Natalie Strynadka

Natalie Strynadka

Natalie Strynadka in 2015, portrait via the Royal Society
Born Natalie C. J. Strynadka
1963 (age 52–53)[1]
Fields
Institutions
Alma mater University of Alberta (BSc, PhD)
Thesis Probing molecular interactions at various levels of structural definition (1990)
Doctoral advisor Michael N. G. James[6]
Doctoral students
  • Andrew Alexander
  • Brianne Burkinshaw[7]
  • Dustin King[8]
  • Franco Li
  • Matt Solomonson[9]
  • Sean Workman[10]
Notable awards

Website

Natalie C. J. Strynadka FRS[11] is a Professor of Biochemistry in the Department of Biochemistry and Molecular Biology at the University of British Columbia.[12][13][14][15][16]

Education

Strynadka was educated at the University of Alberta where she was awarded a PhD in 1990.[17] Her thesis committee included Michael N.G. James and Sir David Chilton Phillips.[17]

Awards and honours

Strynadka was elected a Fellow of the Royal Society (FRS) in 2015. Her certificate of election reads:[11]

Natalie Strynadka is a pioneer in the study of proteins and protein assemblies essential to bacterial pathogenicity and antibiotic resistance. Her agenda-setting dissection of the membrane assemblies involved in infection, virulence and bacterial cell wall synthesis is having major impact in the development of therapeutic agents; both antibiotics and vaccines.

References

  1. ↑ Natalie Strynadka VIAF: 105554096
  2. ↑ Lovering, A. L.; De Castro, L. H.; Lim, D; Strynadka, N. C. (2007). "Structural insight into the transglycosylation step of bacterial cell-wall biosynthesis". Science 315 (5817): 1402–5. doi:10.1126/science.1136611. PMID 17347437.
  3. ↑ Wilke, M. S.; Heller, M; Creagh, A. L.; Haynes, C. A.; McIntosh, L. P.; Poole, K; Strynadka, N. C. (2008). "The crystal structure of MexR from Pseudomonas aeruginosa in complex with its antirepressor ArmR". Proceedings of the National Academy of Sciences 105 (39): 14832–7. doi:10.1073/pnas.0805489105. PMC 2567453. PMID 18812515.
  4. ↑ Strynadka, N. C.; Jensen, S. E.; Johns, K; Blanchard, H; Page, M; Matagne, A; Frère, J. M.; James, M. N. (1994). "Structural and kinetic characterization of a beta-lactamase-inhibitor protein". Nature 368 (6472): 657–60. doi:10.1038/368657a0. PMID 8145854.
  5. ↑ King, A. M.; Reid-Yu, S. A.; Wang, W; King, D. T.; De Pascale, G; Strynadka, N. C.; Walsh, T. R.; Coombes, B. K.; Wright, G. D. (2014). "Aspergillomarasmine a overcomes metallo-β-lactamase antibiotic resistance". Nature 510 (7506): 503–6. doi:10.1038/nature13445. PMID 24965651.
  6. ↑ Strynadka, N. C. J.; James, M. N. G. (1989). "Crystal Structures of the Helix-Loop-Helix Calcium-Binding Proteins". Annual Review of Biochemistry 58: 951–98. doi:10.1146/annurev.bi.58.070189.004511. PMID 2673026.
  7. ↑ Burkinshaw, B. J.; Deng, W; Lameignère, E; Wasney, G. A.; Zhu, H; Worrall, L. J.; Finlay, B. B.; Strynadka, N. C. (2015). "Structural Analysis of a Specialized Type III Secretion System Peptidoglycan-cleaving Enzyme". Journal of Biological Chemistry 290 (16): 10406–17. doi:10.1074/jbc.M115.639013. PMC 4400350. PMID 25678709.
  8. ↑ King, D. T.; Lameignere, E; Strynadka, N. C. (2014). "Structural insights into the lipoprotein outer membrane regulator of penicillin-binding protein 1B". Journal of Biological Chemistry 289 (27): 19245–53. doi:10.1074/jbc.M114.565879. PMC 4081958. PMID 24808177.
  9. ↑ Solomonson, M; Huesgen, P. F.; Wasney, G. A.; Watanabe, N; Gruninger, R. J.; Prehna, G; Overall, C. M.; Strynadka, N. C. (2013). "Structure of the mycosin-1 protease from the mycobacterial ESX-1 protein type VII secretion system". Journal of Biological Chemistry 288 (24): 17782–90. doi:10.1074/jbc.M113.462036. PMC 3682577. PMID 23620593.
  10. ↑ "People in the Strynadka lab". University of British Columbia. Archived from the original on 2014-02-26.
  11. 1 2 3 "Professor Natalie Strynadka FRS". London: The Royal Society. Archived from the original on 2015-05-12.
  12. ↑ Strynadka, N. C.; Adachi, H; Jensen, S. E.; Johns, K; Sielecki, A; Betzel, C; Sutoh, K; James, M. N. (1992). "Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 a resolution". Nature 359 (6397): 700–5. doi:10.1038/359700a0. PMID 1436034.
  13. ↑ Paetzel, M; Karla, A; Strynadka, N. C.; Dalbey, R. E. (2002). "Signal peptidases". Chemical Reviews 102 (12): 4549–80. doi:10.1021/cr010166y. PMID 12475201.
  14. ↑ Gao, S; Kinzig, K. P.; Aja, S; Scott, K. A.; Keung, W; Kelly, S; Strynadka, K; Chohnan, S; Smith, W. W.; Tamashiro, K. L.; Ladenheim, E. E.; Ronnett, G. V.; Tu, Y; Birnbaum, M. J.; Lopaschuk, G. D.; Moran, T. H. (2007). "Leptin activates hypothalamic acetyl-CoA carboxylase to inhibit food intake". Proceedings of the National Academy of Sciences 104 (44): 17358–63. doi:10.1073/pnas.0708385104. PMC 2077261. PMID 17956983.
  15. ↑ Zarivach, R; Deng, W; Vuckovic, M; Felise, H. B.; Nguyen, H. V.; Miller, S. I.; Finlay, B. B.; Strynadka, N. C. (2008). "Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS". Nature 453 (7191): 124–7. doi:10.1038/nature06832. PMID 18451864.
  16. ↑ Natalie Strynadka's publications indexed by the Scopus bibliographic database, a service provided by Elsevier.
  17. 1 2 Strynadka, Natalie C. J. (1990). Probing molecular interactions at various levels of structural definition (PhD thesis). University of Alberta. OCLC 70312424.


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