| Year |
Citation |
Score |
| 2023 |
Anderson DM, Jayanthi LP, Gosavi S, Meiering EM. Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity. Frontiers in Molecular Biosciences. 10: 1021733. PMID 36845544 DOI: 10.3389/fmolb.2023.1021733 |
0.358 |
|
| 2022 |
Deol HK, Broom HR, Siebeneichler B, Lee B, Leonenko Z, Meiering EM. Immature ALS-associated mutant superoxide dismutases form variable aggregate structures through distinct oligomerization processes. Biophysical Chemistry. 288: 106844. PMID 35872467 DOI: 10.1016/j.bpc.2022.106844 |
0.485 |
|
| 2022 |
Schaefer A, Naser D, Siebeneichler B, Tarasca MV, Meiering EM. Methodological advances and strategies for high resolution structure determination of cellular protein aggregates. The Journal of Biological Chemistry. 102197. PMID 35760099 DOI: 10.1016/j.jbc.2022.102197 |
0.384 |
|
| 2022 |
MacKenzie DWS, Schaefer A, Steckner J, Leo CA, Naser D, Artikis E, Broom A, Ko T, Shah P, Ney MQ, Tran E, Smith MTJ, Fuglestad B, Wand AJ, Brooks CL, ... Meiering EM, et al. A fine balance of hydrophobic-electrostatic communication pathways in a pH-switching protein. Proceedings of the National Academy of Sciences of the United States of America. 119: e2119686119. PMID 35737838 DOI: 10.1073/pnas.2119686119 |
0.35 |
|
| 2022 |
Tarasca MV, Naser D, Schaefer A, Soule TG, Meiering EM. Quenched hydrogen-deuterium amide exchange optimization for high-resolution structural analysis of cellular protein aggregates. Analytical Biochemistry. 114675. PMID 35390328 DOI: 10.1016/j.ab.2022.114675 |
0.42 |
|
| 2022 |
Naser D, Tarasca MV, Siebeneichler B, Schaefer A, Deol HK, Soule TGB, Almey J, Kelso S, Mishra GG, Simon H, Meiering EM. High-Resolution NMR H/D Exchange of Human Superoxide Dismutase Inclusion Bodies Reveals Significant Native Features Despite Structural Heterogeneity. Angewandte Chemie (International Ed. in English). e202112645. PMID 35316563 DOI: 10.1002/anie.202112645 |
0.434 |
|
| 2021 |
Trainor K, Doyle CM, Metcalfe-Roach A, Steckner J, Lipovšek D, Malakian H, Langley D, Krystek SR, Meiering EM. Design for Solubility May Reveal Induction of Amide Hydrogen/Deuterium Exchange by Protein Self-Association. Journal of Molecular Biology. 434: 167398. PMID 34902431 DOI: 10.1016/j.jmb.2021.167398 |
0.406 |
|
| 2020 |
Cveticanin J, Mondal T, Meiering EM, Sharon M, Horovitz A. Insight into the autosomal-dominant inheritance pattern of SOD1-associated ALS from native mass spectrometry. Journal of Molecular Biology. PMID 33058881 DOI: 10.1016/j.jmb.2020.09.025 |
0.312 |
|
| 2020 |
Semmler S, Gagné M, Garg P, Pickles SR, Baudouin C, Hamon-Keromen E, Destroismaisons L, Khalfallah Y, Chaineau M, Caron E, Bayne AN, Trempe JF, Cashman NR, Star AT, Haqqani AS, ... ... Meiering EM, et al. TNF receptor associated factor 6 interacts with ALS-linked misfolded superoxide dismutase 1 and promotes aggregation. The Journal of Biological Chemistry. PMID 32029478 DOI: 10.1074/Jbc.Ra119.011215 |
0.395 |
|
| 2019 |
Doyle C, Naser D, Bauman H, Rumfeldt J, Meiering E. Spectrophotometric method for simultaneous measurement of zinc and copper in metalloproteins using 4-(2-pyridylazo)resorcinol. Analytical Biochemistry. PMID 30904440 DOI: 10.1016/j.ab.2019.03.007 |
0.728 |
|
| 2018 |
Culik RM, Sekhar A, Nagesh J, Deol H, Rumfeldt JAO, Meiering EM, Kay LE. Effects of maturation on the conformational free-energy landscape of SOD1. Proceedings of the National Academy of Sciences of the United States of America. PMID 29483249 DOI: 10.1073/Pnas.1721022115 |
0.784 |
|
| 2017 |
Broom A, Jacobi Z, Trainor K, Meiering EM. Computational tools help improve protein stability but with a solubility tradeoff. The Journal of Biological Chemistry. 292: 14349-14361. PMID 28710274 DOI: 10.1074/jbc.M117.784165 |
0.374 |
|
| 2017 |
Trainor K, Broom A, Meiering EM. Exploring the relationships between protein sequence, structure and solubility. Current Opinion in Structural Biology. 42: 136-146. PMID 28160724 DOI: 10.1016/j.sbi.2017.01.004 |
0.329 |
|
| 2016 |
Sekhar A, Rumfeldt JA, Broom HR, Doyle CM, Sobering RE, Meiering EM, Kay LE. Probing the free energy landscapes of ALS disease mutants of SOD1 by NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America. PMID 27791136 DOI: 10.1073/Pnas.1611418113 |
0.775 |
|
| 2016 |
Pickles S, Semmler S, Broom HR, Destroismaisons L, Legroux L, Arbour N, Meiering E, Cashman NR, Vande Velde C. ALS-linked misfolded SOD1 species have divergent impacts on mitochondria. Acta Neuropathologica Communications. 4: 43. PMID 27121871 DOI: 10.1186/S40478-016-0313-8 |
0.407 |
|
| 2016 |
Trainor K, Gingras Z, Shillingford C, Malakian H, Gosselin M, Lipovšek D, Meiering EM. Ensemble Modeling and Intracellular Aggregation of an Engineered Immunoglobulin-Like Domain. Journal of Molecular Biology. 428: 1365-74. PMID 26903090 DOI: 10.1016/j.jmb.2016.02.016 |
0.377 |
|
| 2016 |
Doyle CM, Rumfeldt JA, Broom HR, Sekhar A, Kay LE, Meiering EM. 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. PMID 26849066 DOI: 10.1021/Acs.Biochem.5B01133 |
0.762 |
|
| 2015 |
Broom HR, Vassall KA, Rumfeldt JA, Doyle CM, Tong MS, Bonner JM, Meiering EM. 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. PMID 26710831 DOI: 10.1021/acs.biochem.5b01187 |
0.781 |
|
| 2015 |
Broom A, Ma SM, Xia K, Rafalia H, Trainor K, Colón W, Gosavi S, Meiering EM. Designed protein reveals structural determinants of extreme kinetic stability. Proceedings of the National Academy of Sciences of the United States of America. PMID 26554002 DOI: 10.1073/Pnas.1510748112 |
0.342 |
|
| 2015 |
Broom HR, Rumfeldt JA, Vassall KA, Meiering EM. Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1. Protein Science : a Publication of the Protein Society. 24: 2081-9. PMID 26362407 DOI: 10.1002/pro.2803 |
0.798 |
|
| 2015 |
Sekhar A, Bain AD, Rumfeldt JA, Meiering EM, Kay LE. Evolution of magnetization due to asymmetric dimerization: theoretical considerations and application to aberrant oligomers formed by apoSOD1(2SH). Physical Chemistry Chemical Physics : Pccp. PMID 26156673 DOI: 10.1039/C5Cp03044G |
0.691 |
|
| 2015 |
Sekhar A, Rumfeldt JA, Broom HR, Doyle CM, Bouvignies G, Meiering EM, Kay LE. Thermal fluctuations of immature SOD1 lead to separate folding and misfolding pathways. Elife. 4. PMID 26099300 DOI: 10.7554/Elife.07296 |
0.765 |
|
| 2015 |
Broom A, Gosavi S, Meiering EM. Protein unfolding rates correlate as strongly as folding rates with native structure. Protein Science : a Publication of the Protein Society. 24: 580-7. PMID 25422093 DOI: 10.1002/pro.2606 |
0.332 |
|
| 2015 |
Kay L, Sekhar A, Rumfeldt J, Broom H, Doyle C, Meiering E. Backbone and sidechain 1H, 13C and 15N chemical shifts for human superoxide dismutase (hSOD1) lacking bound metal and the intrasubunit disulfide bond Journal of Back and Musculoskeletal Rehabilitation. DOI: 10.13018/Bmr26570 |
0.692 |
|
| 2015 |
Broom A, Gosavi S, Meiering EM. Protein unfolding rates correlate as strongly as folding rates with native structure Protein Science. 24: 580-587. DOI: 10.1002/pro.2606 |
0.338 |
|
| 2014 |
Broom HR, Rumfeldt JA, Meiering EM. 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. PMID 25131593 DOI: 10.1042/bse0560149 |
0.756 |
|
| 2013 |
Doyle CM, Rumfeldt JA, Broom HR, Broom A, Stathopulos PB, Vassall KA, Almey JJ, Meiering EM. Energetics of oligomeric protein folding and association. Archives of Biochemistry and Biophysics. 531: 44-64. PMID 23246784 DOI: 10.1016/j.abb.2012.12.005 |
0.753 |
|
| 2012 |
Shental-Bechor D, Smith MT, Mackenzie D, Broom A, Marcovitz A, Ghashut F, Go C, Bralha F, Meiering EM, Levy Y. Nonnative interactions regulate folding and switching of myristoylated protein. Proceedings of the National Academy of Sciences of the United States of America. 109: 17839-44. PMID 22847411 DOI: 10.1073/pnas.1201803109 |
0.399 |
|
| 2011 |
Vassall KA, Stubbs HR, Primmer HA, Tong MS, Sullivan SM, Sobering R, Srinivasan S, Briere LA, Dunn SD, Colón W, Meiering EM. 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 of the United States of America. 108: 2210-5. PMID 21257910 DOI: 10.1073/Pnas.0913021108 |
0.489 |
|
| 2010 |
Smith MT, Meissner J, Esmonde S, Wong HJ, Meiering EM. Energetics and mechanisms of folding and flipping the myristoyl switch in the {beta}-trefoil protein, hisactophilin. Proceedings of the National Academy of Sciences of the United States of America. 107: 20952-7. PMID 21097705 DOI: 10.1073/pnas.1008026107 |
0.34 |
|
| 2010 |
Hwang YM, Stathopulos PB, Dimmick K, Yang H, Badiei HR, Tong MS, Rumfeldt JA, Chen P, Karanassios V, Meiering EM. Nonamyloid aggregates arising from mature copper/zinc superoxide dismutases resemble those observed in amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 285: 41701-11. PMID 20974846 DOI: 10.1074/Jbc.M110.113696 |
0.758 |
|
| 2009 |
Galvagnion C, Smith MT, Broom A, Vassall KA, Meglei G, Gaspar JA, Stathopulos PB, Cheyne B, Meiering EM. Folding and association of thermophilic dimeric and trimeric DsrEFH proteins: Tm0979 and Mth1491. Biochemistry. 48: 2891-906. PMID 19290646 DOI: 10.1021/bi801784d |
0.45 |
|
| 2009 |
Rumfeldt JA, Lepock JR, Meiering EM. Unfolding and folding kinetics of amyotrophic lateral sclerosis-associated mutant Cu,Zn superoxide dismutases. Journal of Molecular Biology. 385: 278-98. PMID 18951903 DOI: 10.1016/j.jmb.2008.10.003 |
0.801 |
|
| 2008 |
Meiering EM. The threat of instability: neurodegeneration predicted by protein destabilization and aggregation propensity. Plos Biology. 6: e193. PMID 18666836 DOI: 10.1371/journal.pbio.0060193 |
0.308 |
|
| 2008 |
Rumfeldt JA, Galvagnion C, Vassall KA, Meiering EM. Conformational stability and folding mechanisms of dimeric proteins. Progress in Biophysics and Molecular Biology. 98: 61-84. PMID 18602415 DOI: 10.1016/j.pbiomolbio.2008.05.004 |
0.746 |
|
| 2006 |
Vassall KA, Stathopulos PB, Rumfeldt JA, Lepock JR, Meiering EM. Equilibrium thermodynamic analysis of amyotrophic lateral sclerosis-associated mutant apo Cu,Zn superoxide dismutases. Biochemistry. 45: 7366-79. PMID 16752926 DOI: 10.1021/bi0600953 |
0.796 |
|
| 2006 |
Stathopulos PB, Rumfeldt JA, Karbassi F, Siddall CA, Lepock JR, Meiering EM. Calorimetric analysis of thermodynamic stability and aggregation for apo and holo amyotrophic lateral sclerosis-associated Gly-93 mutants of superoxide dismutase. The Journal of Biological Chemistry. 281: 6184-93. PMID 16407238 DOI: 10.1074/jbc.M509496200 |
0.77 |
|
| 2006 |
Rumfeldt JA, Stathopulos PB, Chakrabarrty A, Lepock JR, Meiering EM. Mechanism and thermodynamics of guanidinium chloride-induced denaturation of ALS-associated mutant Cu,Zn superoxide dismutases. Journal of Molecular Biology. 355: 106-23. PMID 16307756 DOI: 10.1016/j.jmb.2005.10.042 |
0.805 |
|
| 2005 |
Gaspar JA, Liu C, Vassall KA, Meglei G, Stephen R, Stathopulos PB, Pineda-Lucena A, Wu B, Yee A, Arrowsmith CH, Meiering EM. A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 from Thermotoga maritima. Protein Science : a Publication of the Protein Society. 14: 216-23. PMID 15608123 DOI: 10.1110/ps.041068605 |
0.371 |
|
| 2004 |
Wong HJ, Stathopulos PB, Bonner JM, Sawyer M, Meiering EM. Non-linear effects of temperature and urea on the thermodynamics and kinetics of folding and unfolding of hisactophilin. Journal of Molecular Biology. 344: 1089-107. PMID 15544814 DOI: 10.1016/j.jmb.2004.09.091 |
0.375 |
|
| 2004 |
Stathopulos PB, Scholz GA, Hwang YM, Rumfeldt JA, Lepock JR, Meiering EM. Sonication of proteins causes formation of aggregates that resemble amyloid. Protein Science : a Publication of the Protein Society. 13: 3017-27. PMID 15459333 DOI: 10.1110/ps.04831804 |
0.743 |
|
| 2003 |
Stathopulos PB, Rumfeldt JAO, Scholz GA, Irani RA, Frey HE, Hallewell RA, Lepock JR, Meiering EM. Cu/Zn superoxide dismutase mutants associated with amyotrophic lateral sclerosis show enhanced formation of aggregates in vitro Proceedings of the National Academy of Sciences of the United States of America. 100: 7021-7026. PMID 12773627 DOI: 10.1073/pnas.1237797100 |
0.504 |
|
| 1997 |
Johnson JM, Meiering EM, Wright JE, Pardo J, Rosowsky A, Wagner G. NMR solution structure of the antitumor compound PT523 and NADPH in the ternary complex with human dihydrofolate reductase. Biochemistry. 36: 4399-411. PMID 9109647 DOI: 10.1021/bi963039i |
0.404 |
|
| 1995 |
Meiering EM, Li H, Delcamp TJ, Freisheim JH, Wagner G. Contributions of tryptophan 24 and glutamate 30 to binding long-lived water molecules in the ternary complex of human dihydrofolate reductase with methotrexate and NADPH studied by site-directed mutagenesis and nuclear magnetic resonance spectroscopy. Journal of Molecular Biology. 247: 309-25. PMID 7707377 DOI: 10.1006/Jmbi.1994.0141 |
0.673 |
|
| 1995 |
Meiering EM, 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. PMID 7707376 DOI: 10.1006/Jmbi.1994.0140 |
0.405 |
|
| 1994 |
Anteneodo C, Rodahl AM, Meiering E, Heynen ML, Sennisterra GA, Lepock JR. Interaction of Dibucaine with the Transmembrane Domain of the Ca2+-ATPase of Sarcoplasmic Reticulum Biochemistry. 33: 12283-12290. PMID 7918449 DOI: 10.1021/Bi00206A035 |
0.396 |
|
| 1993 |
Meiering EM, Bycroft M, Lubienski MJ, Fersht AR. Structure and dynamics of barnase complexed with 3'-GMP studied by NMR spectroscopy Biochemistry. 32: 10975-10987. PMID 8218163 DOI: 10.1021/Bi00092A006 |
0.473 |
|
| 1992 |
Matouschek A, Serrano L, Meiering EM, Bycroft M, Fersht AR. The folding of an enzyme. V. H/2H exchange-nuclear magnetic resonance studies on the folding pathway of barnase: complementarity to and agreement with protein engineering studies. Journal of Molecular Biology. 224: 837-45. PMID 1569560 DOI: 10.1016/0022-2836(92)90565-2 |
0.328 |
|
| 1991 |
Meiering EM, Bycroft M, Fersht AR. Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR. Biochemistry. 30: 11348-11356. PMID 1958671 DOI: 10.1021/Bi00111A022 |
0.449 |
|
| 1991 |
Sancho J, Meiering EM, Fersht AR. Mapping transition states of protein unfolding by protein engineering of ligand-binding sites. Journal of Molecular Biology. 221: 1007-1014. PMID 1658330 DOI: 10.1016/0022-2836(91)80188-Z |
0.667 |
|
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