UOttawa Publications
35. Kiattiburut, W., Zhi, R.N., Lee, S.G., Foo, A.C., Hickling, D.R., Keillor, J.W., Goto, N.K., Conlan, W., Angel, J.B., Wang, G.S., Tanphaichitr, N (2018) Antimicrobial peptide LL-37 and its truncated forms, GI-20 and GF-17, exert spermicidal effects and microbicidal activity against Neisseria gonorrhoeae. Hum Reprod. 33(12): 2175-2183.
34. Ayed, S.H., Cloutier A.D., McLeod L.J., Foo A.C.Y, Damry A.M. & N.K. Goto (2017) Dissecting the role of conformational change and membrane binding by the bacterial cell division regulator MinE in the stimulation of MinD ATPase activity. J Biol Chem. 292(50): 20732-43.
33. Davey, J.A., Damry, A.M., Goto, N.K. & R.A. Chica (2017) Rational design of proteins that exchange on functional timescales. Nat Chem Biol. 13(12): 1280-85.
32. Qureshi T. & N.K. Goto (2016). Impact of differential detergent interactions on transmembrane helix dimerization affinities. ACS Omega. 1(2): 277-285.
31. Desrochers, G.F., Sherratt, A.R., Blais, D.R., Nasheri, N., Ning, Z., Figeys, D., Goto, N.K. & J.P. Pezacki (2015) Profiling kinase activity during hepatitis C virus replication using a wortmannin probe. ACS Infect Dis. 11(1): 443-52.
30. Davey, J.A., Damry, A.M., Euler, C.K., Goto, N.K. & R.A. Chica (2015) Prediction of stable globular proteins using negative design with non-native backbone ensembles. Structure 23(11): 2011-21.
29. Nasheri, N., Ning, Z., Figeys, D., Yao, S., Goto, N.K., & J.P. Pezacki (2015) Activity-based profiling of the proteasome pathway during hepatitis C virus infection. Proteomics. 15(22): 3815-25.
28. Foo A.C., Harvey B.G., Metz J.J. & N.K. Goto (2015) Influence of hydrophobic mismatch on the catalytic activity of E. coli GlpG rhomboid protease. Protein Sci. 24:464-73.
27. Houman, G., Ka-Cheong Kwok, J.K.-C., Sherratt A.R., Foo, A.C.Y., Qureshi, T. & N.K. Goto (2014) Micelle-catalyzed domain swapping in the GlpG rhomboid protease cytoplasmic domain. Biochemistry 53:5907-15.
26. Sherratt A.R., Nasheri N., McKay C.S., O'Hara S., Hunt A., Ning Z., Figeys D., Goto N.K. & J.P. Pezacki (2014) A new chemical probe for phosphatidylinositol kinase activity. Chembiochem 15:1253-6.
25. N.K. Goto (2014) The importance of intrinsic order in a disordered protein ligand. Biophys J. 106:1557-8.
24. Sherratt, A.R. Blais, D., Ghasriani, H., Pezacki, J. P. & N.K. Goto (2012) Activity-based protein profiling of the E. coli GlpG rhomboid protein delineates the catalytic core. Biochemistry 51: 7794-803.
23. Qureshi, T. & N.K. Goto (2012) Contemporary methods in membrane protein structure determination by solution NMR. In G. Zhu ed Topics in Current Chemistry Springer 326:123-185.
22. Ghasriani, H. & N.K. Goto (2011) Regulation of symmetrical bactetrial cell division by MinE: What is the role of conformational dynamics? Commun Integr Biol 4:101-103.
21. Ghasriani, H., Ducat, T., Hart, C.T., Hafizi, F., Chang, N. Al-Baldawi, A., Ayed, S.H., Lundström, P., Dillon J.A.R. & N.K. Goto (2010) Appropriation of the MinD protein-interaction motif by the dimeric interface of the bacterial cell division regulator MinE. Proc. Natl. Acad. Sci. USA 107:18416-21.
20. Ducat, T. & N.K. Goto (2010) 1H, 13C, 15N chemical shift assignments for the Neisseria gonorrhoeae MinE regulator of cell division septum placement. Biomol. NMR Assign. 4:227-229.
19. Sherratt A.R., Braganza M.V., Nguyen E., Ducat T. & N.K. Goto (2009) Insights into the effect of detergents on the full-length rhomboid protease from Pseudomonas aeruginosa and its cytosolic domain. Biochim. Biophys. Acta - Biomembranes 1788: 2444-2453.
18. Shih S.C., Stoica I. & N.K. Goto (2008) Investigation of the utility of selective methyl protonation for determination of membrane protein structures. J. Biomol. NMR 42: 49-58.
17. Wu, Y., Shih, S.C., & N.K. Goto (2007) Probing the structure of the Ff bacteriophage major coat protein transmembrane helix dimer by solution NMR. Biochim. Biophys. Acta - Biomembranes (Special edition on Membrane Protein NMR) 1768: 3206-3215.
16. Cheng, J., Sagan S.M., Assem, N., Koukiekolo, R., Goto, N.K. & J.P. Pezacki (2007) Stabilized recombinant suppressors of RNA silencing: Functional effects of linking monomers of Carnation Ringspot virus p19. Biochim. Biophys. Acta - Proteins & Proteomics 1774: 1528-1535.
15. Sagan S.M., Koukiekolo R, Rodgers E, Goto, N.K. & J.P. Pezacki (2007) Inhibition of siRNA binding to a p19 viral suppressor of RNA silencing by cysteine alkylation Angew. Chem.- Int. Edit. 46: 2005-2009.
14. Ramos, D., Ducat, T., Cheng, J., Eng, N.F., Dillon, J.A.R. & N.K. Goto (2006) Interactions between the topological specificity domain and anti-MinCD domain of the cell division regulator MinE. Biochemistry 45:4593-4601.
13. Melnyk, R.A., Partridge, A.W., Yip, J., Wu, Y., Goto, N.K. & C.M. Deber (2003) Polar residue tagging of transmembrane peptides. Biopolymers (Pept. Sci.) 71:675-85.
Post-doc Publications
12. *De Guzman, R.N., *Goto, N.K., Dyson, H.J., & P.E. Wright (2006) Structural basis for cooperative transcription factor binding to CBP J. Mol. Biol. 355:1005-13.
11. Mohana-Borges, R., Goto, N.K., Kroon, G., Dyson, H.J. & P.E. Wright (2004) Structural characterization of unfolded and partly folded states of apomyoglobin using residual dipolar couplings. J. Mol. Biol. 340: 1131-42.
10. Goto, N.K., Zor, T. Martinez-Yamout, M., Dyson, H.J. & Wright, P.E. (2002) Cooperativity in transcription factor binding to the coactivator CBP: The MLL activation domain binds to an allosteric site on the KIX domain. J. Biol. Chem. 277: 43168-43174.
Ph.D. Publications
9. Evanas, J., V. Tugarinov, N.R. Skrynnikov, N.K. Goto, R. Muhandiram & L.E. Kay. (2001) Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopy. J. Mol. Biol. 309: 961-974.
8. Goto, N.K., N.R. Skrynnikov, F.W. Dahlquist & L.E. Kay. (2001) What is the average conformation of T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMR. J. Mol. Biol. 308: 745-764.
7. Skrynnikov, N.R., N. K. Goto, D. Yang, W.-Y. Choy, J.R. Tolman, G.A. Mueller & L.E. Kay. (2000) Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin binding protein loaded with β- cyclodextrin. J. Mol. Biol. 295: 1265-1273.
6. Goto, N.K. & L.E. Kay. (2000) Isotope labeling strategies for protein solution NMR. Curr. Opin. Struct. Biol. 10: 585-592.
5. Goto, N.K., K.H. Gardner, G.A. Mueller, R.C. Willis & L.E. Kay. (1999) A robust and cost- effective method for the production of Val, Leu, Ile (δ1) methyl-protonated 15N-, 13C-, 2H- labeled proteins. J. Biomol. NMR 13: 369-374.
4. Yang, D., Tolman, J.R., Goto, N.K. & L.E. Kay (1998) An HNCO-based pulse scheme for the measurement of 13Cα-1Hα one-bond dipolar couplings in 15N, 13C labeled proteins. J. Biomol. NMR. 12: 325-332.
3. Deber, C.M. & N.K. Goto (1996) Folding proteins into membranes. (News and Views). Nature Struct. Biol. 3: 815-818.
2. Liu, L.-P., S.C. Li, N.K. Goto & C.M. Deber. (1996) Threshold hydrophobicity dictates helical conformations of peptides in membrane environments. Biopolymers 39: 465-470.
1. Li, S.C., N.K. Goto, K.A. Williams & C.M. Deber. (1996) Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environment. Proc. Natl. Acad. Sci. 93: 6676- 6681.