Sanjeeva J. Wijeyesakere, Ph.D.

Affiliations: 
2009 University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
Toxicology
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"Sanjeeva Wijeyesakere"
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Parents

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Rudy J. Richardson grad student 2009 University of Michigan
 (Enzyme aging: Structural insights from NTE and patatin.)
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Publications

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Richardson RJ, Fink JK, Glynn P, et al. (2020) Neuropathy target esterase (NTE/PNPLA6) and organophosphorus compound-induced delayed neurotoxicity (OPIDN). Advances in Neurotoxicology. 4: 1-78
Wijeyesakere SJ, Gagnon JK, Arora K, et al. (2015) Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP. Proceedings of the National Academy of Sciences of the United States of America. 112: E5608-17
Richardson RJ, Mark Worden R, Wijeyesakere SJ, et al. (2015) Neuropathy Target Esterase as a Biomarker and Biosensor of Delayed Neuropathic Agents Handbook of Toxicology of Chemical Warfare Agents: Second Edition. 935-952
Wijeyesakere SJ, Richardson RJ, Stuckey JA. (2014) Crystal structure of patatin-17 in complex with aged and non-aged organophosphorus compounds. Plos One. 9: e108245
Wijeyesakere SJ, Rizvi SM, Raghavan M. (2013) Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin. The Journal of Biological Chemistry. 288: 35104-16
Richardson RJ, Hein ND, Wijeyesakere SJ, et al. (2013) Neuropathy target esterase (NTE): overview and future. Chemico-Biological Interactions. 203: 238-44
Raghavan M, Wijeyesakere SJ, Peters LR, et al. (2013) Calreticulin in the immune system: ins and outs. Trends in Immunology. 34: 13-21
Wang Y, Liu X, Schneider B, et al. (2012) Mixed inhibition of adenosine deaminase activity by 1,3-dinitrobenzene: a model for understanding cell-selective neurotoxicity in chemically-induced energy deprivation syndromes in brain. Toxicological Sciences : An Official Journal of the Society of Toxicology. 125: 509-21
Wijeyesakere SJ, Gafni AA, Raghavan M. (2011) Calreticulin is a thermostable protein with distinct structural responses to different divalent cation environments. The Journal of Biological Chemistry. 286: 8771-85
Makhaeva GF, Aksinenko AY, Sokolov VB, et al. (2010) Kinetics and mechanism of inhibition of serine esterases by fluorinated aminophosphonates. Chemico-Biological Interactions. 187: 177-84
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