Publications

  • Schaefer, A., Naser, D., Siebeneichler, B., Tarasca, M.V., and Meiering, E.M.* Methodological advances and strategies for high resolution structure determination of cellular protein aggregates. J. Biol. Chem. (Online ahead of print). doi: 10.1016/j.jbc.2022.102197
  • 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 of hydrophobic-electrostatic communication pathways in a pH- switching protein. Proceedings of the National Academy of Sciences USA 119 e2119686119 (2022). doi: 10.1073/pnas.2119686119
  • 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 61 e202112645 (2022). doi: 10.1002/anie.202112645
  • Sankar, K., Trainor, K., Blazer, L.L., Adams, J.J., Sidhu, S.S., Day, T., Meiering, E.M., and Maier, J.K.X.* A descriptor set for quantitative structure-property relationship prediction in biologics. Mol. Inform. e2100240 (2022). doi: 10.1002/minf.202100240
  • Tarasca, M.V., Naser, D., Schaefer, A., Soule, T.G.B., and Meiering, E.M.* Quenched hydrogen-deuterium amide echange optimization for high-resolution structural analysis of cellular protein aggregates. Analytical Biochem. 652, 114675 (2022). doi: 10.1016/j.ab.2022.114675
  • 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 167398 (2022). doi: 10.1016/j.jmb.2021.167398
  • 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).