Agency
National Institute of Health (NIH)
Institute
National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)
Type
Research Project (R01)
Project #
5R01DK032953-15
Application #
2138934
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1986-09-01
Project End
1997-03-31
Budget Start
1996-04-01
Budget End
1997-03-31
Support Year
15
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Tennessee Health Science Center
Department
Biochemistry
Type
Schools of Medicine
DUNS #
941884009
City
Memphis
State
TN
Country
United States
Zip Code
38163
Thompson, Jackie A; Carlson, Gerald M (2017) The regulatory ? and ? subunits of phosphorylase kinase directly interact with its substrate, glycogen phosphorylase. Biochem Biophys Res Commun 482:221-225
Carlson, Gerald M; Fenton, Aron W (2016) What Mutagenesis Can and Cannot Reveal About Allostery. Biophys J 110:1912-23
Herrera, Julio E; Thompson, Jackie A; Rimmer, Mary Ashley et al. (2015) Activation of Phosphorylase Kinase by Physiological Temperature. Biochemistry 54:7524-30
Thompson, Jackie A; Nadeau, Owen W; Carlson, Gerald M (2015) A model for activation of the hexadecameric phosphorylase kinase complex deduced from zero-length oxidative crosslinking. Protein Sci 24:1956-63
Rimmer, Mary Ashley; Artigues, Antonio; Nadeau, Owen W et al. (2015) Mass Spectrometric Analysis of Surface-Exposed Regions in the Hexadecameric Phosphorylase Kinase Complex. Biochemistry 54:6887-95
Liu, Weiya; Nadeau, Owen W; Sage, Jessica et al. (2013) Physicochemical changes in phosphorylase kinase induced by its cationic activator Mg(2+). Protein Sci 22:444-54
Nadeau, Owen W; Lane, Laura A; Xu, Dong et al. (2012) Structure and location of the regulatory ? subunits in the (????)4 phosphorylase kinase complex. J Biol Chem 287:36651-61
Nadeau, Owen W; Carlson, Gerald M (2012) A review of methods used for identifying structural changes in a large protein complex. Methods Mol Biol 796:117-32
Lane, Laura A; Nadeau, Owen W; Carlson, Gerald M et al. (2012) Mass spectrometry reveals differences in stability and subunit interactions between activated and nonactivated conformers of the (????)4 phosphorylase kinase complex. Mol Cell Proteomics 11:1768-76
Nadeau, Owen W; Liu, Weiya; Boulatnikov, Igor G et al. (2010) The glucoamylase inhibitor acarbose is a direct activator of phosphorylase kinase. Biochemistry 49:6505-7

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