Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
5R01CA064159-03
Application #
2106453
Study Section
Medical Biochemistry Study Section (MEDB)
Project Start
1994-09-01
Project End
1999-06-30
Budget Start
1996-07-01
Budget End
1997-06-30
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost
Name
University of Michigan Ann Arbor
Department
Biochemistry
Type
Schools of Medicine
DUNS #
791277940
City
Ann Arbor
State
MI
Country
United States
Zip Code
48109
Sanker, S; Campbell, H A; Kent, C (2001) Negative cooperativity of substrate binding but not enzyme activity in wild-type and mutant forms of CTP:glycerol-3-phosphate cytidylyltransferase. J Biol Chem 276:37922-8
Friesen, J A; Park, Y S; Kent, C (2001) Purification and kinetic characterization of CTP:phosphocholine cytidylyltransferase from Saccharomyces cerevisiae. Protein Expr Purif 21:141-8
Friesen, J A; Liu, M F; Kent, C (2001) Cloning and characterization of a lipid-activated CTP:phosphocholine cytidylyltransferase from Caenorhabditis elegans: identification of a 21-residue segment critical for lipid activation. Biochim Biophys Acta 1533:86-98
Weber, C H; Park, Y S; Sanker, S et al. (1999) A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from bacillus subtilis. Structure 7:1113-24
Friesen, J A; Campbell, H A; Kent, C (1999) Enzymatic and cellular characterization of a catalytic fragment of CTP:phosphocholine cytidylyltransferase alpha. J Biol Chem 274:13384-9
Park, Y S; Gee, P; Sanker, S et al. (1997) Identification of functional conserved residues of CTP:glycerol-3-phosphate cytidylyltransferase. Role of histidines in the conserved HXGH in catalysis. J Biol Chem 272:15161-6
Wang, Y; Kent, C (1995) Identification of an inhibitory domain of CTP:phosphocholine cytidylyltransferase. J Biol Chem 270:18948-52
Wang, Y; Kent, C (1995) Effects of altered phosphorylation sites on the properties of CTP:phosphocholine cytidylyltransferase. J Biol Chem 270:17843-9