Bansidhar Datta

Summary

Affiliation: Kent State University
Country: USA

Publications

  1. doi request reprint Roles of P67/MetAP2 as a tumor suppressor
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Biochim Biophys Acta 1796:281-92. 2009
  2. ncbi request reprint 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
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, United States
    Exp Cell Res 303:174-82. 2005
  3. ncbi request reprint Mutation at the acidic residue-rich domain of eukaryotic initiation factor 2 (eIF2alpha)-associated glycoprotein p67 increases the protection of eIF2alpha phosphorylation during heat shock
    Bansidhar Datta
    Department of Chemistry, Kent State University, OH 44242, USA
    Arch Biochem Biophys 413:116-22. 2003
  4. ncbi request reprint Eukaryotic initiation factor 2-associated glycoprotein, p67, shows differential effects on the activity of certain kinases during serum-starved conditions
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Arch Biochem Biophys 427:68-78. 2004
  5. ncbi request reprint 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
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, Ohio 44242, USA
    Biochemistry 43:14821-31. 2004
  6. ncbi request reprint The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Arch Biochem Biophys 452:138-48. 2006
  7. ncbi request reprint Autoproteolysis of rat p67 generates several peptide fragments: the N-terminal fragment, p26, is required for the protection of eIF2alpha from phosphorylation
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, Ohio 44242, USA
    Biochemistry 46:3465-75. 2007
  8. ncbi request reprint A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha
    Rekha Datta
    Department of Chemistry, Kent State University, Kent, Ohio 44242, USA
    Biochemistry 42:5453-60. 2003
  9. ncbi request reprint Negative regulation of the protection of eIF2alpha phosphorylation activity by a unique acidic domain present at the N-terminus of p67
    Rekha Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Exp Cell Res 283:237-46. 2003
  10. doi request reprint p67/MetAP2 suppresses K-RasV12-mediated transformation of NIH3T3 mouse fibroblasts in culture and in athymic mice
    Avijit Majumdar
    School of Biomedical Sciences, Kent State University, Kent, Ohio 44242, United States
    Biochemistry 49:10146-57. 2010

Research Grants

  1. PROTEIN SYNTHESIS INITIATION IN ANIMAL CELLS
    Bansidhar Datta; Fiscal Year: 2002

Collaborators

  • Rekha Datta
  • Arnab Ghosh
  • Avijit Majumdar
  • Bethany C Prudner
  • Samit Datta
  • Mahasweta Bhattacharya
  • Ravinder Tammali
  • Papiya Choudhury

Detail Information

Publications11

  1. doi request reprint Roles of P67/MetAP2 as a tumor suppressor
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Biochim Biophys Acta 1796:281-92. 2009
    ..In this article, roles of p67/MetAP2 in the suppression of cancer development are also discussed...
  2. ncbi request reprint 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
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, United States
    Exp Cell Res 303:174-82. 2005
    ..p67 binds to ERK2 and inhibits its activity in vitro. Taken together, these results suggest that the stability of p67 increases during myotube formation while inhibiting the phosphorylation of ERKs 1 and 2...
  3. ncbi request reprint Mutation at the acidic residue-rich domain of eukaryotic initiation factor 2 (eIF2alpha)-associated glycoprotein p67 increases the protection of eIF2alpha phosphorylation during heat shock
    Bansidhar Datta
    Department of Chemistry, Kent State University, OH 44242, USA
    Arch Biochem Biophys 413:116-22. 2003
    ..Taken together, these results suggest that the lysine-rich domains and conserved amino acid residues of p67 are involved in the regulation of eIF2alpha phosphorylation during heat shock...
  4. ncbi request reprint Eukaryotic initiation factor 2-associated glycoprotein, p67, shows differential effects on the activity of certain kinases during serum-starved conditions
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Arch Biochem Biophys 427:68-78. 2004
    ..Altogether, our data provide evidence to suggest that p67 modulates the expression and activity of certain eIF2alpha-specific kinases...
  5. ncbi request reprint 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
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, Ohio 44242, USA
    Biochemistry 43:14821-31. 2004
    ..These results suggest that fumagillin increases the stability of p67 and its affinity to ERKs 1 and 2 and causes the inhibition of the phosphorylation of ERKs 1 and 2...
  6. ncbi request reprint The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Arch Biochem Biophys 452:138-48. 2006
    ..Altogether, our data demonstrate that the increased binding of the D6/2 mutant with the subunits of eIF2 may be in part the cause for its high POEP activity...
  7. ncbi request reprint Autoproteolysis of rat p67 generates several peptide fragments: the N-terminal fragment, p26, is required for the protection of eIF2alpha from phosphorylation
    Bansidhar Datta
    Department of Chemistry, Kent State University, Kent, Ohio 44242, USA
    Biochemistry 46:3465-75. 2007
    ..Altogether, our data provide evidence that rat p67 has autoproteolytic activity that generates p26, which is required to block eIF2alpha from phosphorylation...
  8. ncbi request reprint A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha
    Rekha Datta
    Department of Chemistry, Kent State University, Kent, Ohio 44242, USA
    Biochemistry 42:5453-60. 2003
    ..These results suggest that glycosylation within the (60)SGTS(63) sequence of p67 plays an important role in its stability and thus its regulation of protein synthesis by modulating the phosphorylation of the alpha-subunit of eIF2...
  9. ncbi request reprint Negative regulation of the protection of eIF2alpha phosphorylation activity by a unique acidic domain present at the N-terminus of p67
    Rekha Datta
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Exp Cell Res 283:237-46. 2003
    ..Taken together, these data suggest that the acidic residue-rich domain present at the N-terminus of p67 may have a negative role in POEP activity...
  10. doi request reprint p67/MetAP2 suppresses K-RasV12-mediated transformation of NIH3T3 mouse fibroblasts in culture and in athymic mice
    Avijit Majumdar
    School of Biomedical Sciences, Kent State University, Kent, Ohio 44242, United States
    Biochemistry 49:10146-57. 2010
    ....
  11. ncbi request reprint 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
    Arnab Ghosh
    Department of Chemistry, Kent State University, Kent, OH 44242, USA
    Exp Cell Res 312:3184-203. 2006
    ..Altogether, our data provide genetic evidence for the interaction between p67 and eIF2gamma and that this interaction modulates the phosphorylation of eIF2alpha...

Research Grants4

  1. PROTEIN SYNTHESIS INITIATION IN ANIMAL CELLS
    Bansidhar Datta; Fiscal Year: 2002
    ..This research is expected to provide valuable information regarding the mechanism of protein synthesis initiation in normal, cancerous, and virus- infected animal cells. ..