological systems would involve rather small amounts ofThiocianate ion. Expand
Pyrrolysine analogues as substrates for pyrrolysyl‐tRNA synthetase
- C. Polycarpo, S. Herring, A. Bérubé, J. L. Wood, D. Söll, A. Ambrogelly
- Biology, Medicine
- FEBS letters
- 11 December 2006
In vitro aminoacylation of tRNAPyl by PylRS with two Pyl analogues is reported with the formation of active β‐galactosidase shows that a specialized mRNA motif is not essential for stop‐codon recoding, unlike for selenocysteine incorporation. Expand
Labeled sulfur uptake by thyroids of rats with low plasma thiocyanate levels.
It has been observed that raising the iodide level of the plasma obscures the normal thyroid-serum iodine gradient, since the capacity of the gland to absorb iodide is limited, and the thyroid might be similarly limited in its ability to absorb thiocyanate. Expand