Dhiraj Srivastava

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2013-2016 University of Iowa, Iowa City, IA 
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"Dhiraj Srivastava"
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Publications

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Nandi S, Razzaghi M, Srivastava D, et al. (2020) Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation. The Journal of Biological Chemistry. 295: 17425-17440
Nandi S, Razzaghi M, Srivastava D, et al. (2020) Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation. The Journal of Biological Chemistry
Srivastava D, Nandi S, Dey M. (2019) Mechanistic and Structural Insights into Cysteine-Mediated Inhibition of Pyruvate Kinase Muscle Isoform 2. Biochemistry
Srivastava D, Razzaghi M, Henzl MT, et al. (2017) Structural Investigation of a Dimeric Variant of Pyruvate Kinase Muscle Isoform 2. Biochemistry
Pemberton TA, Srivastava D, Sanyal N, et al. (2014) Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. Biochemistry. 53: 1350-9
Luo M, Arentson BW, Srivastava D, et al. (2012) Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release. Biochemistry. 51: 10099-108
Pemberton TA, Still BR, Christensen EM, et al. (2012) Proline: Mother Nature's cryoprotectant applied to protein crystallography. Acta Crystallographica. Section D, Biological Crystallography. 68: 1010-8
Srivastava D, Singh RK, Moxley MA, et al. (2012) The three-dimensional structural basis of type II hyperprolinemia. Journal of Molecular Biology. 420: 176-89
Srivastava D, Schuermann JP, White TA, et al. (2010) Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum. Proceedings of the National Academy of Sciences of the United States of America. 107: 2878-83
Srivastava D, Zhu W, Johnson WH, et al. (2010) The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction. Biochemistry. 49: 560-9
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