Publications
(* = corresponding author)
Moise, G., Gallup, N.M., Alexandrova, A.N., Hengge, A.C.*, and Johnson, S.J.* (2015). “Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites.” Biochemistry 54 (42): 6490-6500. (doi: 10.1021/acs.biochem.5b00496) PubMed
Losh, J.S., King, A.K., Bakelar, J., Taylor, L., Loomis, J., Rosenzweig, J.A., Johnson, S.J., van Hoof, A.* (2015). “Interaction between the RNA-dependent ATPase and poly(A) polymerase subunits of the TRAMP complex is mediated by short peptides and important for snoRNA processing.” Nucleic Acids Research 43(3): 1848-1858. (doi: 10.1093/nar/gkv005) PubMed
Taylor, L., Jackson, R.N., Rexhepaj, M., King, A.K., Lott, L.K., van Hoof, A., Johnson, S.J.* (2014). “The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding.” Nucleic Acids Research 42(22):13861-72. (doi: 10.1093/nar/gku1208) PubMed
Bakelar, J., Silwa, D. and Johnson, S.J.* (2013). “Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases.” Archives of Biochemistry and Biophysics 533 (1-2):62-68. (doi: 10.1016/j.abb.2013.02.017) PubMed
Zeng, J., Lytle, A.K., Gage, D., Johnson, S.J. and Zhan, J.* (2013). “Specific chlorination of isoquinolines by a fungal flavin-dependent halogenase.” Bioorganic and Medicinal Chemistry Letters 23 (4):1001-1003. (doi: 10.1016/j.bmcl.2012.12.038) PubMed
Johnson, S.J.* and Jackson, R.N. (2013). “Structures of Ski2-like RNA helicases: common themes and complex assemblies.” RNA Biology 10 (1):33-43. (doi: 10.4161/rna.22101) PubMed
Kuznetsov, V.I., Hengge, A.C.* and Johnson, S.J.* (2012) “New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening.” Biochemistry 51(49):9869-79. (doi: 10.1021/bi300908y) PubMed
Schaeffer, D., Reis, F.P., Johnson, S.J., Arraiano, C.M. and van Hoof, A.* (2012). “The CR3 motif of Rrp44p is important for interaction with the core exosome and exosome function.” Nucleic Acids Research. 40 (18):9298-9307. (doi: 10.1093/nar/gks693) PubMed
Brandão, T.A.S., Johnson, S.J.* and Hengge, A.C.* (2012).The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B. Archives of Biochemistry and Biophysics. 525(1):53-59. (doi: 10.1016/j.abb.2012.06.002) PubMed
Gui, L., Wooderchack, W., Porter, P., Daly, M., Johnson, S.J. and Hevel, J.M.* (2011). Investigation of the Molecular Origins of Protein Arginine Methyltransferase I (PRMT1) Product Specificity Reveals a Role for Two Conserved Methionine Residues. Journal of Biological Chemistry. 286(33):29118-29126. (doi: 10.1074/jbc.M111.224097) PubMed
Close, D., Johnson, S.J., Sadano, M., McDonald, S., Robinson, H. and Hill, C.P.* (2011). Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain. Journal of Molecular Biology. 408(4):697-713. (doi:10.1016/j.jmb.2011.03.002) PubMed
Hintze, B.J. and Johnson, S.J.* (2010). ResDe: A New Tool for Visual Definition of Distance Restraints for Crystallographic Refinement. The Journal of Applied Crystallography. 6, 1540-1542 (doi:10.1107/S0021889810038689) Journal Site
Jackson, R.N., Klauer, A.A., Hintze, B.J., Robinson, H., van Hoof, A. and Johnson, S.J.* (2010). The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. The EMBO Journal. 29, 2205-2216. (doi:10.1038/emboj.2010.107) PubMed
Brandão, T.A.S., Hengge, A.C.* and Johnson, S.J.* (2010) Insights into the reaction of protein tyrosine phosphatase 1B. Crystal structures for transition-state analogs of both catalytic steps. Journal of Biological Chemistry. 285(21):15874-83. (doi: 10.1074/jbc.M109.066951) PubMed
Brandão, T.A.S., Robinson, H., Johnson, S.J.* and Hengge, A.C.* (2009). Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures. Journal of the American Chemical Society. 131(2), 778-786. (doi:10.1021/ja807418b) PubMed
Johnson, S.J., Close, D., Robinson, H., Vallet-Gely, I., Dove, S.L, Hill, C.P.* (2008). Crystal Structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. Journal of Molecular Biology. 377(5), 1460-1473. (doi:10.1016/j.jmb.2008.01.096) PubMed
Johnson, S.J., Beese, L.S.* (2004). Structures of mismatch replication errors observed in a DNA polymerase. Cell 116(6), 803-816. (doi:10.1016/S0092-8674(04)00252-1) PubMed
Johnson, S.J., Taylor, J.S., Beese, L.S.* (2003). Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proceedings of the National Academy of Sciences USA, 100, 3895-3900. (doi:10.1073/pnas.0630532100) PubMed
Moise, G., Gallup, N.M., Alexandrova, A.N., Hengge, A.C.*, and Johnson, S.J.* (2015). “Conservative Tryptophan Mutants of the Protein Tyrosine Phosphatase YopH Exhibit Impaired WPD-Loop Function and Crystallize with Divanadate Esters in Their Active Sites.” Biochemistry 54 (42): 6490-6500. (doi: 10.1021/acs.biochem.5b00496) PubMed
Losh, J.S., King, A.K., Bakelar, J., Taylor, L., Loomis, J., Rosenzweig, J.A., Johnson, S.J., van Hoof, A.* (2015). “Interaction between the RNA-dependent ATPase and poly(A) polymerase subunits of the TRAMP complex is mediated by short peptides and important for snoRNA processing.” Nucleic Acids Research 43(3): 1848-1858. (doi: 10.1093/nar/gkv005) PubMed
Taylor, L., Jackson, R.N., Rexhepaj, M., King, A.K., Lott, L.K., van Hoof, A., Johnson, S.J.* (2014). “The Mtr4 ratchet helix and arch domain both function to promote RNA unwinding.” Nucleic Acids Research 42(22):13861-72. (doi: 10.1093/nar/gku1208) PubMed
Bakelar, J., Silwa, D. and Johnson, S.J.* (2013). “Crystal structures of S-HPCDH reveal determinants of stereospecificity for R- and S-hydroxypropyl-coenzyme M dehydrogenases.” Archives of Biochemistry and Biophysics 533 (1-2):62-68. (doi: 10.1016/j.abb.2013.02.017) PubMed
Zeng, J., Lytle, A.K., Gage, D., Johnson, S.J. and Zhan, J.* (2013). “Specific chlorination of isoquinolines by a fungal flavin-dependent halogenase.” Bioorganic and Medicinal Chemistry Letters 23 (4):1001-1003. (doi: 10.1016/j.bmcl.2012.12.038) PubMed
Johnson, S.J.* and Jackson, R.N. (2013). “Structures of Ski2-like RNA helicases: common themes and complex assemblies.” RNA Biology 10 (1):33-43. (doi: 10.4161/rna.22101) PubMed
Kuznetsov, V.I., Hengge, A.C.* and Johnson, S.J.* (2012) “New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening.” Biochemistry 51(49):9869-79. (doi: 10.1021/bi300908y) PubMed
Schaeffer, D., Reis, F.P., Johnson, S.J., Arraiano, C.M. and van Hoof, A.* (2012). “The CR3 motif of Rrp44p is important for interaction with the core exosome and exosome function.” Nucleic Acids Research. 40 (18):9298-9307. (doi: 10.1093/nar/gks693) PubMed
Brandão, T.A.S., Johnson, S.J.* and Hengge, A.C.* (2012).The molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1B. Archives of Biochemistry and Biophysics. 525(1):53-59. (doi: 10.1016/j.abb.2012.06.002) PubMed
Gui, L., Wooderchack, W., Porter, P., Daly, M., Johnson, S.J. and Hevel, J.M.* (2011). Investigation of the Molecular Origins of Protein Arginine Methyltransferase I (PRMT1) Product Specificity Reveals a Role for Two Conserved Methionine Residues. Journal of Biological Chemistry. 286(33):29118-29126. (doi: 10.1074/jbc.M111.224097) PubMed
Close, D., Johnson, S.J., Sadano, M., McDonald, S., Robinson, H. and Hill, C.P.* (2011). Crystal structures of the S. cerevisiae Spt6 core and C-terminal tandem SH2 domain. Journal of Molecular Biology. 408(4):697-713. (doi:10.1016/j.jmb.2011.03.002) PubMed
Hintze, B.J. and Johnson, S.J.* (2010). ResDe: A New Tool for Visual Definition of Distance Restraints for Crystallographic Refinement. The Journal of Applied Crystallography. 6, 1540-1542 (doi:10.1107/S0021889810038689) Journal Site
Jackson, R.N., Klauer, A.A., Hintze, B.J., Robinson, H., van Hoof, A. and Johnson, S.J.* (2010). The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. The EMBO Journal. 29, 2205-2216. (doi:10.1038/emboj.2010.107) PubMed
Brandão, T.A.S., Hengge, A.C.* and Johnson, S.J.* (2010) Insights into the reaction of protein tyrosine phosphatase 1B. Crystal structures for transition-state analogs of both catalytic steps. Journal of Biological Chemistry. 285(21):15874-83. (doi: 10.1074/jbc.M109.066951) PubMed
Brandão, T.A.S., Robinson, H., Johnson, S.J.* and Hengge, A.C.* (2009). Impaired acid catalysis by mutation of a protein loop hinge residue in a YopH mutant revealed by crystal structures. Journal of the American Chemical Society. 131(2), 778-786. (doi:10.1021/ja807418b) PubMed
Johnson, S.J., Close, D., Robinson, H., Vallet-Gely, I., Dove, S.L, Hill, C.P.* (2008). Crystal Structure and RNA binding of the Tex protein from Pseudomonas aeruginosa. Journal of Molecular Biology. 377(5), 1460-1473. (doi:10.1016/j.jmb.2008.01.096) PubMed
Johnson, S.J., Beese, L.S.* (2004). Structures of mismatch replication errors observed in a DNA polymerase. Cell 116(6), 803-816. (doi:10.1016/S0092-8674(04)00252-1) PubMed
Johnson, S.J., Taylor, J.S., Beese, L.S.* (2003). Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Proceedings of the National Academy of Sciences USA, 100, 3895-3900. (doi:10.1073/pnas.0630532100) PubMed