R. Datta

发表

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.

R. Balusu, A. Majumdar, B. Datta, 2004, Biochemistry.

The N-Terminal Acidic Residue-Rich Domain and Lysine-Rich Domains I and II of P67 are Required for Stable Expression of Focal Adhesion Kinase (FAK)

B. Datta, R. Datta, Rekha Datta, 2016 .

P 67 is involved in the regulation of cytoskeleton dynamics by modulating the expression and activity of Pak 1 in differentiated C 2 C 12 myoblasts

B. Datta, R. Datta, Rekha Datta, 2016 .

Analysis of P67 Expression in Different Mouse Tissues

B. Datta, R. Datta, 2016 .

Phosphorylation of Eukaryotic Initiation Factor 2α During Differentiation of Mouse Myoblasts into Myotubes is Mediated by an unknown Kinase

B. Datta, R. Datta, 2014 .

Autoproteolysis of rat p67 generates several peptide fragments: the N-terminal fragment, p26, is required for the protection of eIF2alpha from phosphorylation.

Arnab Ghosh, A. Majumdar, B. Datta, 2007, Biochemistry.

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, A. Majumdar, B. Datta, 2006, Experimental cell research.

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.

Arnab Ghosh, A. Majumdar, B. Datta, 2005, Experimental cell research.

Eukaryotic initiation factor 2-associated glycoprotein, p67, shows differential effects on the activity of certain kinases during serum-starved conditions.

Arnab Ghosh, A. Majumdar, B. Datta, 2004, Archives of biochemistry and biophysics.

Negative regulation of the protection of eIF2alpha phosphorylation activity by a unique acidic domain present at the N-terminus of p67.

R. Tammali, B. Datta, R. Datta, 2003, Experimental cell research.

Expression and activity of p67 are induced during heat shock.

N. Gupta, B. Datta, M. Chatterjee, 1998, Biochemical and biophysical research communications.

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.

B. Datta, R. Datta, 2003, Archives of biochemistry and biophysics.

A glycosylation site, 60SGTS63, of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2alpha.

Arnab Ghosh, Arnab Ghosh, P. Choudhury, 2003, Biochemistry.

The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2alpha from phosphorylation by kinases.

Arnab Ghosh, A. Majumdar, B. Datta, 2006, Archives of biochemistry and biophysics.

Increased phosphorylation of eukaryotic initiation factor 2alpha at the G2/M boundary in human osteosarcoma cells correlates with deglycosylation of p67 and a decreased rate of protein synthesis.

S. Mukherjee, Z. Zhang, B. Datta, 1999, Experimental cell research.

Induction of apoptosis due to lowering the level of eukaryotic initiation factor 2-associated protein, p67, from mammalian cells by antisense approach.

B. Datta, R. Datta, Rekha Datta, 1999, Experimental cell research.

Protection of translation initiation factor eIF2 phosphorylation correlates with eIF2-associated glycoprotein p67 levels and requires the lysine-rich domain I of p67.

Y. Zhou, P. Choudhury, B. Datta, 2001, Biochimie.

Phosphorylation of Eukaryotic Initiation Factor 2α During Differentiation of Mouse Myoblasts into Myotubes is Mediated by an unknown Kinase

B. Datta, R. Datta, Rekha Datta, 2014 .