Natalia N Singh

PhD
Adjunct Associate Professor
Biomedical Sciences
515-294-2451
2008 Patterson Hall
ISU Directory Link
Education & Certifications  
  • PhD, Biochemistry, 1995, Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino, Russia
  • MSc, Bioengineering, 1988, Leningrad Institute of Technology, St. Petersburg, Russia
Teaching  
  • 2015-Present                       Adjunct Associate Professor, Department of Biomedical Sciences, College of Veterinary Medicine, Iowa State University, Ames, IA
  • 2007-2015                          Adjunct Assistant Professor, Department of Biomedical Sciences, College of Veterinary Medicine, Iowa State University, Ames, IA
  • 2006-2007                          Research Assistant Professor, Department of Medicine, University of Massachusetts Medical School, Worcester, MA

  • 2001-2006                          Instructor, Department of Medicine, University of Massachusetts Medical School, Worcester, MA

  • 2001-2001                          Post Doctoral Fellow, New England Medical Center, Boston, MA (with Dr. Elliot Androphy and Dr. Ravindra Singh)

  • 1998-2001                          Post Doctoral Fellow, Institute for Cellular and Molecular Biology, University of Texas at Austin, TX  (with Dr. Alan Lambowitz)

  • 1996-1998                          Post Doctoral Research Associate, Oregon State University, Corvallis, OR (with Dr. David Barnes)

Honors & Awards  
  • Graduated High School with Gold Medal
  • Graduated University with Distinction
  • Russian Academy of Sciences Fellowship for Postgraduate Research
Memberships  
  1. The RNA Society
  2. The American Society of Human Genetics
Selected Publications  

Peer Reviewd: 27 selected publications out of over 100.  

Link to PubMed

  1. Howell MD, Ottesen EW, Singh NN, Anderson RL, Singh RN. (2017) Gender-specific amelioration of SMA Phenotype upon disruption of a deep intronic structure by an oligonucleotide. Mol Ther. doi: 10.1016/j.ymthe.2017.03.036 Pubmed.
  2. Ilchinko, A.P., Vasilkova, N.N. and  Tikhonova, E.B. (1991). The effect of dissolved oxygen concentration in the medium on the dynamics of the activities of alcohol oxidase and NAD-dependent aldehyde dehydrogenase during adaptation of yeast Torulopsis candida to hexadecane. Mikrobiologia (Moscow) 60, 454-460.
  3. Ilchinko, A.P., Vasilkova, N.N. and   Matyashova, R.N. (1991). Changes in the activity of enzymes utilizing H2O2 under different conditions of yeast cultivation. Mikrobiologia (Moscow) 60, 55-64.
  4. Ilchinko, A.P., Morgunov, I.G., Honec, H., Mauersberger, S., Vasilkova, N.N. and Muller, H.G. (1994) Purification and properties of the alcohol oxidase from the yeast Yarrowia lipolytica H-222. Biochemistry (Moscow) 59, 969-974.
  5. Ilchinko, A.P., Vasilkova, N.N., Shishkanova, N.V. And Finogenova, T.V. (1994) Influence of the ratio of Zn and Fe ions on the acetate excretion and activity of NAD-dependent alcohol and aldehyde dehydrogenases in Torulopsis candida growing on ethanol. Mikrobiologia (Moscow) 63, 613-623.
  6. Ilchinko, A.P., Singh, N.N., Shishkanova, N.V. and Finogenova, T.V.  (1995) Influence of the ethanol concentration and the ratio of Zn and Fe ions on the respiratory chain functioning during the growth of yeast Torulopsis candida on ethanol. Mikrobiologia (Moscow) 65, 305-313.
  7. Ilchinko, A.P., Fausek E., Singh, N.N., Shishkanova, N.V. and Finogenova, T.V. (1995) Comparative study of the physiological and biochemical peculiarities of two Yarrowia lypolytica species during the growth on ethanol. Mikrobiologia (Moscow) 65, 189-196.
  8. Singh, N.N., Fischer, K., Hedstrom, O. and Barnes D.W. (2001). Fibroblast growth factor inhibits expression of neural markers in cultures of zebrafish early embryo cells. Marine Biotechnology 3, 27-35.
  9. Singh, N.N. and Lambowitz A.M. (2001). Interaction of a group II intron ribonucleoprotein endonuclease with its DNA target site investigated by DNA footprinting and modification interference. Journal of Molecular Biology 309, 361-386.
  10. Singh, N.N., Androphy E.J. and Singh R.N. (2004). An extended inhibitory context causes skipping of exon 7 of SMN2 in spinal muscular atrophy. Biophysical Biochemical Research Communication 315, 381-388.
  11. Singh, N.N., Androphy E.J. and Singh R.N. (2004). In vivo selection reveals features of combinatorial control that defines a critical exon in the spinal muscular atrophy genes. RNA 10, 1291-1305.
  12. Singh, N.N., Androphy E.J. and Singh R.N. (2004). The Regulation and Regulatory Activities of Alternative Splicing of the SMN gene. Critical Reviews in Eukaryotic Gene Expression 14, 271-285.
  13. *Singh, N.N., *Singh N.K., Androphy, E.J. and Singh, R.N. (2006) Splicing of a critical exon of human Survival Motor Neuron is regulated by a unique silencer element located in the last intron.  Molecular and Cellular Biology, 26, 1333-1346. (*Equal first authors)
  14. Singh, N.N*., Singh, R.N. and Androphy, E.J. (2007) Modulating role of a RNA structure in alternative splicing of a critical exon in the spinal muscular atrophy genes. Nucleic Acids Research, 35, 371-389. *Corresponding author.
  15. Singh, N.N., Shishimorova, M., Cao, L.C., Gangwani, L. and Singh R.N. (2009) A short antisence oligonucleotide masking a unique intronic motif prevents skipping of a critical exon in spinal muscular atrophy. RNA Biology, 6, 341-350.
  16. Singh, N.N., Hollinger, K., Bhattacharya, D. and Singh, R.N. (2010) An antisense microwalk reveals critical role of an intronic position linked to a unique long-distance interaction in pre-mRNA splicing. RNA, 16, 1167-1181.
  17. Singh, N.N.*, Seo, J., Ottesen, E.W., Shishimorova, M., Bhattacharya, D. and Singh, R.N.* (2011) TIA1 prevents skipping of a critical exon associated with spinal muscular atrophy. Molecular and Cellular Biology, 31, 935-954. *Corresponding authors
  18. Singh, N.N. and Singh, R.N. (2011) Alternative splicing in spinal muscular atrophy underscores the role of an intron definition model. RNA Biology, July 1, 8(4), 600-606.
  19. Singh, N.N., Seo, J., Rahn, S. and Singh, R.N. (2012). A multi-exon-skipping detection assay reveals surprising diversity of splice isoforms of spinal muscular atrophy genes. PLoS One, 7 (11):e49595.
  20. Custer, S.K., Todd, A.G., Singh, N.N. and Androphy, E.J. (2013) Dilysine motifs in exon 2b of SMN protein mediate binding to the COPI vesicle protein a-COP and neurite outgrowth in a cell culture model of spinal muscular atrophy. Human Molecular Genetics 22, 4043-4052.
  21. Singh, N.N., Lawler, M.N., Ottesen, E.W., Upreti, D., Kaczynski, J.R. and Singh, R.N. (2013). An intronic structure enabled by a long-distance interaction serves as a novel target for splicing correction in spinal muscular atrophy. Nucleic Acids Research 41, 8144-8165.
  22. Seo, J., Howell, M.D., Singh, N.N. and Singh, R.N. (2013). Spinal muscular atrophy: An update on therapeutic progress. Biochimica et  Biophysica Acta 1832, 2180-2190.
  23. Howell, M.D., Singh, N.N. and Singh R.N. (2014). Advances in therapeutic development for spinal muscular atrophy. Future Med. Chem. 6, 1081-1099.
  24. Singh, N.N., Lee, B. M. and Singh R. N. (2015) Splicing regulation in spinal muscular atrophy by a RNA structure formed by long distance interactions. Annals of the New York Academy of Sciences, 1341, 176-187.
  25. Singh, N.N., Lee, B.M., DiDonato, C.J and Singh, R.N. (2015) Mechanistic principles of antisense targets for the treatment of spinal muscular atrophy. Future Medical Chemistry, 7, 1793-1808.
  26. Ottesen, E.W., Howell, M.D., Singh, N.N., Seo J., Whitley, E.M. and Singh, R.N. (2016). Severe impairment of male reproductive organ development in a low SMN expressing mouse model of spinal muscular atrophy. Scientific Reports, 6, 20193.
  27. Seo, J., Singh, N.N., Ottesen, E.W., Sivanesan, S., Shishimorova, M. and Singh, R.N. (2016) Oxidative stress triggers body-wide skipping of multiple exons of spinal muscular atrophy gene. PLOS One, 11(4):e0154390.
  28. Seo, J., Singh, N.N., Ottesen, E.W., Lee, B.M. and Singh, R.N. (2016). A novel human-specific splice isoform alters the critical C-terminus of Survival Motor Neuron protein. Scientific Reports, 6, 30778.