Bansidhar Datta
Affiliations: | Kent State University, Kent, OH, United States |
Area:
Oncology, Cell Biology, BiochemistryGoogle:
"Bansidhar Datta"Mean distance: (not calculated yet)
Children
Sign in to add trainee| Arnab Ghosh | grad student | 2006 | Kent State |
| Avijit Majumdar | grad student | 2008 | Kent State |
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Publications
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| Majumdar A, Ghosh A, Datta S, et al. (2010) p67/MetAP2 suppresses K-RasV12-mediated transformation of NIH3T3 mouse fibroblasts in culture and in athymic mice. Biochemistry. 49: 10146-57 |
| Datta B. (2009) Roles of P67/MetAP2 as a tumor suppressor. Biochimica Et Biophysica Acta. 1796: 281-92 |
| Datta B, Ghosh A, Majumdar A, et al. (2007) Autoproteolysis of rat p67 generates several peptide fragments: the N-terminal fragment, p26, is required for the protection of eIF2alpha from phosphorylation. Biochemistry. 46: 3465-75 |
| Ghosh A, Datta R, Majumdar A, et al. (2006) The N-terminal lysine residue-rich domain II and the 340-430 amino acid segment of eukaryotic initiation factor 2-associated glycoprotein p67 are the binding sites for the gamma-subunit of eIF2. Experimental Cell Research. 312: 3184-203 |
| Datta B, Datta R, Ghosh A, et al. (2006) The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases. Archives of Biochemistry and Biophysics. 452: 138-48 |
| Srinivasan VB, Virk RK, Kaundal A, et al. (2006) Mechanism of drug resistance in clonally related clinical isolates of Vibrio fluvialis isolated in Kolkata, India. Antimicrobial Agents and Chemotherapy. 50: 2428-32 |
| Datta B, Datta R, Majumdar A, et al. (2005) The stability of eukaryotic initiation factor 2-associated glycoprotein, p67, increases during skeletal muscle differentiation and that inhibits the phosphorylation of extracellular signal-regulated kinases 1 and 2. Experimental Cell Research. 303: 174-82 |
| Datta B, Majumdar A, Datta R, et al. (2004) Treatment of cells with the angiogenic inhibitor fumagillin results in increased stability of eukaryotic initiation factor 2-associated glycoprotein, p67, and reduced phosphorylation of extracellular signal-regulated kinases. Biochemistry. 43: 14821-31 |
| Datta B, Datta R, Ghosh A, et al. (2004) Eukaryotic initiation factor 2-associated glycoprotein, p67, shows differential effects on the activity of certain kinases during serum-starved conditions. Archives of Biochemistry and Biophysics. 427: 68-78 |
| Datta R, Choudhury P, Ghosh A, et al. (2003) A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha. Biochemistry. 42: 5453-60 |