@article{gieger_rassnick_siegel_proulx_bergman_anderson_ladue_smith_northrup_roberts_2008, title={Palliation of clinical signs in 48 dogs with nasal carcinomas treated with coarse-fraction radiation therapy}, volume={44}, ISSN={["1547-3317"]}, DOI={10.5326/0440116}, abstractNote={Data from 48 dogs with nasal carcinomas treated with palliative radiation therapy (PRT) were retrospectively reviewed. Factors potentially influencing resolution of clinical signs and survival after PRT were evaluated. Clinical signs completely resolved in 66% of dogs for a median of 120 days. The overall median survival time was 146 days. Duration of response to PRT was shorter in dogs that had clinical signs for <90 days before PRT. Survival times were shorter in dogs that had partial or no resolution of clinical signs after PRT than in dogs that had complete resolution of clinical signs.}, number={3}, journal={JOURNAL OF THE AMERICAN ANIMAL HOSPITAL ASSOCIATION}, author={Gieger, Tracy and Rassnick, Kenneth and Siegel, Sheri and Proulx, David and Bergman, Philip and Anderson, Christine and LaDue, Tracy and Smith, Annette and Northrup, Nicole and Roberts, Royce}, year={2008}, pages={116–123} }
 @article{anderson_tatchell_2001, title={Hyperactive glycogen synthase mutants of Saccharomyces cerevisiae suppress the glc7-1 protein phosphatase mutant}, volume={183}, ISSN={["1098-5530"]}, DOI={10.1128/JB.183.3.821-829.2001}, abstractNote={ABSTRACT
          
            A yeast
            glc7-1
            mutant expressing a variant of protein phosphatase type 1 fails to accumulate glycogen. This defect is associated with hyperphosphorylated and inactive glycogen synthase, consistent with Glc7p acting directly to dephosphorylate and activate glycogen synthase. To characterize the glycogen synthesis defect of this mutant in more detail, we isolated 26 pseudorevertants of the
            glc7-1
            mutant. All pseudoreversion events were due to missense mutations in
            GSY2
            , the gene encoding the major isoform of glycogen synthase. A majority of the mutations responsible for the suppression were in the 3′ end of the gene, corresponding to the phosphorylated COOH terminus of Gsy2p. Phosphorylation of the mutant proteins was reduced, suggesting that they are poor substrates for glycogen synthase kinases. Suppressor mutations outside this domain did not decrease the phosphorylation of the resulting proteins, indicating that these proteins are immune to the regulatory effects of phosphorylation. Since no growth defect has been observed for strains with altered glycogen levels, the relative levels of fitness of
            GSY2
            mutants that fail to accumulate glycogen and that hyperaccumulate glycogen were assayed by cocultivation experiments. A wild-type strain outcompeted both hypo- and hyperaccumulating strains, suggesting that glycogen levels contribute substantially to the fitness of yeast.
          }, number={3}, journal={JOURNAL OF BACTERIOLOGY}, author={Anderson, C and Tatchell, K}, year={2001}, month={Feb}, pages={821–829} }