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).
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 Chemistry295, 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. Neurochem00, 1-15 (2020). doi: 10.1111/jnc.15126.
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. Biochemistry55, 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, 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 Science24, 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 Phys18, 5720-8 (2015).
Broom, A., Gosavi, S., and Meiering, E.M.* Protein unfolding rates correlate as strongly as folding rates with native structure. Protein Science24, 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. eLife4, 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 Biochemistry56, 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 Physics138, 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 Biophysics531, 44-64 (2013).
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 Society134, 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. Structure20, 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)
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. Biochemistry48, 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 Biology385, 278-98 (2009).
Meiering, E.M.* The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensity. PLoS Biology6, e193 (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. Biochemistry45, 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 Chemistry281, 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 Biology355, 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 Science14, 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 Science13, 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 USA100, 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 Science11, 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. Biochemistry41, 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.Biochemistry40, 3817-27 (2001).
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 Biochemistry255, 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. Biochemistry36, 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 Biology247, 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 Biology247, 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. Biochemistry33, 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).
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 Biology224, 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. Biochemistry30, 11348-11356 (1991).