PhotosBiographyFacebookTwitter

From Wikipedia, the free encyclopedia

Natalie Strynadka
Natalie Strynadka at the Royal Society admissions day in London, July 2015
Born
Natalie C. J. Strynadka

1963 (age 60–61)
Alma mater University of Alberta (BSc, PhD)
Awards
Scientific career
Fields
Institutions
Thesis Probing molecular interactions at various levels of structural definition (1990)
Doctoral advisor Michael N. G. James [6]
Website

Natalie C. J. Strynadka FRS [1] is a professor [7] [8] of Biochemistry in the Department of Biochemistry and Molecular Biology at the University of British Columbia. [9] [10] [11] [12] [13]

Education

Strynadka was educated at the University of Alberta where she was awarded a PhD in 1990. [14] Her thesis committee included Michael N. G. James and Sir David Chilton Phillips. [14]

Awards and honours

Strynadka was elected a Fellow of the Royal Society (FRS) in 2015. Her certificate of election reads: [1]

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. ^ a b c Anon (2015). "Professor Natalie Strynadka FRS". London: royalsociety.org. Archived from the original on 12 May 2015.
  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. Bibcode: 2007Sci...315.1402L. doi: 10.1126/science.1136611. PMID  17347437. S2CID  41658295.
  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. Bibcode: 2008PNAS..10514832W. 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. Bibcode: 1994Natur.368..657S. doi: 10.1038/368657a0. PMID  8145854. S2CID  25485212.
  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. Bibcode: 2014Natur.510..503K. doi: 10.1038/nature13445. PMC  4981499. 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. ^ "Strynadka laboratory". strynadkalab.biochem.ubc.ca. Archived from the original on 12 August 2015.
  8. ^ "Natalie C.J. Strynadka, PhD: Senior International Research Scholar / 2012–Present". hhmi.org. Archived from the original on 18 May 2015.
  9. ^ 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. Bibcode: 1992Natur.359..700S. doi: 10.1038/359700a0. PMID  1436034. S2CID  4253788.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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. Bibcode: 2008Natur.453..124Z. doi: 10.1038/nature06832. PMID  18451864. S2CID  205212689.
  13. ^ Natalie Strynadka publications indexed by the Scopus bibliographic database. (subscription required)
  14. ^ a b Strynadka, Natalie C. J. (1990). Probing molecular interactions at various levels of structural definition (PhD thesis). University of Alberta. doi: 10.7939/R37D2QG6S. OCLC  70312424. ProQuest  230755977. Open access icon


From Wikipedia, the free encyclopedia

Natalie Strynadka
Natalie Strynadka at the Royal Society admissions day in London, July 2015
Born
Natalie C. J. Strynadka

1963 (age 60–61)
Alma mater University of Alberta (BSc, PhD)
Awards
Scientific career
Fields
Institutions
Thesis Probing molecular interactions at various levels of structural definition (1990)
Doctoral advisor Michael N. G. James [6]
Website

Natalie C. J. Strynadka FRS [1] is a professor [7] [8] of Biochemistry in the Department of Biochemistry and Molecular Biology at the University of British Columbia. [9] [10] [11] [12] [13]

Education

Strynadka was educated at the University of Alberta where she was awarded a PhD in 1990. [14] Her thesis committee included Michael N. G. James and Sir David Chilton Phillips. [14]

Awards and honours

Strynadka was elected a Fellow of the Royal Society (FRS) in 2015. Her certificate of election reads: [1]

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. ^ a b c Anon (2015). "Professor Natalie Strynadka FRS". London: royalsociety.org. Archived from the original on 12 May 2015.
  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. Bibcode: 2007Sci...315.1402L. doi: 10.1126/science.1136611. PMID  17347437. S2CID  41658295.
  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. Bibcode: 2008PNAS..10514832W. 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. Bibcode: 1994Natur.368..657S. doi: 10.1038/368657a0. PMID  8145854. S2CID  25485212.
  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. Bibcode: 2014Natur.510..503K. doi: 10.1038/nature13445. PMC  4981499. 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. ^ "Strynadka laboratory". strynadkalab.biochem.ubc.ca. Archived from the original on 12 August 2015.
  8. ^ "Natalie C.J. Strynadka, PhD: Senior International Research Scholar / 2012–Present". hhmi.org. Archived from the original on 18 May 2015.
  9. ^ 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. Bibcode: 1992Natur.359..700S. doi: 10.1038/359700a0. PMID  1436034. S2CID  4253788.
  10. ^ 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.
  11. ^ 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.
  12. ^ 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. Bibcode: 2008Natur.453..124Z. doi: 10.1038/nature06832. PMID  18451864. S2CID  205212689.
  13. ^ Natalie Strynadka publications indexed by the Scopus bibliographic database. (subscription required)
  14. ^ a b Strynadka, Natalie C. J. (1990). Probing molecular interactions at various levels of structural definition (PhD thesis). University of Alberta. doi: 10.7939/R37D2QG6S. OCLC  70312424. ProQuest  230755977. Open access icon



Videos

Youtube | Vimeo | Bing

Websites

Google | Yahoo | Bing

Encyclopedia

Google | Yahoo | Bing

Facebook