| Year |
Citation |
Score |
| 2023 |
Kurttila M, Rumfeldt J, Takala H, Ihalainen JA. The interconnecting hairpin extension "arm": An essential allosteric element of phytochrome activity. Structure (London, England : 1993). PMID 37392739 DOI: 10.1016/j.str.2023.06.007 |
0.682 |
|
| 2022 |
Kurttila M, Etzl S, Rumfeldt J, Takala H, Galler N, Winkler A, Ihalainen JA. The structural effect between the output module and chromophore-binding domain is a two-way street via the hairpin extension. Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society For Photobiology. PMID 35984631 DOI: 10.1007/s43630-022-00265-5 |
0.656 |
|
| 2022 |
Lehtivuori H, Rumfeldt J, Mustalahti S, Kurkinen S, Takala H. Conserved histidine and tyrosine determine spectral responses through the water network in Deinococcus radiodurans phytochrome. Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society For Photobiology. PMID 35906527 DOI: 10.1007/s43630-022-00272-6 |
0.656 |
|
| 2021 |
Rumfeldt J, Kurttila M, Takala H, Ihalainen JA. The hairpin extension controls solvent access to the chromophore binding pocket in a bacterial phytochrome: a UV-vis absorption spectroscopy study. Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society For Photobiology. 20: 1173-1181. PMID 34460093 DOI: 10.1007/s43630-021-00090-2 |
0.716 |
|
| 2021 |
Kurttila M, Stucki-Buchli B, Rumfeldt J, Schroeder L, Häkkänen H, Liukkonen A, Takala H, Kottke T, Ihalainen JA. Site-by-site tracking of signal transduction in an azidophenylalanine-labeled bacteriophytochrome with step-scan FTIR spectroscopy. Physical Chemistry Chemical Physics : Pccp. 23: 5615-5628. PMID 33656023 DOI: 10.1039/d0cp06553f |
0.667 |
|
| 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 |
0.641 |
|
| 2019 |
Rumfeldt JA, Takala H, Liukkonen A, Ihalainen JA. UV-Vis Spectroscopy Reveals a Correlation Between Y263 and BV Protonation States in Bacteriophytochromes. Photochemistry and Photobiology. 95: 969-979. PMID 30843203 DOI: 10.1111/Php.13095 |
0.675 |
|
| 2018 |
Lenngren N, Edlund P, Takala H, Stucki-Buchli B, Rumfeldt J, Peshev I, Häkkänen H, Westenhoff S, Ihalainen JA. Coordination of the biliverdin D-ring in bacteriophytochromes. Physical Chemistry Chemical Physics : Pccp. 20: 18216-18225. PMID 29938729 DOI: 10.1039/C8Cp01696H |
0.712 |
|
| 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 |
0.709 |
|
| 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 |
0.704 |
|
| 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 |
0.69 |
|
| 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 |
0.709 |
|
| 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 |
0.722 |
|
| 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 |
0.611 |
|
| 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 |
0.689 |
|
| 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 |
0.62 |
|
| 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 |
0.665 |
|
| 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 |
0.679 |
|
| 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 |
0.664 |
|
| 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 |
0.719 |
|
| 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 |
0.675 |
|
| 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 |
0.717 |
|
| 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 |
0.688 |
|
| 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 |
0.729 |
|
| 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 |
0.663 |
|
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