@inbook{10896, abstract = {Under physiological conditions the brain, via the purine salvage pathway, reuses the preformed purine bases hypoxanthine, derived from ATP degradation, and adenine (Ade), derived from polyamine synthesis, to restore its ATP pool. However, the massive degradation of ATP during ischemia, although providing valuable neuroprotective adenosine, results in the accumulation and loss of diffusible purine metabolites and thereby leads to a protracted reduction in the post-ischemic ATP pool size. In vivo, this may both limit the ability to deploy ATP-dependent reparative mechanisms and reduce the subsequent availability of adenosine, whilst in brain slices results in tissue with substantially lower levels of ATP than in vivo. In the present review, we describe the mechanisms by which brain tissue replenishes its ATP, how this can be improved with the clinically tolerated chemicals D-ribose and adenine, and the functional, and potential therapeutic, implications of doing so.}, author = {zur Nedden, Stephanie and Doney, Alexander S. and Frenguelli, Bruno G.}, booktitle = {Adenosine}, editor = {Masino, Susan and Boison, Detlev}, isbn = {9781461439028}, pages = {109--129}, publisher = {Springer}, title = {{The double-edged sword: Gaining Adenosine at the expense of ATP. How to balance the books}}, doi = {10.1007/978-1-4614-3903-5_6}, year = {2012}, } @article{3405, abstract = {Glutamate is the major excitatory neurotransmitter in the mammalian central nervous system and gates non-selective cation channels. The origins of glutamate receptors are not well understood as they differ structurally and functionally from simple bacterial ligand-gated ion channels. Here we report the discovery of an ionotropic glutamate receptor that combines the typical eukaryotic domain architecture with the 'TXVGYG' signature sequence of the selectivity filter found in K+ channels. This receptor exhibits functional properties intermediate between bacterial and eukaryotic glutamate-gated ion channels, suggesting a link in the evolution of ionotropic glutamate receptors.}, author = {Janovjak, Harald L and Sandoz, Guillaume and Isacoff, Ehud}, journal = {Nature Communications}, number = {232}, pages = {1 -- 6}, publisher = {Nature Publishing Group}, title = {{Modern ionotropic glutamate receptor with a K+ selectivity signature sequence}}, doi = {10.1038/ncomms1231}, volume = {2}, year = {2011}, }