Publications

MacKenzie, D.W.S., Schaefer, A., Steckner, J., Leo, C.A., Naser, D., Artikis, E., Broom, A., Ko, T., Shah, P., Ney, M.Q., Tran, E., Smith, M.T.J., Fuglestad, B., Wand, A.J., Brooks, C.L., and Meiering, E.M.* A fine balance: Hydrophobic-electrostatic communication pathways in a pH switching protein. Proceedings of the National Academy of Sciences USA (accepted)
Schaefer, A., Naser, D., Siebeneichler, B., Tarasca, M.V., and Meiering, E.M.* On the path to determining high resolution structures of cellular protein aggregates. Journal of Biological Chemistry (accepted)
Sankar, K., Trainor, K., Blazer, L.L., Adams, J.J., Sidhu, S.S., Day, T., Meiering, E.M., and Maier, J.K.X.* A computational framework for addressing liabilities in biologics. Molecular Informatics (accepted)
Tarasca, M.V., Naser, D., Schaefer, A., Soule, T.G.B., and Meiering, E.M.* Towards high-resolution structure of protein inclusion body aggregates by quenched hydrogen-deuterium amide exchange. Analytical Biochemistry (Epub, in press).
Naser, D., Tarasca, M.T., Siebeneichler, B., Schaefer, A., Deol, H.K., Soule, T.G.B., Almey, J., Kelso, S., Mishra, G.G., Simon, H., and Meiering, E.M.* High resolution NMR H/D exchange of human Cu,Zn superoxide dismutase inclusion bodies reveals significant native features despite structural heterogeneity. Angewandte Chemie International Edition (Epub, in press). Article Share link
Trainor, K., Doyle, C.M., Metcalfe-Roach, A., Steckner, J., Lipovsek, D., Malakian, H., Langley, D., Krystek, S.R., and Meiering, E.M.* Design for solubility may reveal induction of amide hydrogen/deuterium exchange by protein self-association. J. Mol. Biol. 434 (Epub, in press).
Cveticanin, J., Monda, T., Meiering, E.M.*, Sharon, M.*, and Horovitz, A.* Insight into the autosomal-dominant inheritance pattern of SOD1-associated ALS from native mass spectrometry. J. Mol. Biol. 432, 5995-6002 (2020). doi: 10.1016/j.jmb.2020.09.025 Commentary
Broom, A., Trainor, K., Jacobi, Z., and Meiering, E.M.* Computational modelling of protein stability: quantitative analysis reveals solutions to pervasive problems. Structure 28, 717-726 (2020). doi: 10.1016/j.str.2020.04.003
Semmler, S., Gagné, M., Pickles, S.R., Baudouin, C., Hamon-Keromen, E., Destroismaisons, L., Khalfallah, Y., Chaineau, M., Caron, E., Baynes, A.N., Trempe, J.F., Cashman, N.R., Star, A.T, Haggani, A.S., Durcan, T.M., Meiering, E.M., Roberson, J., Grandvaux, N., Plotkin, S.S., McBride, H.M., and VandeVelde, C.* TNF receptor associated factor 6 interacts with ALS-linked misfolded superoxide dismutase 1 and promotes aggregation. Journal of Biological Chemistry 295, 3808-25 (2020). doi: 10.1074/jbc.RA119.011215.
Da Ros, M., Deol, H.K., Savard, A, Guo, H.S., Meiering, E.M., and Gibbings, D.* Wild-type and mutant SOD1 localizes to RNA-rich structures in cells and mice but does not bind RNA. J. Neurochem 00, 1-15 (2020). doi: 10.1111/jnc.15126.
Trainor, K., Palumbo, J.A., MacKenzie, D.W.S., and Meiering, E.M.* Temperature dependence of NMR chemical shifts: Tracking and statistical analysis. Protein Science 29, 306-314 (2020). doi: 10.1002/pro.3785.
Doyle, C.M., Naser, D., Bauman, H.A., Rumfeldt, J.A.O., and Meiering, E.M.* Spectrophotometric method for simultaneous measurement of zinc and copper in metalloproteins using 4-(2-pyridylazo)resorcinol. Analytical Biochemistry 579, 44-56 (2019). doi: 10.1016/j.ab/2019.03.007.
Culik, R.M., Sekhar, A., Nagesh, J., Deol, H., Rumfeldt, J.A.O., Meiering, EM., and Kay, L.E.* Effects of maturation on the conformational free-energy landscape of SOD1. Proceedings of the National Academy of Sciences USA 115, E2546-E2555 (2018). doi: 10.1073/pnas.1721022115.
Broom, A., Jacobi, Z., Trainor, K., and Meiering, E.M.* Computational tools help improve protein stability but with a solubility tradeoff. Journal of Biological Chemistry 292, 14349-61 (2017). doi: 10.1074/jbc.M117.784165. Protein Stability Meta-Predictor
Cui, D.S., Broom, A., Mcleod, Meiering, E.M., and Holyoak, T.* Asymmetric anchoring is required for efficient Ω-loop opening and closing in cytosolic phosphoenolpyruvate carboxykinase. Biochemistry 56, 2106-15 (2017). doi: 10.1021/acs.biochem.7b00178.
Trainor, K., Broom, A., and Meiering, E.M.* Exploring the relationships between protein sequence, structure and solubility. Curr. Op. Struct. Biol. 42 , 136-146 (2017). doi: 10.1016/j.sbi.2017.01.004
Sekhar, A., Rumfeldt, J.A.O., Broom, H.R., Doyle, C.M., Sobertin, R.E., Meiering, E.M., and Kay, L.E.* Probing the free energy landscape of ALS disease mutants of SOD1 by NMR spectroscopy. Proceedings of the National Academy of Sciences USA 113, E6939-E6945 (2016). (pdf)
Pickles, S., Semmler, S., Broom, H.R., Destroismaisons, L., Legroux, L., Arbour, N., Meiering, E.M., Cashman, N.R., and vande Velde, C.* ALS-linked misfolded SOD1 species have divergent impacts on mitochondria. Acta Neuropath. Comm. 4, 43 (2016). (pdf)
Meiering, EM*, and Aravind, L.* Protein function - Synthesizing information from sequence, structure and disorder. Curr. Op. Struct. Biol. 38 , vii-ix (2016). doi: 10.1016/j.sbi.2016.06.016
Broom, A., Trainor, K., MacKenzie, D.W.S. and Meiering, E.M.* Using natural sequences and modularity to design common and novel protein topologies. Curr. Op. Struct. Biol. 38, 26-36 (2016). doi: 10.1016/j.sbi.2016.05.007
Trainor, K., Gingras, Z., Shillingford, C., Malakian, H., Gosselin, M., Lipovsek, D., and Meiering, E.M.* Ensemble modeling and intracellular aggregation of an engineered immunoglobulin-like domain. J. Mol. Biol. 428, 1365-74 (2016). doi: 10.1016/j.jmb.2016.02.016
Doyle, C.M., Rumfeldt, J.A., Broom, H.R., Sekhar, A., Kay, L.E., and Meiering, E.M.* Concurrent increases and decreases in local stability and conformational heterogeneity in Cu,Zn superoxide dismutase variants revealed by temperature-dependence of amide chemical shifts. Biochemistry 55, 1346-1361 (2016). doi: 10.1021/acs.biochem.5b01133
Broom, H.R., Vassall, K.A., Rumfeldt, J.A.O., Doyle, C.M., Tong, M.S., Bonner, J.M., and Meiering, E.M.* Combined isothermal titration and differential scanning calorimetry define 3-state thermodynamics of fALS-associated mutant apo SOD1 dimers and increased population of folded monomer. Biochemistry 55, 519-33 (2016). doi: 10.1021/acs.biochem.5b01187
Broom, A., Ma, S.M., Xia, K., Rafalia, H., Trainor, K., Colon, W., Gosavi, S., and Meiering, E.M.* Designed protein reveals structural determinants of extreme kinetic stability. Proceedings of the National Academy of Sciences USA 112, 14605-10 (2015). (pdf)
Broom, H.R., Rumfeldt, J.A., Vassall, K.A., and Meiering, E.M.* Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1. Protein Science 24, 2081-9 (2015). (pdf)
Sekhar, A., Bain, A.D., Rumfeldt, J.A.O., Meiering, E.M., and Kay, L.E.* Evolution of magnetization due to asymmetric dimerization: theoretical considerations and application to aberrant oligomers formed by apoSOD1(2SH). Phys Chem Chem Phys 18, 5720-8 (2015).
Broom, A., Gosavi, S., and Meiering, E.M.* Protein unfolding rates correlate as strongly as folding rates with native structure. Protein Science 24, 580-7 (2015). (pdf)
Sekhar, A.*, Rumfeldt, J.A., Broom, H.R., Doyle, C.M., Bouvignies, G., Meiering, E.M.*, and Kay, L.E.* Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways. eLife 4, e07296/33pgs (2015). (pdf)
Broom, H.R., Rumfeldt, J.A.O., and Meiering, E.M.* Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis. Essays in Biochemistry 56, 149-65 (2014). (pdf)
Tritzant-Martinez, Y., Broom, A., Meiering, E., Le Roy, R.J., and Roy, P.N.* On the analytical representation of free energy profiles with a Morse/long-range model: application to the water dimer. Journal of Chemical Physics 138, 234103/12pgs (2013).
Doyle, C.M., Rumfeldt, J.A., Broom, H.R., Broom, A., Stathopulos, P.B., Vassall, K.A., Almey, J.J., and Meiering, E.M.* Energetics of oligomeric protein folding and association. Archives of Biochemistry and Biophysics 531, 44-64 (2013).
Shental-Bechor, D., Smith, M.T.J., Mackenzie, D., Broom, A., Marcovitz, A., Ghashut, F., Go, C., Bralha, F., Meiering, E.M.*, and Levy, Y.* Nonnative interactions regulate folding and switching of myristoylated protein. Proceedings of the National Academy of Sciences USA 109, 17839-44 (2012). (pdf)
Deng, L., Broom, A., Kitova, E.N., Richards, M.R., Zheng, R.B., Shoemaker, G.K., Meiering, E.M., and Klassen, J.S.* Kinetic stability of the streptavidin-biotin interaction enhanced in the gas phase. Journal of the American Chemical Society 134, 16586-96 (2012).
Broom, A., Doxey, A.C., Lobsanov, Y.D., Berthin, L.G., Rose, D.R., Howell, P.L., McConkey, B.J.*, and Meiering, E.M.* Modular Evolution and the origins of symmetry: Reconstruction of a three-fold symmetric globular protein. Structure 20, 161-171 (2012). (pdf)
Stubbs, H.R., Primmer, H.A., Rumfeldt, J.A.O., Stathopulos, P.B., Vassall, K.A, Hwang, Y-M., and Meiering, E.M. Folding and aggregation of Cu,Zn-superoxide dismutase. Amyotrophic Lateral Sclerosis, 265-300
Martin H. Maurer (Editor), InTech Open Access Publisher, Rijeka, Croatia, ISBN: 978-953-307-806-9
Vassall, K.A., Stubbs, H.R., Primmer, H.A., Tong, M.S., Sullivan, S.M., Sobering, R., Srinivasan, S., Briere, L.A.K., Dunn, S.D., Colon, W., and Meiering, E.M.* Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS. Proceedings of the National Academy of Sciences USA108, 2210-2215 (2011). (pdf)
Smith, M.T.J., MacKenzie, D.W.S., and Meiering, E.M.* Dissecting the molecular determinants of ligand-binding-induced macromolecular switching using thermodynamic cycles. Protein Engineering Design and Selection 24, 213-217 (2011).
Hwang, Y.M., Stathopulos, P.B., Dimmick, K., Yang, H., Badiei, H.R., Tong, M.S., Rumfeldt, J.A.O., Chen, P., Karanassios, V., and Meiering, E.M.* Nonamyloid Aggregates Arising from Mature Copper/Zinc Superoxide Dismutases Resemble Those Observed in Amyotrophic Lateral Sclerosis. The Journal of Biological Chemistry 285, 41701-41711 (2010).
Smith, M.T.J., Meissner, J., Esmonde, S., Wong, H.J., and Meiering, E.M.* Energetics and mechanmisms of folding and flipping the myristoyl switch in the beta-trefoil protein, hisactophilin. Proceedings of the National Academy of Sciences USA 107, 20952-20957 (2010). (pdf)
Galvagnion, C., Meglei, G., Vassall, K.A., Gaspar, J.A., Stathopulos, P.B., Cheyne, B. and Meiering, E.M.* Folding and association of thermophilic dimeric and trimeric DsrEFH proteins: Tm0979 and Mth1491. Biochemistry 48, 2891-2906 (2009).
Rumfeldt, J.A.O., Lepock, J.R. and Meiering, E.M.* Unfolding and folding kinetics of amyotrophic lateral sclerosis-associated mutant Cu,Zn superoxide dismutases. Journal of Molecular Biology 385, 278-98 (2009).
Doxey, A.C., Lynch, M.D.J., Muller, K.M., Meiering, E.M. and McConkey, B.J.* Evolutionary origins of clostridial neurotoxins. BMC Evolutionary Biology 8, 316 (9 pages) (2008).
Meiering, E.M.* The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensity. PLoS Biology 6, e193 (2008).
Rumfeldt, J.A.O., Galvagnion, C., Vassall, K.A. and Meiering, E.M.* Conformational stability and folding mechanisms of dimeric proteins. Progress in Biophysics and Molecular Biology 98, 61-84 (2008).
Vassall, K.A., Stathopulos, P.B., Rumfeldt, J.A.O., Lepock, J.R. and Meiering, E.M.* Equilibrium thermodynamic analysis of amyotrophic lateral sclerosis-associated mutant apo Cu,Zn superoxide dismutases. Biochemistry 45, 7366-79 (2006).
Stathopulos, P.B., Rumfeldt, J.A.O., Siddall, C.A., Lepock, J.R., and Meiering, E.M.* Calorimetric analysis of thermodynamic stability and aggregation for apo and holo ALS-associated gly93 mutants of superoxide dismutase. Journal of Biological Chemistry 281, 6184-93 (2006).
Rumfeldt, J.A.O., Stathopulos, P.B., Chakrabartty, A., Lepock, J.R. and Meiering, E.M.* Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu,Zn superoxide dismutases. Journal of Molecular Biology 355, 106-123 (2006).
Gaspar, J.A., Liu, C., Vassall, K.A., Meglei, G., Stephen, R., Stathopulos, P.B., Pineda-Lucena, A., Wu, B., Yee, A., Arrowsmith, C.H. and Meiering, E.M.* A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 form Thermotoga maritima. Protein Science 14, 216-223 (2005).
Wong, H.J., Stathopulos, P.B., Bonner, J.M., Sawyer, M. and Meiering, E.M.* Nonlinear Effects of Temperature and Urea on the Thermodynamics and Kinetics of Folding and Unfolding of Hisactophilin. Journal of Molecular Biology344, 1089-1107 (2004).
Stathopulos, P.B., Scholz, G.A., Rumfeldt, J.A.O., Lepock, J.R. and Meiering, E.M.* Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Science 13, 3017-3027 (2004).
Stathopulos, P.B., Rumfeldt, J.A.O., Scholz, G.A., Irani, R.A., Frey, H.E., Hallewell, R.A., Lepock, J.R. and Meiering, E.M.* Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro. Proceedings of the National Academy of Sciences USA 100, 7021-7026 (2003).
Liu, C., Gaspar, J.A., Wong, H.J. and Meiering, E.M.*Conserved and nonconserved features of the folding pathway of hisactophilin, a b-trefoil protein. Protein Science 11, 669-679 (2002).
Houliston, R.S., Liu, C., Singh, L.M.R. and Meiering, E.M.* pH and urea dependence of amide hydrogen-deuterium exchange rates in b-trefoil protein hisactophilin. Biochemistry 41, 1182-94 (2002).
Liu, C., Chu, D., Wideman, R.D., Houliston, R.S., Wong, H.J. and Meiering, E.M.* Thermodynamics of denaturation of hisactophilin, a b-trefoil protein.Biochemistry 40, 3817-27 (2001).
Hammond, M.S., Houliston, R.S. and Meiering, E.M.* Two-dimensional 1H and 15N NMR titration studies of hisactophilin. Biochemistry and Cell Biology 76, 294-301 (1998).
Wilquet, V., Gaspar, J.A., van de Lande, M., van de Casteele, M., Legrain, C., Meiering, E.M. and Glandsorff, N.* Purification and characterization of recombinant Thermotoga maritima dihydrofolate reductase. European Journal of Biochemistry 255, 628-637 (1998).
Johnson, J.M., Meiering, E.M., Wright, J.E., Pardo, J., Rosowsky, A. and Wagner, G.* NMR solution structure of the antitumour compound PT523 and NADPH in the ternary complex with human dihydrofolate reductase. Biochemistry 36, 4399-4411 (1997).
Meiering, E.M., Li, H., Delcamp, T.J., Freisheim, J.H. and Wagner, G.* Contributions of tryptophan-24 and glutamate-30 to binding long-lived bound water molecules in the ternary complex of human dihydrofolate reductase with methotrexate and NADPH studied by site-directed mutagenesis and NMR. Journal of Molecular Biology 247, 309-325 (1995).
Meiering, E.M. and Wagner, G.* Detection of long-lived bound water molecules in complexes of human dihydrofolate reductase with methotrexate and NADPH. Journal of Molecular Biology 247, 294-308 (1995).
Anteneodo, C., Rodahl, A.M., Meiering, E., Heynen, M.L., Sennisterra, G.A. and Lepock, J.R.* Interaction of dibucaine with the transmembrane domain of the Ca2+-ATPase of sarcoplasmic reticulum. Biochemistry 33, 12283-12290 (1994).
Meiering, E.M., Bycroft, M. and Fersht, A.R.* The structure and dynamics of barnase complexed with 3’GMP studied by NMR spectroscopy. Biochemistry32, 10975-10987 (1993).
Meiering, E.M., Serrano, L. and Fersht, A.R.* Effect of active site residues in barnase on stability and activity. Journal of Molecular Biology 225, 585-589 (1992).
Matouschek, A., Serrano, L., Meiering, E.M., Bycroft, M. and Fersht, A.R.* The folding of an enzyme V. H/D exchange-NMR studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies. Journal of Molecular Biology 224, 837-845 (1992).
Meiering, E.M., Bycroft, M., and Fersht, A.R.* Characterization of phosphate binding to the ribonuclease barnase by site-directed mutagenesis and NMR. Biochemistry 30, 11348-11356 (1991).
Sancho, J., Meiering, E.M., and A.R. Fersht* Mapping transition states of protein folding by protein engineering of ligand binding sites. Journal of Molecular Biology 221, 1007-1014 (1991).
Anderson, A.*, Andrews, B., Meiering, E.M. and Torrie, B.H. Raman and far-infrared study of the lattice vibrations of methanol. Journal of Raman Spectroscopy 19, 85-91 (1988).