Mom Das, Ph.D. - Publications
Affiliations: | 2012 | Biochemistry | Ohio State University, Columbus, Columbus, OH |
Area:
Substrate Recognition by Aminoacyl-tRNA Synthetases, RNA-Protein Interactions in HIVYear | Citation | Score | |||
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2014 | Das M, Vargas-Rodriguez O, Goto Y, Suga H, Musier-Forsyth K. Distinct tRNA recognition strategies used by a homologous family of editing domains prevent mistranslation. Nucleic Acids Research. 42: 3943-53. PMID 24371276 DOI: 10.1093/Nar/Gkt1332 | 0.63 | |||
2013 | Kumar S, Das M, Hadad CM, Musier-Forsyth K. Aminoacyl-tRNA substrate and enzyme backbone atoms contribute to translational quality control by YbaK. The Journal of Physical Chemistry. B. 117: 4521-7. PMID 23185990 DOI: 10.1021/Jp308628Y | 0.656 | |||
2012 | Kumar S, Das M, Hadad CM, Musier-Forsyth K. Substrate and enzyme functional groups contribute to translational quality control by bacterial prolyl-tRNA synthetase. The Journal of Physical Chemistry. B. 116: 6991-9. PMID 22458656 DOI: 10.1021/Jp300845H | 0.681 | |||
2012 | Kumar S, Das M, Hadad CM, Musier-Forsyth K. Substrate specificity of bacterial prolyl-tRNA synthetase editing domain is controlled by a tunable hydrophobic pocket. The Journal of Biological Chemistry. 287: 3175-84. PMID 22128149 DOI: 10.1074/Jbc.M111.313619 | 0.701 | |||
2011 | So BR, An S, Kumar S, Das M, Turner DA, Hadad CM, Musier-Forsyth K. Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons. The Journal of Biological Chemistry. 286: 31810-20. PMID 21768119 DOI: 10.1074/Jbc.M111.232611 | 0.648 | |||
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