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Department of Plant Pathology Molecular Plant Pathology Laboratory

Tanaka Lab – Personnel

 

Natalia Moroz

Postdoctoral Associate

Contact Information

WSU Plant Pathology
PO BOX 646430
Pullman, WA, 99163-6430
Office – Johnson Hall 372
Lab – Johnson Hall 358
Phone: (509) 335-5813 | Fax: (509) 335-9581

natalia.moroz [at] wsu.edu

Education
  • 1998 Ph.D. (Chemistry), Department of Chemistry, Moscow State University, Russia
  • 1991 B.S. (Chemistry), Department of Chemistry, Kyrgyz State University, Frunze (now Bishkek), Kyrgyzstan
Professional Experience
  • Postdoctoral Research Associate, Department of Plant Pathology, Washington State University, Pullman, WA (2015 – Present)
  • Postdoctoral Research Associate, The Gene and Linda Voiland School of Chemical Engineering and Bioengineering, Washington State University, Pullman, WA (2012 – 2015)
  • Research Associate III, Neuroscience and Cell Biology Department, Rutgers Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, NJ (2010 – 2011)
  • Research Scholar, W.M. Burke Medical Research Institute, Cornell University Medical College, White Plains, NY (2008 – 2009)
  • Lumtek, LLC, Moscow, Russia (2004 – 2008)
  • Senior Research Scientist, Chemistry Department, Moscow State University, Russia (1997 – 2008)
Academic Honors, Awards, and Achievements
  • Postdoc Travel Award to attend American Society for Cell Biology. New Orleans, LN, USA (2013)
  • PhD student Travel Award to attend XIII International Congress on Fibrinolysis and Thrombolysis. Barcelona, Spain (1996)
  • PhD student Travel Award to attend III International Union of Biology and Molecular Biology Conference “Molecular Recognition”. Singapore (1995)
Teaching Experience
  • Guest lecturer for Pl_P 535 Molecular Genetics of Plant-Pathogen Interactions at WSU, Pullman, WA (2016)
  • Guest lecturer for BE 481 Protein Bioengineering, Chemical Engineering and Bioengineering, at WSU, Pullman, WA
Current Research Focus
  • Improved disease control strategies for potato powdery scab
Profile links

Loop | ResearchGate | LinkedIn

Publications
  1. Moroz N, Huffaker A, Tanaka K (2017) Extracellular alkalinization assay for detection of early defense response. Curr. Protoc. Plant Biol. 2: 210-220 doi:10.1002/cppb.20057
  2. Moroz N, Fritch KR, Marcec MJ, Tripathi D, Smertenko A, Tanaka K (2017) Extracellular alkalinization as a defense response in potato cells. Front. Plant Sci. 8: 32 doi:10.3389/fpls.2017.00032
  3. Ly T*, Moroz N*, Pappas CT, Novak SM, Tolkatchev D, Wooldridge D, Mayfield RM, Helms G, Gregorio CC, Kostyukova AS (2016) The N-terminal tropomyosin- and actin-binding sites are important for leiomodin 2’s function. Mol. Biol. Cell 27: 2565-75 *equal contribution doi:10.1091/mbc.E16-03-0200
  4. Colpan M, Moroz NA, Gray KT, Cooper DA, Diaz CA, Kostyukova AS (2016) Tropomyosin-binding properties modulate competition between tropomodulin isoforms. Arch. Biochem. Biophys. 600: 23-32 doi:10.1016/j.abb.2016.04.006
  5. Colpan M, Tolkatchev D, Grover S, Helms G, Cort J, Moroz N, Kostyukova AS (2016). Localization of the Binding Interface between Leiomodin-2 and alpha-Tropomyosin. Biochem. Biophys. Acta 1864: 523-30 doi:10.1016/j.bbapap.2016.02.009
  6. Yuen M, Sandaradura SA, Dowling JJ, Kostyukova AS, Moroz N et al. (2014) Leiomodin-3 dysfunction results in thin filament disorganization and nemaline myopathy. J. Clinic. Invest. 124: 4693-708 doi:10.1172/JCI75199
  7. Guillaud L, Gray KT, Moroz N, Pantazis C, Pate E, Kostyukova AS (2014) Role of Tropomodulin’s Leucine Rich Repeat Domain in the Formation of Neurite-like Processes. Biochemistry 53: 2689-700 doi:10.1021/bi401431k
  8. Galeva A, Moroz N, Yoon Y-H, Hughes KT, Samatey FA, Kostyukova AS (2014) Bacterial flagellin-specific chaperone FliS interacts with anti-sigma factor FlgM. J. Bacteriol. 196: 1215–21 doi:10.1128/JB.01278-13
  9. Colpan M, Moroz N, Kostyukova AS (2013) Tropomodulins and Tropomyosins: Working as a team. J. Muscle Res. Cell Motility 3: 247-60 doi:10.1007/s10974-013-9349-6
  10. Moroz N, Novak S, Azevedo R, Colpan M, Uversky V, Gregorio C, Kostyukova AS (2013) Alteration of tropomyosin-binding properties of tropomodulin1 affects its capping ability and localization in skeletal myocytes. J. Biol. Chem. 288: 4899-907 doi:10.1074/jbc.M112.434522
  11. Moroz N, Guillaud L, Desai B, Kostyukova AS (2013) Mutations changing tropomyosin affinity in site 1 of tropomodulin alter neurite formation and extension. Peer J. 1: e7 doi:10.7717/peerj.7
  12. Tsukada T, Pappas CT, Moroz N, Antin PB, Kostyukova AS, Gregorio CC (2010) Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle. J. Cell Sci. 123: 3136-45 doi:10.1242/jcs.071837
  13. Smirnova N, Rakhman I, Moroz N, Basso M, Payapilli J, Hernandes-Guzman F, Kazakov S, Gaysina I, Ratan R, Gazaryan I (2010) Utilization of an in vivo reporter for high-throughput screen for HIF stabilizers: identification of novel group of branched HIF prolyl hydroxylase inhibitors. Chemistry & Biology 17: 380–91 doi:10.1016/j.chembiol.2010.03.008
  14. Moroz NA, Gursky DY, Ugarova NN (2008) Stabilization of ATP- Reagents containing firefly luciferase Luciola mingrelica by polyols. Moscow University Chemistry Bulletin 49: 86-90 doi:10.3103/S0027131408020041
  15. Froundjian VG, Lomakina GY, Moroz NA, Ugarova NN (2005) Bioluminescence assay of microbial contamination of force-meat. Meat Industry 2: 54-57
  16. Gladysheva IP, Moroz NA, Karmakova TA, Nemtsova ER, Yakubovskaya RI, Larionova NI (2002) Immunoconjugates of soybean Bowman-Birk protease inhibitor as targeted antitumor polymeric agents. J. Drug Target. 9: 303-16 doi:10.3109/10611860108998767
  17. Balabushevitch NG, Sukhorukov GB, Moroz NA, Kazanskaya NF, Larionova NI, Volodkin DV, Donath E, Mehwald H (2001) Encapsulation of proteins by layer-by-layer adsorption of polyelectrolytes onto protein aggregates: Factors regulating the protein release. Biotechnology and Bioengineering 76: 207-13 doi:10.1002/bit.1184
  18. Gladysheva IP, Moroz NA, Papisova AI, Larionova NI (2001) Soybean Bowman-Birk inhibitor conjugates with clinical dextran: synthesis and antiproteolytic activity. Biochemistry (Moscow) 66: 384-9 doi:10.1023/A:1010241127300
  19. Gladysheva IP, Balabushevich NG, Moroz NA, Larionova NI (2000) Isolation and characterization of soybean Bowman-Birk inhibitor from different sources. Biochemistry (Moscow) 65: 198-203 PMID:10713547
  20. Larionova NI, Moroz NA, Tyurina OP (1999) Molecular design, characterization activity of conjugates of protein proteinase inhibitors. S. T. P. Pharma Sci. 9: 65-80
  21. Kil’deeva NR, Trusova SP, Gorchakova VA, Khomyakov KP, Larionova NI, Balabushevitch NG, Moroz NA, Virnik AD (1997) Multicomponent Polymer Systems Containing Biologically Active Proteins and Antimicrobial Compounds. Applied Biochem. Microbiol. 33: 433-6 doi:10.1007/BF02785695
  22. Balabushevitch NG, Kildeyeva NR, Moroz NA, Trusova SP, Khromov GL, Larionova NI (1996) Regulating Aspects of Biosoluble and Insoluble Film Release Systems Containing Protein Proteinase Inhibitor. Applied Biochem. Biotech. 61: 129-38 doi:10.1007/BF02785695
  23. Moroz NA, Balabushevitch NG, Khromov GL, Kildeyeva NR, Larionova NI (1995) Engineering-Enzymological Approach to the Design of Polymeric Forms of Aprotinin. Vestnik Moskovskogo Universiteta Seriya 2 Khimiya 36: 139-44
  24. Larionova NI, Balabushevitch NG, Gladysheva IP, Moroz NA, Kazanskaya NF, Polekhina OV, Donetsky IA (1994) Natural Protease Inhibitors as a Basis for the New Drug Synthesis. Voprosi Med. Khimii 40: 25-31 PMID: 7521547