Miljan Simonovic, Ph.D.

2002 University of Illinois at Chicago, Health Sciences Center 
"Miljan Simonovic"
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Peter G. W. Gettins grad student 2002 University of Illinois at Chicago, Health Sciences Center
 (Crystallographic analysis of serpins and bacterial response regulator.)
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Puppala AK, French RL, Matthies D, et al. (2016) Structural basis for early-onset neurological disorders caused by mutations in human selenocysteine synthase. Scientific Reports. 6: 32563
Ognjenović J, Wu J, Matthies D, et al. (2016) The crystal structure of human GlnRS provides basis for the development of neurological disorders. Nucleic Acids Research
Holman KM, Wu J, Ling J, et al. (2015) The crystal structure of yeast mitochondrial ThrRS in complex with the canonical threonine tRNA. Nucleic Acids Research
Gagné D, French RL, Narayanan C, et al. (2015) Perturbation of the Conformational Dynamics of an Active-Site Loop Alters Enzyme Activity. Structure (London, England : 1993). 23: 2256-2266
Anttonen AK, Hilander T, Linnankivi T, et al. (2015) Selenoprotein biosynthesis defect causes progressive encephalopathy with elevated lactate. Neurology. 85: 306-15
French RL, Gupta N, Copeland PR, et al. (2014) Structural asymmetry of the terminal catalytic complex in selenocysteine synthesis. The Journal of Biological Chemistry. 289: 28783-94
Ling J, Peterson KM, Simonovic I, et al. (2012) The mechanism of pre-transfer editing in yeast mitochondrial threonyl-tRNA synthetase. The Journal of Biological Chemistry. 287: 28518-25
Ling J, Peterson KM, Simonović I, et al. (2012) Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment. Proceedings of the National Academy of Sciences of the United States of America. 109: 3281-6
Su D, Lieberman A, Lang BF, et al. (2011) An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine. Nucleic Acids Research. 39: 4866-74
Palioura S, Herkel J, Simonović M, et al. (2010) Human SepSecS or SLA/LP: selenocysteine formation and autoimmune hepatitis. Biological Chemistry. 391: 771-6
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