Publicaciones

Año 2020

  • Risso VA, Romero-Rivera A, Gutierrez-Rus LI, Ortega-Muñoz M, Santoyo-Gonzalez F, Gavira JA, Sanchez-Ruiz JM, Kamerlin SCL (2020). “Enhancing a de novo enzyme activity by computationally-focused ultra-low-throughput screening”. Chem Sci 19, 6134-6148.

  • Bernardo J Gomez-Fernandez, Valeria A Risso, Andres Rueda, Jose M Sanchez-Ruiz, Miguel Alcalde (2020). “Ancestral resurrection and directed evolution of fungal mesozoic laccases”. Applied and environmental microbiology 86 (14).

  • Bernardo J Gomez-Fernandez, Valeria A Risso, Jose M Sanchez-Ruiz, Miguel Alcalde (2020). “Consensus design of an evolved high-redox potential laccase”. Frontiers in Bioengineering and Biotechnology 8, 354.

  • Jasmine M Gardner, Michal Biler, Valeria A Risso, Jose M Sanchez-Ruiz, Shina CL Kamerlin (2020). “Manipulating conformational dynamics to repurpose ancient proteins for modern catalytic functions”. ACS Catalysis 10 (9), 4863-4870.

Año 2019

  • Campos LA, Sharma R, Alvira S, Ruiz FM, Ibarra-Molero B, Sadqi M, Alfonso C, Rivas G, Sanchez-Ruiz JM, Romero-Garrido A, Valpuesta JM, Muñoz V (2019). “Engineering protein assemblies with allosteric control via monomer fold-switching”. Nature Communications 13, 5703.

  • Gamiz-Arco G, Risso VA, Candel AM, Inglés-Prieto A, Romero-Romero ML, Gaucher EA, Gavira JA, Ibarra-Molero B, Sanchez-Ruiz JM (2019). “Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding”. Biochem J 12 (23), 3631-3647.

Año 2018

  • Risso, V.A., Sanchez-Ruiz, J.M., and Ozkan, S.B. (2018). Biotechnological and protein-engineering implications of ancestral protein resurrection. Curr. Opin. Struct. Biol. 51, 106–115.

  • Petrović, D., Risso, V.A., Kamerlin, S.C.L., and Sanchez-Ruiz, J.M. (2018). Conformational dynamics and enzyme evolution. J. R. Soc. Interface 15.

  • Gomez-Fernandez, B.J., Garcia-Ruiz, E., Martin-Diaz, J., Gomez de Santos, P., Santos-Moriano, P., Plou, F.J., Ballesteros, A., Garcia, M., Rodriguez, M., Risso, V.A., et al. (2018). Directed -in vitro- evolution of Precambrian and extant Rubiscos. Sci. Rep. 8, 5532.

  • Pabis, A., Risso, V.A., Sanchez-Ruiz, J.M., and Kamerlin, S.C. (2018). Cooperativity and flexibility in enzyme evolution. Curr. Opin. Struct. Biol. 48, 83–92.

  • Martín-Escolano, R., Moreno-Viguri, E., Santivañez-Veliz, M., Martin-Montes, A., Medina-Carmona, E., Paucar, R., Marín, C., Azqueta, A., Cirauqui, N., Pey, A.L., et al. (2018). Second Generation of Mannich Base-Type Derivatives with in Vivo Activity against Trypanosoma cruzi. J. Med. Chem. 61, 5643–5663.

  • McAuley, M., Mesa-Torres, N., McFall, A., Morris, S., Huang, M., Pey, A.L., and Timson, D.J. (2018). Improving the Activity and Stability of Human Galactokinase for Therapeutic and Biotechnological Applications. ChemBioChem 19, 1088–1095.

  • Medina-Carmona, E., Betancor-Fernández, I., Santos, J., Mesa-Torres, N., Grottelli, S., Batlle, C., Naganathan, A.N., Oppici, E., Cellini, B., Ventura, S., et al. (2018a). Insight into the specificity and severity of pathogenic mechanisms associated with missense mutations through experimental and structural perturbation analyses. Hum. Mol. Genet.

  • Medina-Carmona, E., Rizzuti, B., Martín-Escolano, R., Pacheco-García, J.L., Mesa-Torres, N., Neira, J.L., Guzzi, R., and Pey, A.L. (2018b). Phosphorylation compromises FAD binding and intracellular stability of wild-type and cancer-associated NQO1: Insights into flavo-proteome stability. Int. J. Biol. Macromol.

  • Mesa-Torres, N., Betancor-Fernández, I., Oppici, E., Cellini, B., Salido, E., Pey, A., Mesa-Torres, N., Betancor-Fernández, I., Oppici, E., Cellini, B., et al. (2018). Evolutionary Divergent Suppressor Mutations in Conformational Diseases. Genes (Basel). 9, 352.

  • Pey, A.L. (2018). Biophysical and functional perturbation analyses at cancer-associated P187 and K240 sites of the multifunctional NADP(H):quinone oxidoreductase 1. Int. J. Biol. Macromol. 118, 1912–1923.

Año 2017

  • Betancor-Fernández, I., Timson, D.J., Salido, E., and Pey, A.L. (2017). Natural (and Unnatural) Small Molecules as Pharmacological Chaperones and Inhibitors in Cancer. (Springer, Cham), pp. 155–190.

  • Clavería-Gimeno, R., Velazquez-Campoy, A., and Pey, A.L. (2017). Thermodynamics of cooperative binding of FAD to human NQO1: Implications to understanding cofactor-dependent function and stability of the flavoproteome. Arch. Biochem. Biophys. 636, 17–27.

  • Majtan, T., Pey, A.L., Gimenez-Mascarell, P., Martínez-Cruz, L.A., Szabo, C., Kožich, V., and Kraus, J.P. (2017). Potential Pharmacological Chaperones for Cystathionine Beta-Synthase-Deficient Homocystinuria. (Springer, Cham), pp. 345–383.

  • Medina-Carmona, E., Fuchs, J.E., Gavira, J.A., Mesa-Torres, N., Neira, J.L., Salido, E., Palomino-Morales, R., Burgos, M., Timson, D.J., and Pey, A.L. (2017). Enhanced vulnerability of human proteins towards disease-associated inactivation through divergent evolution. Hum. Mol. Genet. 26, 3531–3544.

  • Muñoz, I.G., Morel, B., Medina-Carmona, E., and Pey, A.L. (2017). A mechanism for cancer-associated inactivation of NQO1 due to P187S and its reactivation by the consensus mutation H80R. FEBS Lett. 591, 2826–2835.

  • Santofimia-Castaño, P., Rizzuti, B., Pey, Á.L., Soubeyran, P., Vidal, M., Urrutia, R., Iovanna, J.L., and Neira, J.L. (2017). Intrinsically disordered chromatin protein NUPR1 binds to the C-terminal region of Polycomb RING1B. Proc. Natl. Acad. Sci. U. S. A. 114, E6332–E6341.

  • Risso, V.A., Martinez-Rodriguez, S., Candel, A.M., Krüger, D.M., Pantoja-Uceda, D., Ortega-Muñoz, M., Santoyo-Gonzalez, F., Gaucher, E.A., Kamerlin, S.C.L., Bruix, M., et al. (2017). De novo active sites for resurrected Precambrian enzymes. Nat. Commun. 8, 16113.

  • Candel A.M., Romero-Romero M.L., Gamiz-Arco G., Ibarra-Molero B., Sanchez-Ruiz J.M. (2017) “Fast folding and slow unfolding of a resurrected Precambrian protein”. Proc Natl Acad Sci USA 114:E4122-E4123.

  • Delgado A., Arco R., Ibarra-Molero B., Sanchez-Ruiz J.M. (2017) “Using resurrected ancestral proviral proteins to engineer virus resistance”. Cell Rep 19:1247-1256.

  • Medina-Carmona, E., Neira, J.L., Salido, E., Fuchs, J.E., Palomino-Morales, R., Timson, D.J., Pey, A.L. (2017) “Site-to-site interdomain communication may mediate different loss-of-function mechanisms in a cancer-associated NQO1 polymorphism”. Scientific Reports 7:44352.

  • Gimenez-Mascarell, P., Oyenarte, I., Hardy, S., Breiderhoff, T., Stuiver, M., Kostantin, E., Diercks, T, Pey, A.L., Ereno-Orbea, J., Martinez-Chantar, M.L., Khalaf-Nazzal, R., Claverie-Martin, F., Muller, D., Tremblay, M.L., Martinez-Cruz, M.L. (2017) “Structural Basis of the Oncogenic Interaction of Phosphatase PRL-1 with the Magnesium Transporter CNNM2”. J Biol Chem no. 292 (3):786-801. doi: 10.1074/jbc.M116.759944.

Año 2016

  • Romero-Romero M.L., Risso V.A., Martinez-Rodriguez S., Ibarra-Molero B., Sanchez-Ruiz J.M. (2016) “Engineering ancestral protein hyperstability”. Biochem J 473:3611-3620.

  • Medina-Carmona, E., Palomino-Morales, R.J., Fuchs, J.E., Padín-Gonzalez, E., Mesa-Torres, N., Salido, E., Timson, D.J., Pey, A.L. (2016) “Conformational dynamics is key to understanding loss-of-function of NQO1 cancer-associated polymorphisms and its correction by pharmacological ligands”. Scientific Reports 6:20331. doi: 10.1038/srep20331.

  • Mesa-Torres, N., Calvo, A.C., Oppici, E., Titelbaum, N., Montioli, R., Miranda-Vizuete, A., Cellini, B., Salido, E., Pey, A.L. (2016) “Caenorhabditis elegans AGXT-1 is a mitochondrial and temperature-adapted ortholog of peroxisomal human AGT1: New insights into between-species divergence in glyoxylate metabolism”. Biochim Biophys Acta 1864 (9):1195-205. doi: 10.1016/j.bbapap.2016.05.004.

  • Neira, J.L., Medina-Carmona, E., Hernandez-Cifre, J.G., Montoliu-Gaya, L., Camara-Artigas, A., Seffouh, I., Gonnet, F., Daniel, R., Villegas, S., de la Torre, J.G., Pey, A.L., Li, F. (2016) “The chondroitin sulfate/dermatan sulfate 4-O-endosulfatase from marine bacterium Vibrio sp FC509 is a dimeric species: Biophysical characterization of an endosulfatase”. Biochimie 131:85-95. doi: 10.1016/j.biochi.2016.09.015.

  • Pey, A.L., Megarity, C.F., Medina-Carmona, E., Timson, D.J. (2016) “Natural small molecules as stabilizers and activators of cancer-associated NQO1 polymorphisms”. Curr Drug Targets 17:1506-1514. doi: 10.2174/1389450117666160101121610.

  • Romero-Romero, M.L., Risso, V.A., Martinez-Rodriguez, S., Gaucher, E.A., Ibarra-Molero, B., Sanchez-Ruiz, J.M. (2016) “Selection for Protein Kinetic Stability Connects Denaturation Temperatures to Organismal Temperatures and Provides Clues to Archaean Life”. PLoS One,11(6):e0156657. doi: 10.1371/journal.pone.0156657. eCollection 2016.

  • Ibarra-Molero, B., Naganathan, A.N., Sanchez-Ruiz, J.M., Muñoz, V. (2016) “Modern Analysis of Protein Folding by Differential Scanning Calorimetry”. Methods Enzymol.,567:281-318. doi: 10.1016/bs.mie.2015.08.027. Epub 2015 Nov 6.

  • Fuchs, J.E., Muñoz, I.G., Timson, D.J., Pey, A.L. (2016) “Experimental and computational evidence on conformational fluctuations as a source of catalytic defects in genetic diseases”. RSC Adv. 6:58604. doi: 10.1039/C6RA05499D

  • Majtan, T., Pey, A.L., Ereño-Orbea, J., Martinez-Cruz, L.A., Kraus, J.P. (2016) “Targeting Cystathionine Beta-Synthase Misfolding in Homocystinuria by Small Ligands: State of the Art and Future Directions”. Current Drug Targets 17:1455-1470.

  • Majtan, T., Pey, A.L., Kraus, J.P. (2016) “Kinetic stability of cystathionine beta-synthase can be modulated by structural analogs of Sadenosylmethionine: Potential approach to pharmacological chaperone therapy for homocystinuria”. Biochimie. 126:6-13. doi: 10.1016/j.biochi.2016.01.009.

  • McAuley, M., Kristiansson, H., Huang, M., Pey, A.L., Timson, D.J. (2016) “Galactokinase promiscuity: a question of flexibility?”. Biochem Soc Trans 44 (1):116-22. doi: 10.1042/BST20150188.

  • McCorvie, T.J., Kopec, J., Pey, A.L., Fitzpatrick, F., Patel, D., Chalk, R., Streetha, L., Yue, W.W. (2016) “Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase”. Hum Mol Genet 25:2234-2244. doi: 10.1093/hmg/ddw091.

Año 2015

  • Naganathan AN, Sanchez-Ruiz JM, Munshi S, Suresh S. (2015) ” Are protein folding intermediates the evolutionary consequence of functional constraints?”. J Phys Chem B 119:1323-1333.

  • Risso VA, Manssour-Triedo F, Delgado-Delgado A, Arco R, Barroso-delJesus A, Ingles-Prieto A, Godoy-Ruiz R, Gavira JA, Gaucher EA, Ibarra-Molero B, Sanchez-Ruiz JM.”Mutational studies on resurrected ancestral proteins reveal conservation of site-specific amino acid preferences throughout evolutionary history”. Mol Biol Evol. (2015) Feb;32(2):440-55. doi: 10.1093/molbev/msu312. Epub 2014 Nov 12.

  • Zou T, Risso VA, Gavira JA, Sanchez-Ruiz JM, Ozkan SB. “Evolution of conformational dynamics determines the conversion of a promiscuous generalist into a specialist enzyme”. Mol Biol Evol. (2015) Jan;32(1):132-43. doi: 10.1093/molbev/msu281. Epub 2014 Oct 13.

Año 2014

  • Rincón V, Rodríguez-Huete A, López-Argüello S, Ibarra-Molero B, Sanchez-Ruiz JM, Harmsen MM, Mateu MG. “Identification of the structural basis of thermal lability of a virus provides a rationale for improved vaccines”. Structure. (2014) Nov 4;22(11):1560-70. doi: 10.1016/j.str.2014.08.019. Epub 2014 Oct 9.

  • VA. Risso, JA. Gavira, JM. Sanchez-Ruiz (2014) “Thermostable and promiscuous Precambrian proteins”. Environmental Microbiology and Environmental Microbiology Reports (16:1485-1489).

Año 2013

  • VA. Risso, JA. Gavira, DF. Mejia-Carmona, EA. Gaucher, JM. Sanchez-Ruiz (2013) Hyperstability and substrate promiscuity in laboratory resurrections of Precambrian beta-lactamases. J Am Chem Soc 135, 2899-902.

  • A. Ingles-Prieto, B. Ibarra-Molero, A. Delgado-Delgado, R. Perez- Jimenez, JM. Fernandez, EA. Gaucher, JM. Sanchez-Ruiz, JA. Gavira (2013) Conservation of protein structure over four billion years. Structure 3,1690-7.

  • I. Sanchez- Romero, A. Ariza, KS. Wilson, M. Skjot, J. Vind, L. De Maria, LK. Skov, JM. Sanchez- Ruiz (2013) Mechanism of protein kinetic stabilization by engineered disulfide crosslinks. PLoS One 8, e70013.

  • Y. Aguirre, N. Cabrera, B. Aguirre, R. Pérez-Montfort, A. Hernandez-Santoyo, A. Hernandez-Santoyo,H. Reyes-Vivas, S. Enríquez-Flores, MT. de Gómez-Puyou, A. Gómez- Puyou, JM Sanchez-Ruiz, M. Costas (2013) Different contribution of conserved amino acids to the global properties of triosephosphate isomerases. Proteins.

  • AL. Pey, T. Majtan, JM. Sanchez-Ruiz, JP. Kraus (2013) Human cystathiomine ?-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM. Biochem J 449,109-21.

  • AL. Pey, A. Albert, E. Salido (2013) Protein homeostasis defects of alanine-glyoxylate aminotransferase: new therapeutic strategies in primary hyperoxaluria type I. Biomed Res Int 2013,687658.

  • AL. Pey (2013) The interplay between protein stability and dynamics in conformational diseases: The case of hPGK1 deficiency. Biochim Biophys Acta 1834,2502-2511.

  • AL. Pey, N. Mesa- Torres, LR. Chiarelli, G.Valentini (2013) Structural and energetic basis of protein kinetic destabilization in human phosphoglycerate kinase 1 defiency. Biochemistry 52,1160-70.

Año 2012

  • A. Hnízda, T. Majtan, L. Liu, AL. Pey, JF. Carpenter, M. Kodicek, V. Kozich, JP. Kraus (2012) Correction to Conformational Properties of Nine Purified Cystathionine ?-Synthase Mutants. Biochemistry 51,5540.

  • A. Hnízda, T. Majtan, L. Liu, AL. Pey, JF. Carpenter, M. Kodicek, V. Kozich, JP. Kraus(2012) Conformational properties of nine purified cystathionine ?-synthase mutants. Biochemistry 51, 4755-63.

  • P. Kosuri, J. Alegre-Cebollada, J. Feng, A. Kaplan, A. Inglés-Prieto, C.L. Badilla, B.R. Stockwell, J.M. Sanchez-Ruiz, A. Holmgren, A.J. Fernández (2012) Protein folding drives disulfide formation. Cell 151, 794-806.

  • H. Bustad Johannessen, L. Skjærven, M. Ying, J. Underhaug, A. Baumann, Ø. Halskau,D. Rodriguez-Larrea, M. Costas, J.M. Sanchez-Ruiz, A. Martinez (2012) The peripheral binding of 14-3-3y to membranes involves isoform-specific histidine residues. PLoS ONE (in press).

  • Salido, E., Pey, A.L., Rodriguez, R., Lorenzo, V. (2012) Primary hyperoxalurias: Disorders of glyoxylate detoxification. Biochim Biophys Acta. In press

  • Hnízda, A., Majtan, T., Liu, L., Pey, A. L., Carpenter, J. F., Kodíček, M., Kožich, V. and Kraus, J. P. (2012) Conformational properties of nine purified cystathionine beta-synthase mutants. Biochemistry. In press.

  • J.M. Sanchez-Ruiz (2012). On promiscuity, changing enviroments and the possibility of re-playing the molecular tape of life. Biochemical Journal, 445:e1-3.

  • H. Garcia-Seisdedos, B. Ibarra-Molero, J.M. Sanchez-Ruiz (2012). Probing the Mutational Interplay Between Primary and Promiscuous Protein Functions: A Computational-Experimental Approach. PLoS Computational Biology, 8:e1002558.

  • H. Garcia-Seisdedos, B. Ibarra-Molero, J.M. Sanchez-Ruiz (2012). How many ionizable groups can sit on a protein hydrophobic core?. Proteins 80, 1-7.

Año 2011

  • Ana Cristina Calvo, Angel Luis Pey Rodriguez, Antonio Miranda Vizuete, Anne P. Doskeland, Aurora Martinez (2011). Divergence in enzyme regulation between Caenorhabditis elegans and human tyrosine hydroxylase, the key enzyme in the synthesis of dopamine. Biochemical Journal 434, 133 - 141.

  • Angel Luis Pey Rodriguez, Eduardo C. Salido, Jose Manuel Sanchez Ruiz (2011). Role of low native state kinetic stability and interaction of partially unfolded states with molecular chaperones in the mitochondrial protein mistargeting associated with primary hyperoxaluria. Amino Acids 41, 1233 - 1245.

  • Khanh K. Dao, Angel L. Pey Rodriguez, Anja Underhaug Gjerde, Knut Teigen, In-Ja L. Byeon, Stein Ove Doskeland, Angela M. Gronenborn, Aurora Martinez (2011). The regulatory subunit of PKA-I remains partially structured and undergoes beta-aggregation upon thermal denaturation, PLoS One 6, e17602.

  • M.L. Romero-Romero, A. Inglés-Prieto, B. Ibarra-Molero, J.M. Sanchez-Ruiz (2011). Highly anomalous energetics of protein cold denaturation linked to folding-unfolding kinetics. PLoS One. 6, e23050.

  • A.N. Naganathan, R. Perez-Jimenez, V. Muñoz, J.M. Sanchez-Ruiz (2011). Estimation of protein folding free energy barriers from calorimetric data by multi-model Bayesian analysis. Physical Chemistry Chemical Physics 13, 17064-76.

  • R. Perez-Jimenez, A. Inglés-Prieto, Z.M. Zhao, I. Sanchez-Romero, J. Alegre-Cebollada, P. Kosuri, S. Garcia-Manyes, T.J. Kappock, M. Tanokura, A. Holmgren, J.M. Sanchez-Ruiz, E.A. Gaucher, J.M. Fernandez (2011). Single-molecule paleoenzymology probes the chemistry of resurrected enzymes. Nature Structural & Molecular Biology 18, 592-6.

  • J.M. Sanchez-Ruiz (2011). Probing free-energy surfaces with differential scanning calorimetry. Annual Review of Physical Chemistry 62, 231-55. Review.

  • A.L. Pey, E. Salido, J.M. Sanchez-Ruiz (2011). Role of low native state kinetic stability and interaction of partially unfolded states with molecular chaperones in the mitochondrial protein mistargeting associated with primary hyperoxaluria. Amino Acids. 41, 1233-45.

Año 2010

  • A.N. Naganathan, P. Li, R. Perez-Jimenez, J.M. Sanchez-Ruiz, V. Muñoz (2010). Navigating the downhill protein folding regime via structural homologues. Journal of the American Chemical Society 132, 11183-90.

  • D. Rodriguez-Larrea, R. Perez-Jimenez, I. Sanchez-Romero, A. Delgado-Delgado, J.M. Fernandez, J.M. Sanchez-Ruiz (2010). Role of conservative mutations in protein multi-property adaptation. Biochemical Journal 429, 243-9.

  • G. Tur-Arlandis, D. Rodriguez-Larrea, B. Ibarra-Molero, J.M. Sanchez-Ruiz (2010). Proteolytic scanning calorimetry: a novel methodology that probes the fundamental features of protein kinetic stability. Biophysical Journal 98, L12-4.

  • J.M. Sanchez-Ruiz (2010). Protein kinetic stability. Biophysical Chemistry 148(1-3), 1-15. Review.

  • A.L. Pey, D. Rodriguez-Larrea, J.A. Gavira, B. Garcia-Moreno, J.M. Sanchez-Ruiz (2010). Modulation of buried ionizable groups in proteins with engineered surface charge. Journal of the American Chemical Society 132, 1218-9.

  • M. Suarez, P. Tortosa, M.M. Garcia-Mira, D. Rodríguez-Larrea, R. Godoy-Ruiz, B. Ibarra-Molero, J.M. Sanchez-Ruiz, A. Jaramillo (2010). Using multi-objective computational design to extend protein promiscuity. Biophysical Chemistry 147, 13-9.

  • A. Negri, D. Rodríguez-Larrea, E. Marco, A. Jiménez-Ruiz, J.M. Sánchez- Ruiz, F. Gago (2010). Protein-protein interactions at an enzyme-substrate interface: characterization of transient reaction intermediates throughout a full catalytic cycle of Escherichia coli thioredoxin reductase. Proteins 78, 36-51.

Año 2009

  • R. Perez-Jimenez, J. Li, P. Kosuri, I. Sanchez-Romero, A.P. Wiita, D. Rodriguez-Larrea, A. Chueca, A. Holmgren, A. Miranda-Vizuete, K. Becker, S.H. Cho, J. Beckwith, E. Gelhaye, J.P. Jacquot, E. Gaucher, J.M. Sanchez-Ruiz, B.J. Berne, J.M. Fernandez (2009). Diversity of chemical mechanisms in thioredoxin catalysis revealed by single-molecule force spectroscopy. Nature Structural and Molecular Biology 16, 890-6.

  • M. Sadqi, E. de Alba, R. Perez-Jimenez, J.M. Sanchez-Ruiz, V. Muñoz (2009). A designed protein as experimental model of primordial folding. Proceedings of the National Academy of Sciences of USA 106, 4127-32.

  • L.M. Blancas-Mejia, L.A. Tellez, L. Del Pozo-Yauner, B. Becerril, J.M. Sanchez-Ruiz, D.A. Fernandez-Velasco (2009). Thermodynamic and kinetic characterization of a germ line human lambda6 light-chain protein: The relation between unfolding and fibrillogenesis. Journal of Molecular Biology 386, 1153-66.

  • M. Costas, D. Rodriguez-Larrea, L. De Maria, T.V. Borchert, A. Gomez-Puyou, J.M.Sanchez-Ruiz (2009). Between-Species variation in the kinetic stability of TIM proteins linked to solvation-barrier free energies. Journal of Molecular Biology 385, 924-37.

Año 2008

  • R. Perez-Jimenez, A.P. Wiita, D. Rodriguez-Larrea, P. Kosuri, J.A. Gavira, J.M.Sanchez-Ruiz, J.M. Fernandez (2008). Force-clamp spectroscopy detects residue co-evolution in enzyme catalysis. The Journal of Biological Chemistry 283, 27121-9.

  • A. Fung, P. Li, R. Godoy-Ruiz, J.M.Sanchez-Ruiz, V. Muñoz (2008). Expanding the realm of ultrafast protein folding: gpW, a mid-size natural single-domain with novel α+β topology that folds downhill. Journal of American Chemical Society 130, 7489-95.

  • O. Halskau, R. Perez-Jimenez, B. Ibarra-Molero, J. Underhaug, V. Muñoz, A. Martinez, J.M. Sanchez-Ruiz (2008). Large-scale modulation of thermodynamic protein folding barriers linked to electrostatics. Proceedings of the National Academy of Sciences of USA 105, 8625-30.

  • R. Szoszkiewicz, S.R.K. Ainavarapu, A.P. Wiita, R. Perez-Jimenez, J. M. Sanchez-Ruiz, J. Fernandez (2008). Dwell time analysis of a single molecule mechanochemical reaction. Langmuir 24, 1356-64.

  • R. Godoy-Ruiz, E.R. Henry, J. Kubelka, J. Hofrichter, V. Muñoz, J. M. Sanchez-Ruiz, W.A. Eaton (2008). Estimating free energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data. Journal of Physical Chemistry B 112, 5938-49.

  • A. L. Pey, D. Rodríguez-Larrea, S. Bomke, S. Dammers, R. Godoy-Ruiz, M. M. Garcia-Mira, J. M. Sanchez-Ruiz (2008). Engineering proteins with tunable thermodynamic and kinetic stabilities. Proteins 71, 165-74.

  • B. Ibarra-Molero and J. M. Sanchez-Ruiz (2008). Statistical differential scanning calorimetry: Probing protein folding-unfolding ensembles. In “Protein Folding, Misfolding and Aggregation” (V. Muñoz ed.), RSC Publishing, 85-103.

  • D. Rodriguez-Larrea, B. Ibarra-Molero, L. de Maria, T. V. Borchert, J. M. Sanchez-Ruiz (2008). Beyond Lumry-Eyring: an unexpected pattern of operational reversibility/irreversibility in protein denaturation. Proteins 70, 19-24.

Año 2007

  • A. Wiita, R. Perez-Jimenez, K. A. Walther, F. Grater, B. J. Berne, A. Holmgren, J. M. Sanchez-Ruiz, J. Fernandez (2007). Probing the chemistry of thioredoxin catalysis with force. Nature 450, 124-7.

  • J. M. Sanchez-Ruiz (2007). Ligand effects on protein thermodynamic stability. Biophysical Chemistry 126, 43-49.

Año 2006

  • R. Godoy-Ruiz, F. Ariza, D. Rodriguez-Larrea, R. Perez-Jimenez, B. Ibarra-Molero and J. M. Sanchez-Ruiz (2006). Natural selection for kinetic stability is a likely origin of correlations between mutation effects on protein energetics and frequencies of amino-acid occurrences in sequence alignments. Journal of Molecular Biology 362, 966-978.

  • D. Rodriguez-Larrea, B. Ibarra-Molero and J. M. Sanchez-Ruiz (2006). Energetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding rates. Biophysical Journal 91, 48-50.

  • D. Rodriguez-Larrea, S. Minning, T.V. Borchert and J. M. Sanchez-Ruiz (2006). Role of solvation barriers in protein kinetic stability. Journal of Molecular Biology 360, 715-724.

  • B. Ibarra-Molero and J. M. Sanchez-Ruiz (2006). Differential scanning calorimetry of proteins: an overview and some recent advances. In “Advanced Techniques in Biophysics” (Arrondo JL and Alonso A, eds). Elsevier, 27-48.

  • R. Perez-Jimenez, R. Godoy-Ruiz, A. Parody-Morreale, B. Ibarra-Molero and J.M. Sanchez-Ruiz (2006). ” A simple tool to explore the distance distribution of correlated mutations in proteins”. Biophysical Chemistry 119, 240-6.

Año 2005

  • A.N. Naganathan, J. M. Sanchez-Ruiz and V. Muñoz (2005). “Direct measurement of barrier heights in protein folding”. Journal of American Chemical Society 127, 17970-1.

  • R. Godoy-Ruiz, R. Perez-Jimenez, M.M. Garcia-Mira, I.M. Plaza del Pino and J.M. Sanchez-Ruiz (2005). “Empirical parametrization of pK values for carboxylic acids in proteins using a genetic algorithm”. Biophysical Chemistry 115, 263-6.

  • R. Perez-Jimenez, R. Godoy-Ruiz, B. Ibarra-Molero and J.M. Sanchez-Ruiz (2005). ” The effect of charge-introduction mutations on E. coli thioredoxin stability”. Biophysical Chemistry 115, 105-7.

  • R. Godoy-Ruiz, R. Perez-Jimenez, B. Ibarra-Molero and J. M. Sanchez-Ruiz (2005). “A stability pattern of protein hydrophobic mutations that reflects evolutionary structural optimization”. Biophysical Journal 89, 3320-31.

  • A.N. Naganathan, R. Perez-Jimenez, J. M. Sanchez-Ruiz and V. Muñoz (2005). “Robustness of downhill folding: guidelines for the analysis of equilibrium folding experiments on small proteins”. Biochemistry 44, 7435-49.

Publicaciones Seleccionadas (1999-2004)

  • V. Muñoz and J. M. Sanchez-Ruiz (2004). “Exploring protein-folding ensembles: a variable-barrier model for the analysis of equilibrium unfolding experiments”. Proceedings of the National Academy of Sciences of USA 101, 17646-51.

  • L.A. Campos, M.M. Garcia-Mira, R. Godoy-Ruiz, J. M. Sanchez-Ruiz and J. Sancho (2004). “Do proteins always benefit from a stability increase? Relevant and residual stabilisation in a three-state protein by charge optimisation”. Journal of Molecular Biology 344, 223-37.

  • J. Lopez-Llano, S. Maldonado, S. Jain, A. Lostao, R. Godoy-Ruiz, J. M. Sanchez-Ruiz, M. Cortijo, J. Fernandez-Recio and J. Sancho (2004). “The long and short flavodoxins:II. The role of the differentiating loop in apoflavodoxin stability and folding mechanism”. The Journal of Biological Chemistry 279, 47184-91.

  • F.F. Miranda, M. Thorolfsson, K. Teigen, J. M. Sanchez-Ruiz, A. Martinez (2004). “Structural and stability effects of phosphorylation: Localized structural changes in phenylalanine hydroxylase”. Protein Science 13, 1219-26.

  • R. Perez-Jimenez, R. Godoy-Ruiz, B. Ibarra-Molero and J. M. Sanchez-Ruiz (2004). “The efficiency of different salts to screen charge interactions in proteins: a Hofmeister effect?”. Biophysical Journal 86, 2414-29.

  • R. Godoy-Ruiz, R. Perez-Jimenez, B. Ibarra-Molero and J. M. Sanchez-Ruiz (2004). “Relation between protein stability, evolution and structure, as probed by carboxylic acid mutations”. Journal of Molecular Biology 336, 313-8.

  • S. Robic, M. Guzman-Casado, J. M. Sanchez-Ruiz and S. Marqusee (2003). “Role of residual structure in the unfolded state of a thermophilic protein”. Proceedings of the National Academy of Sciences of USA 100, 11345-9.

  • M. Guzman-Casado, A. Parody-Morreale, S. Robic, S. Marqusee and J. M. Sanchez-Ruiz (2003). “Energetic evidence for formation of a pH-dependent hydrophobic cluster in the denatured state of Thermus thermophilus ribonuclease H”. Journal of Molecular Biology 329, 731-43.

  • M. M. Garcia-Mira, M. Sadqui, N. Fischer, J. M. Sanchez-Ruiz, and V. Muñoz (2002). “Experimental identification of downhill protein folding”. Science 298, 2191-2195.

  • B. Ibarra-Molero and J. M. Sanchez-Ruiz (2002). “A genetic algorithm to design stabilizing surface charge distributions in proteins”. The Journal of Physical Chemistry B 106, 6609-6613.

  • M. Sundd, N. Iverson, B. Ibarra-Molero, J. M. Sanchez-Ruiz and A. D. Robertson (2002). “Electrostatic interactions in ubiquitin: Stabilization of carboxylates by lysine amino groups”. Biochemistry 41, 7586-7596.

  • M. Thorolfsson, B. Ibarra-Molero, P. Fojan, S. B. Petersen, J. M. Sanchez-Ruiz and A. Martinez (2002). “L-phenylalanine binding and domain organization in human phenylalanine hydroxylase: A differential scanning calorimetry study”. Biochemistry 41, 7573-7585.

  • A. V. Gribenko, M. Guzman-Casado, M. M. Lopez and G.I. Makhatadze (2002). “Conformational and thermodynamic properties of peptide binding to the human S100P protein”. Protein Science 11, 1367-1375.

  • M. P. Irún, M. M. Garcia-Mira, J. M. Sanchez-Ruiz and J. Sancho (2001). “Native hydrogen bonds in a molten globule: The apoflavodoxin thermal intermediate”. Journal of Molecular Biology 306, 877-888.

  • M. M. Garcia-Mira and J. M. Sanchez-Ruiz (2001). “pH corrections and protein ionization in water/guanidinium-chloride”. Biophysical Journal 81, 3489-3502.

  • J. M. Sanchez-Ruiz and G. I. Makhatadze (2001). “To charge or not to charge?”. Trends in Biotechnology 19, 132-134.

  • B. Ibarra-Molero, G.I. Makhatadze and C.R. Matthews (2001). “Mapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1”. Biochemistry 40, 719-31.

  • B. Ibarra-Molero, I. M. Plaza del Pino, B. Souhail, H. O. Hammou and J. M. Sanchez-Ruiz (2000). “The sarcosine effect on protein stability: A case of nonadditivity?”. Protein Science 9, 820-826.

  • I. M. Plaza del Pino, B. Ibarra-Molero and J. M. Sanchez-Ruiz (2000). “Lower kinetic limit to protein thermal stability: A proposal regarding protein stability in vivo and its relation with misfolding diseases”. Proteins: Structure, Function and Genetics 40, 58-70.

  • A. Lostao, M. El Harrous, F. Daouidi, A. Romero, A. Parody-Morreale and J. Sancho (2000). “Dissecting the energetics of the apoflavodoxin-FMN complex”. Journal of Biological Chemistry 275, 9518-9526.

  • J.A. Zitzewitz, B. Ibarra-Molero, D.R. Fishel, K.L. Terry and C.R. Matthews (2000). “Preformed secondary structure drives the association reaction of GCN4-p1, a model coiled-coil system”. Journal of Molecular Biology 296, 1105-16.

  • V. V. Lolazde, B. Ibarra-Molero, J. M. Sanchez-Ruiz and G. I. Makhatadze (1999). “Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface”. Biochemistry 38, 16419-16423.

  • B. Ibarra-Molero, V. V. Lolazde, G. I. Makhatadze and J. M. Sanchez-Ruiz (1999). “Thermal versus guanidine-induced unfolding of ubiquitin. An analysis in terms of the contributions from charge-charge interactions to protein stability”. Biochemistry 38, 8138-8149.