Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM027904-18
Application #
2175029
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1990-08-01
Project End
1997-06-30
Budget Start
1996-04-01
Budget End
1997-06-30
Support Year
18
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Cytel Corporation
Department
Type
DUNS #
City
San Diego
State
CA
Country
United States
Zip Code
92121
Datta, A K; Chammas, R; Paulson, J C (2001) Conserved cysteines in the sialyltransferase sialylmotifs form an essential disulfide bond. J Biol Chem 276:15200-7
Datta, A K; Sinha, A; Paulson, J C (1998) Mutation of the sialyltransferase S-sialylmotif alters the kinetics of the donor and acceptor substrates. J Biol Chem 273:9608-14
Sjoberg, E R; Kitagawa, H; Glushka, J et al. (1996) Molecular cloning of a developmentally regulated N-acetylgalactosamine alpha2,6-sialyltransferase specific for sialylated glycoconjugates. J Biol Chem 271:7450-9
Kitagawa, H; Mattei, M G; Paulson, J C (1996) Genomic organization and chromosomal mapping of the Gal beta 1,3GalNAc/Gal beta 1,4GlcNAc alpha 2,3-sialyltransferase. J Biol Chem 271:931-8
Datta, A K (1995) Efficient amplification using 'megaprimer' by asymmetric polymerase chain reaction. Nucleic Acids Res 23:4530-1
Datta, A K; Paulson, J C (1995) The sialyltransferase ""sialylmotif"" participates in binding the donor substrate CMP-NeuAc. J Biol Chem 270:1497-500
Williams, M A; Kitagawa, H; Datta, A K et al. (1995) Large-scale expression of recombinant sialyltransferases and comparison of their kinetic properties with native enzymes. Glycoconj J 12:755-61
Weinstein, J; Jacobsen, F W; Hsu-Chen, J et al. (1994) A novel mammalian protein, p55CDC, present in dividing cells is associated with protein kinase activity and has homology to the Saccharomyces cerevisiae cell division cycle proteins Cdc20 and Cdc4. Mol Cell Biol 14:3350-63
Kitagawa, H; Paulson, J C (1994) Cloning of a novel alpha 2,3-sialyltransferase that sialylates glycoprotein and glycolipid carbohydrate groups. J Biol Chem 269:1394-401
Kitagawa, H; Paulson, J C (1994) Differential expression of five sialyltransferase genes in human tissues. J Biol Chem 269:17872-8

Showing the most recent 10 out of 38 publications