B. Datta

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The phylogenetically invariant ACAGAGA and AGC sequences of U6 small nuclear RNA are more tolerant of mutation in human cells than in Saccharomyces cerevisiae

A. Weiner, B. Datta, 1993, Molecular and cellular biology.

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.

Roles of a 67-kDa polypeptide in reversal of protein synthesis inhibition in heme-deficient reticulocyte lysate.

N. Gupta, A. Roy, D. Chakrabarti, 1988, Proceedings of the National Academy of Sciences of the United States of America.

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, 2016 .

P67 Shows Differential Effects in Proteolysis and Maturation of Cell Cycle Regulatory Proteins, Cyclins and Cdks

B. Datta, S. Datta, 2016 .

p67/MetAP2 suppresses K-RasV12-mediated transformation of NIH3T3 mouse fibroblasts in culture and in athymic mice.

Arnab Ghosh, A. Majumdar, B. Datta, 2010, Biochemistry.

Protein Synthesis Initiation in Animal Cells

N. Gupta, A. Roy, B. Datta, 1993 .

Natural mRNA is required for directing Met-tRNA(f) binding to 40S ribosomal subunits in animal cells: involvement of Co-eIF-2A in natural mRNA-directed initiation complex formation.

D. Chakrabarti, N. Gupta, A. Roy, 1988, Biochemistry.

Characteristics of the eukaryotic initiation factor 2 associated 67-kDa polypeptide.

A. Bose, D. Saha, T. Kinzy, 1993, Biochemistry.

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, 2016 .

Roles of P67/MetAP2 as a tumor suppressor.

B. Datta, 2009, Biochimica et biophysica acta.

Intra-molecular and Intermolecular Proteolysis Activity of p67

B. Datta, 2016 .

Analysis of P67 Expression in Different Mouse Tissues

B. Datta, R. Datta, 2016 .

Constitutive Expression of P67 Increases cPKCalpha Level in C2C12 Myoblasts and Decreases in Myotubes

B. Datta, S. Datta, 2016 .

Differential Expression of MARCKS in C2C12 Myoblasts and Myotubes Constitutively Expressing P67

B. Datta, S. Datta, 2016 .

Involvement of p67 in Actin Cytoskeleton Dynamics, Survival, Migration, and Motility during Differentiation of C2C12 Myoblasts into Multinucleated Myotubes

B. 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.

Nanoparticles of Metal-Organic Cages Overcoming Drug Resistance in Ovarian Cancer

B. Datta, He Liu, Amarasooriya M. D. S. Jayawardhana, 2019, Front. Chem..

MAPs and POEP of the roads from prokaryotic to eukaryotic kingdoms.

B. Datta, 2000, Biochimie.

Expression and activity of p67 are induced during heat shock.

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

ThePhylogenetically Invariant ACAGAGA andAGC Sequences ofU6SmallNuclear RNA AreMoreTolerant of Mutation inHumanCells thaninSaccharomyces cerevisiae

B. Datta, Biophysics andBiochemistry, 1993 .

p202, an Interferon-inducible Modulator of Transcription, Inhibits Transcriptional Activation by the p53 Tumor Suppressor Protein, and a Segment from the p53-binding Protein 1 That Binds to p202 Overcomes This Inhibition*

P. Lengyel, D. Choubey, G. Nallur, 1996, The Journal of Biological Chemistry.

Genetic evidence for base pairing between U2 and U6 snRNA in mammalian mRNA splicing

A. Weiner, B. Datta, 1991, Nature.

Increase in p202 Expression during Skeletal Muscle Differentiation: Inhibition of MyoD Protein Expression and Activity by p202

P. Lengyel, S. Burma, W. Min, 1998, Molecular and Cellular Biology.

Increase in p 202 Expression during Skeletal Muscle Differentiation : Inhibition of MyoD Protein Expression and Activity by p 202 †

P. Lengyel, S. Burma, W. Min, 1998 .

Inhibition of E2F‐mediated transcription by p202.

P. Lengyel, D. Choubey, S. Li, 1996, The EMBO journal.

Terminal Differentiation of Myogenic Cells Requires Stable Form of Tumor Suppressor Protein , P 53 Bansidhar Datta

B. Datta, 2016 .

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.

The interferon-activatable gene 200 cluster: from structure toward function

P. Lengyel, D. Choubey, Shyr-Jiann Li, 1995 .

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.

The eukaryotic initiation factor 2-associated 67-kDa polypeptide (p67) plays a critical role in regulation of protein synthesis initiation in animal cells.

N. Gupta, A. Chattopadhyay, A. Chakraborty, 1992, Proceedings of the National Academy of Sciences of the United States of America.

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.

Glycosylation of eukaryotic peptide chain initiation factor 2 (eIF-2)-associated 67-kDa polypeptide (p67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2 alpha-subunit.

D. Chakrabarti, N. Gupta, B. Datta, 1989, The Journal of biological chemistry.

Peptide Chain Initiation in Animal Cells: Mechanism and Regulation

N. Gupta, A. Roy, B. Datta, 1990 .

Protein synthesis in rabbit reticulocytes. A study of the mechanism of Co-eIF-2 action.

D. Chakrabarti, N. Gupta, B. Datta, 1985, The Journal of biological chemistry.

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.

Cross-linking of U1 snRNA using nitrogen mustard. Evidence for higher order structure.

A. Weiner, B. Datta, 1992, The Journal of biological chemistry.

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

B. Datta, R. Datta, 2014 .