Year |
Citation |
Score |
2023 |
Bertrand Q, Coquille S, Iorio A, Sterpone F, Madern D. Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from Selenomonas ruminantium provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family of lactate and malate dehydrogenases. Journal of Structural Biology. 215: 108039. PMID 37884067 DOI: 10.1016/j.jsb.2023.108039 |
0.349 |
|
2023 |
Robin AY, Brochier-Armanet C, Bertrand Q, Barette C, Girard E, Madern D. Deciphering Evolutionary Trajectories of Lactate Dehydrogenases Provides New Insights into Allostery. Molecular Biology and Evolution. 40. PMID 37797308 DOI: 10.1093/molbev/msad223 |
0.344 |
|
2022 |
Iorio A, Brochier-Armanet C, Mas C, Sterpone F, Madern D. Protein Conformational Space at the Edge of Allostery: Turning a Non-allosteric Malate Dehydrogenase into an "Allosterized" Enzyme using Evolution Guided Punctual Mutations. Molecular Biology and Evolution. PMID 36056899 DOI: 10.1093/molbev/msac186 |
0.33 |
|
2021 |
Iorio A, Roche J, Engilberge S, Coquelle N, Girard E, Sterpone F, Madern D. Biochemical, structural and dynamical studies reveal strong differences in the thermal-dependent allosteric behavior of two extremophilic lactate dehydrogenases. Journal of Structural Biology. 107769. PMID 34229075 DOI: 10.1016/j.jsb.2021.107769 |
0.332 |
|
2021 |
Blanquart S, Groussin M, Le Roy A, Szöllosi GJ, Girard E, Franzetti B, Gouy M, Madern D. Resurrection of Ancestral Malate Dehydrogenases Reveals the Evolutionary History of Halobacterial Proteins : Deciphering Gene Trajectories and Changes in Biochemical Properties. Molecular Biology and Evolution. PMID 33974066 DOI: 10.1093/molbev/msab146 |
0.305 |
|
2020 |
Timr S, Madern D, Sterpone F. Protein thermal stability. Progress in Molecular Biology and Translational Science. 170: 239-272. PMID 32145947 DOI: 10.1016/bs.pmbts.2019.12.007 |
0.323 |
|
2020 |
Halgand F, Houée-Lévin C, Weik M, Madern D. Remote oxidative modifications induced by oxygen free radicals modify T/R allosteric equilibrium of a hyperthermophilic lactate dehydrogenase. Journal of Structural Biology. 107478. PMID 32087239 DOI: 10.1016/J.Jsb.2020.107478 |
0.605 |
|
2020 |
Katava M, Marchi M, Madern D, Sztucki M, Maccarini M, Sterpone F. Temperature Unmasks Allosteric Propensity in a Thermophilic Malate Dehydrogenase via Dewetting and Collapse. The Journal of Physical Chemistry. B. PMID 31961162 DOI: 10.1021/acs.jpcb.9b10776 |
0.318 |
|
2019 |
Roche J, Girard E, Mas C, Madern D. The archaeal LDH-like malate dehydrogenase from Ignicoccus islandicus displays dual substrate recognition, hidden allostery and a non-canonical tetrameric oligomeric organization. Journal of Structural Biology. PMID 31301348 DOI: 10.1016/j.jsb.2019.07.006 |
0.326 |
|
2017 |
Katava M, Maccarini M, Villain G, Paciaroni A, Sztucki M, Ivanova O, Madern D, Sterpone F. Thermal activation of 'allosteric-like' large-scale motions in a eukaryotic Lactate Dehydrogenase. Scientific Reports. 7: 41092. PMID 28112231 DOI: 10.1038/Srep41092 |
0.349 |
|
2016 |
Kim HS, Martel A, Girard E, Moulin M, Härtlein M, Madern D, Blackledge M, Franzetti B, Gabel F. SAXS/SANS on Supercharged Proteins Reveals Residue-Specific Modifications of the Hydration Shell. Biophysical Journal. 110: 2185-2194. PMID 27224484 DOI: 10.1016/j.bpj.2016.04.013 |
0.616 |
|
2016 |
Lassalle L, Engilberge S, Madern D, Vauclare P, Franzetti B, Girard E. New insights into the mechanism of substrates trafficking in Glyoxylate/Hydroxypyruvate reductases. Scientific Reports. 6: 20629. PMID 26865263 DOI: 10.1038/srep20629 |
0.306 |
|
2014 |
Kalimeri M, Girard E, Madern D, Sterpone F. Interface matters: the stiffness route to stability of a thermophilic tetrameric malate dehydrogenase. Plos One. 9: e113895. PMID 25437494 DOI: 10.1371/Journal.Pone.0113895 |
0.367 |
|
2014 |
Vauclare P, Madern D, Girard E, Gabel F, Zaccai G, Franzetti B. New insights into microbial adaptation to extreme saline environments Bio Web of Conferences. 2: 02001. DOI: 10.1051/BIOCONF/20140202001 |
0.521 |
|
2012 |
Colletier JP, Aleksandrov A, Coquelle N, Mraihi S, Mendoza-Barberá E, Field M, Madern D. Sampling the conformational energy landscape of a hyperthermophilic protein by engineering key substitutions. Molecular Biology and Evolution. 29: 1683-94. PMID 22319152 DOI: 10.1093/Molbev/Mss015 |
0.649 |
|
2010 |
Coquelle N, Talon R, Juers DH, Girard E, Kahn R, Madern D. Gradual adaptive changes of a protein facing high salt concentrations. Journal of Molecular Biology. 404: 493-505. PMID 20888835 DOI: 10.1016/J.Jmb.2010.09.055 |
0.373 |
|
2009 |
Fabiani E, Stadler ÆAM, Madern D, Koza MM, Tehei M, Hirai M, Zaccai G. Dynamics of apomyoglobin in the α-to-β transition and of partially unfolded aggregated protein European Biophysics Journal. 38: 237-244. PMID 18853152 DOI: 10.1007/S00249-008-0375-Z |
0.603 |
|
2007 |
Coquelle N, Fioravanti E, Weik M, Vellieux F, Madern D. Activity, stability and structural studies of lactate dehydrogenases adapted to extreme thermal environments. Journal of Molecular Biology. 374: 547-62. PMID 17936781 DOI: 10.1016/J.Jmb.2007.09.049 |
0.643 |
|
2007 |
Madern D, Ebel C. Influence of an anion-binding site in the stabilization of halophilic malate dehydrogenase from Haloarcula marismortui. Biochimie. 89: 981-7. PMID 17451860 DOI: 10.1016/j.biochi.2007.03.008 |
0.304 |
|
2007 |
Fioravanti E, Vellieux FM, Amara P, Madern D, Weik M. Specific radiation damage to acidic residues and its relation to their chemical and structural environment. Journal of Synchrotron Radiation. 14: 84-91. PMID 17211074 DOI: 10.1107/S0909049506038623 |
0.56 |
|
2006 |
Karlström M, Steen IH, Madern D, Fedöy AE, Birkeland NK, Ladenstein R. The crystal structure of a hyperthermostable subfamily II isocitrate dehydrogenase from Thermotoga maritima. The Febs Journal. 273: 2851-68. PMID 16759231 DOI: 10.1111/j.1742-4658.2006.05298.x |
0.353 |
|
2006 |
Gabel F, Wang D, Madern D, Sadler A, Dayie K, Daryoush MZ, Schwahn D, Zaccai G, Lee X, Williams BR. Dynamic flexibility of double-stranded RNA activated PKR in solution. Journal of Molecular Biology. 359: 610-23. PMID 16650856 DOI: 10.1016/J.Jmb.2006.03.049 |
0.609 |
|
2005 |
Tehei M, Madern D, Franzetti B, Zaccai G. Neutron scattering reveals the dynamic basis of protein adaptation to extreme temperature. The Journal of Biological Chemistry. 280: 40974-9. PMID 16203729 DOI: 10.1074/Jbc.M508417200 |
0.677 |
|
2005 |
Fioravanti E, Vellieux FMD, Madern D, Weik M. Lactate dehydrogenases from extremophile organisms: clues for radio-resistance? Acta Crystallographica Section A. 61: 267-267. DOI: 10.1107/S0108767305088616 |
0.478 |
|
2004 |
Madern D, Camacho M, RodrÃguez-Arnedo A, Bonete MJ, Zaccai G. Salt-dependent studies of NADP-dependent isocitrate dehydrogenase from the halophilic archaeon Haloferax volcanii. Extremophiles : Life Under Extreme Conditions. 8: 377-84. PMID 15221656 DOI: 10.1007/S00792-004-0398-Z |
0.319 |
|
2004 |
Madern D, Zaccai G. Molecular adaptation: the malate dehydrogenase from the extreme halophilic bacterium Salinibacter ruber behaves like a non-halophilic protein. Biochimie. 86: 295-303. PMID 15194233 DOI: 10.1016/J.Biochi.2004.04.004 |
0.315 |
|
2004 |
Irimia A, Madern D, Zaccaï G, Vellieux FM. Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes. The Embo Journal. 23: 1234-44. PMID 15014443 DOI: 10.1038/Sj.Emboj.7600147 |
0.696 |
|
2004 |
Tehei M, Franzetti B, Madern D, Ginzburg M, Ginzburg BZ, Giudici-Orticoni MT, Bruschi M, Zaccai G. Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering. Embo Reports. 5: 66-70. PMID 14710189 DOI: 10.1038/Sj.Embor.7400049 |
0.627 |
|
2004 |
Irimia A, Vellieux FM, Madern D, Zaccaï G, Karshikoff A, Tibbelin G, Ladenstein R, Lien T, Birkeland NK. The 2.9A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation. Journal of Molecular Biology. 335: 343-56. PMID 14659762 DOI: 10.1016/J.Jmb.2003.10.054 |
0.703 |
|
2003 |
Irimia A, Ebel C, Madern D, Richard SB, Cosenza LW, Zaccaï G, Vellieux FM. The Oligomeric states of Haloarcula marismortui malate dehydrogenase are modulated by solvent components as shown by crystallographic and biochemical studies. Journal of Molecular Biology. 326: 859-73. PMID 12581646 DOI: 10.1016/S0022-2836(02)01450-X |
0.691 |
|
2001 |
Tehei M, Madern D, Pfister C, Zaccai G. Fast dynamics of halophilic malate dehydrogenase and BSA measured by neutron scattering under various solvent conditions influencing protein stability Proceedings of the National Academy of Sciences of the United States of America. 98: 14356-14361. PMID 11734642 DOI: 10.1073/Pnas.251537298 |
0.66 |
|
2000 |
Madern D, Ebel C, Zaccai G. Halophilic adaptation of enzymes. Extremophiles. 4: 91-98. PMID 10805563 DOI: 10.1007/S007920050142 |
0.357 |
|
2000 |
Madern D, Ebel C, Mevarech M, Richard SB, Pfister C, Zaccai G. Insights into the molecular relationships between malate and lactate dehydrogenases: structural and biochemical properties of monomeric and dimeric intermediates of a mutant of tetrameric L-[LDH-like] malate dehydrogenase from the halophilic archaeon Haloarcula marismortui. Biochemistry. 39: 1001-1010. PMID 10653644 DOI: 10.1021/Bi9910023 |
0.393 |
|
2000 |
Richard SB, Madern D, Garcin E, Zaccai G. Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry. 39: 992-1000. PMID 10653643 DOI: 10.1021/Bi991001A |
0.387 |
|
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