Year |
Citation |
Score |
2015 |
Menon VK, Gottumukkala RS, Chen J, Su X, Mistry N, Majumdar A, Shin J, Li S, Shetty K, Wu X, Weston B, Miller E, Stroehlein JR, Davila ML, Shafi MA, et al. Abstract 67: Genomic and mutational profiling of human colon adenomas reveals early driver mutations and a TGF-β-CEA regulated profile Cancer Research. 75: 67-67. DOI: 10.1158/1538-7445.Am2015-67 |
0.306 |
|
2014 |
Majumdar A, Chen J, Lin SH, Katz L, Raju GS, Shetty K, White J, Wu X, Rashid A, McMurray JS, Shaw KR, Su X, Weston B, Thirumurthi S, He AR, et al. Abstract 4703: Genome & exome analysis of early colon cancers reveals new targets Cancer Research. 74: 4703-4703. DOI: 10.1158/1538-7445.Am2014-4703 |
0.311 |
|
2013 |
Majumdar A, Li Y, Lin S, Mishra L. Abstract 4335: CEA: A therapeutic target for the treatment of advanced colorectal cancer. Cancer Research. 73: 4335-4335. DOI: 10.1158/1538-7445.Am2013-4335 |
0.308 |
|
2012 |
Li Y, Majumdar A, Lin S, Mishra L. Abstract 897: CEA induces colorectal cancer metastases by disrupting TGF-β signaling Cancer Research. 72: 897-897. DOI: 10.1158/1538-7445.Am2012-897 |
0.319 |
|
2011 |
Berry DC, Jin H, Majumdar A, Noy N. Signaling by vitamin A and retinol-binding protein regulates gene expression to inhibit insulin responses. Proceedings of the National Academy of Sciences of the United States of America. 108: 4340-5. PMID 21368206 DOI: 10.1073/Pnas.1011115108 |
0.344 |
|
2010 |
Majumdar A, Ghosh A, Datta S, Prudner BC, Datta B. p67/MetAP2 suppresses K-RasV12-mediated transformation of NIH3T3 mouse fibroblasts in culture and in athymic mice. Biochemistry. 49: 10146-57. PMID 21033716 DOI: 10.1021/Bi101225D |
0.737 |
|
2007 |
Datta B, Ghosh A, Majumdar A, Datta R. 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. PMID 17311411 DOI: 10.1021/Bi061838N |
0.75 |
|
2006 |
Ghosh A, Datta R, Majumdar A, Bhattacharya M, Datta B. 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. PMID 16857189 DOI: 10.1016/J.Yexcr.2006.03.034 |
0.737 |
|
2006 |
Datta B, Datta R, Ghosh A, Majumdar A. 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. PMID 16843428 DOI: 10.1016/J.Abb.2006.06.009 |
0.744 |
|
2005 |
Datta B, Datta R, Majumdar A, Ghosh A. 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. PMID 15572037 DOI: 10.1016/J.Yexcr.2004.09.018 |
0.758 |
|
2004 |
Datta B, Majumdar A, Datta R, Balusu R. 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. PMID 15544353 DOI: 10.1021/Bi049172P |
0.771 |
|
2004 |
Datta B, Datta R, Ghosh A, Majumdar A. 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. PMID 15178489 DOI: 10.1016/J.Abb.2004.04.002 |
0.762 |
|
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