| Year |
Citation |
Score |
| 2024 |
Galano-Frutos JJ, Sancho J. Energy, water, and protein folding: A molecular dynamics-based quantitative inventory of molecular interactions and forces that make proteins stable. Protein Science : a Publication of the Protein Society. 33: e4905. PMID 38284492 DOI: 10.1002/pro.4905 |
0.314 |
|
| 2023 |
Galano-Frutos JJ, Nerín-Fonz F, Sancho J. Calculation of Protein Folding Thermodynamics Using Molecular Dynamics Simulations. Journal of Chemical Information and Modeling. PMID 37955428 DOI: 10.1021/acs.jcim.3c01107 |
0.319 |
|
| 2022 |
Galano-Frutos JJ, García-Cebollada H, López A, Rosell M, Cruz X, Fernández-Recio J, Sancho J. PirePred: An Accurate Online Consensus Tool to Interpret Newborn Screening-Related Genetic Variants in Structural Context. The Journal of Molecular Diagnostics : Jmd. PMID 35143952 DOI: 10.1016/j.jmoldx.2022.01.005 |
0.713 |
|
| 2020 |
Piñana M, Vila J, Maldonado C, Galano-Frutos JJ, Valls M, Sancho J, Nuvials FX, Andrés C, Martín-Gómez MT, Esperalba J, Codina MG, Pumarola T, Antón A. Insights into immune evasion of human metapneumovirus: novel 180- and 111-nucleotide duplications within viral G gene throughout 2014-2017 seasons in Barcelona, Spain. Journal of Clinical Virology. 132: 104590. PMID 32957052 DOI: 10.1016/J.Jcv.2020.104590 |
0.311 |
|
| 2020 |
Salillas S, Sancho J. Flavodoxins as Novel Therapeutic Targets Against Helicobacter pylori and Other Gastric Pathogens International Journal of Molecular Sciences. 21: 1881. PMID 32164177 DOI: 10.3390/Ijms21051881 |
0.301 |
|
| 2019 |
Galano-Frutos JJ, García-Cebollada H, Sancho J. Molecular dynamics simulations for genetic interpretation in protein coding regions: where we are, where to go and when. Briefings in Bioinformatics. PMID 31813950 DOI: 10.1093/Bib/Bbz146 |
0.336 |
|
| 2019 |
Galano-Frutos JJ, Sancho J. Accurate Calculation of Barnase and SNase Folding Energetics using short MD simulations and an Atomistic Model of the Unfolded Ensemble. Evaluation of Force Fields and Water Models. Journal of Chemical Information and Modeling. PMID 31513394 DOI: 10.1021/Acs.Jcim.9B00430 |
0.399 |
|
| 2019 |
González A, Salillas S, Velázquez-Campoy A, Espinosa Angarica V, Fillat MF, Sancho J, Lanas Á. Identifying potential novel drugs against Helicobacter pylori by targeting the essential response regulator HsrA. Scientific Reports. 9: 11294. PMID 31383920 DOI: 10.1038/S41598-019-47746-9 |
0.314 |
|
| 2018 |
Villanueva R, Romero-Tamayo S, Laplaza R, Martínez-Oliván J, Velazquez-Campoy A, Sancho J, Ferreira P, Medina M. Redox and ligand binding dependent conformational ensembles in the human apoptosis-inducing factor regulate its pro-life and cell death functions. Antioxidants & Redox Signaling. PMID 30450916 DOI: 10.1089/Ars.2018.7658 |
0.36 |
|
| 2017 |
Lamazares E, Vega S, Ferreira P, Medina M, Galano-Frutos JJ, Martínez-Júlvez M, Velázquez-Campoy A, Sancho J. Direct examination of the relevance for folding, binding and electron transfer of a conserved protein folding intermediate. Physical Chemistry Chemical Physics : Pccp. PMID 28702545 DOI: 10.1039/C7Cp02606D |
0.459 |
|
| 2016 |
Rodríguez-Cárdenas Á, Rojas AL, Conde-Giménez M, Velázquez-Campoy A, Hurtado-Guerrero R, Sancho J. Streptococcus pneumoniae TIGR4 Flavodoxin: Structural and Biophysical Characterization of a Novel Drug Target. Plos One. 11: e0161020. PMID 27649488 DOI: 10.1371/Journal.Pone.0161020 |
0.368 |
|
| 2016 |
Hidalgo J, Latorre P, Carrodeguas JA, Velázquez-Campoy A, Sancho J, López-Buesa P. Inhibition of Pig Phosphoenolpyruvate Carboxykinase Isoenzymes by 3-Mercaptopicolinic Acid and Novel Inhibitors. Plos One. 11: e0159002. PMID 27391465 DOI: 10.1371/Journal.Pone.0159002 |
0.326 |
|
| 2016 |
Velazquez-Campoy A, Sancho J, Abian O, Vega S. Biophysical Screening for Identifying Pharmacological Chaperones and Inhibitors against Conformational and Infectious Diseases. Current Drug Targets. PMID 26844568 DOI: 10.2174/1389450117666160201110449 |
0.346 |
|
| 2016 |
Angarica VE, Orozco M, Sancho J. Exploring the complete mutational space of the LDL receptor LA5 domain using molecular dynamics: linking SNPs with disease phenotypes in familial hypercholesterolemia. Human Molecular Genetics. 25: 1233-46. PMID 26755827 DOI: 10.1093/Hmg/Ddw004 |
0.343 |
|
| 2016 |
Estrada J, Echenique P, Sancho J. Predicting stabilizing mutations in proteins using Poisson-Boltzmann based models: study of unfolded state ensemble models and development of a successful binary classifier based on residue interaction energies. Physical Chemistry Chemical Physics : Pccp. 17: 31044-54. PMID 26530878 DOI: 10.1039/c5cp04348d |
0.302 |
|
| 2015 |
Luján MA, Martínez JI, Alonso PJ, Torrado A, Roncel M, Ortega JM, Sancho J, Picorel R. In vivo reconstitution of a homodimeric cytochrome b559 like structure: The role of the N-terminus α-subunit from Synechocystis sp. PCC 6803. Journal of Photochemistry and Photobiology. B, Biology. PMID 26183783 DOI: 10.1016/J.Jphotobiol.2015.07.006 |
0.333 |
|
| 2015 |
Lamazares E, Clemente I, Bueno M, Velázquez-Campoy A, Sancho J. Rational stabilization of complex proteins: a divide and combine approach. Scientific Reports. 5: 9129. PMID 25774740 DOI: 10.1038/Srep09129 |
0.427 |
|
| 2015 |
Martínez-Oliván J, Fraga H, Arias-Moreno X, Ventura S, Sancho J, Mobli M. Intradomain confinement of disulfides in the folding of two consecutive modules of the LDL receptor Plos One. 10. DOI: 10.1371/Journal.Pone.0132141 |
0.359 |
|
| 2015 |
Laurents DV, Pantoja-Uceda D, López LC, Carrodeguas JA, Mompeán M, Jiménez M, Sancho J. DMSO affects Aβ1-40's conformation and interactions with aggregation inhibitors as revealed by NMR Rsc Advances. 5: 69761-69764. DOI: 10.1039/C5Ra12100K |
0.307 |
|
| 2015 |
Galano-Frutos JJ, Carmen Morón M, Sancho J. The mechanism of water/ion exchange at a protein surface: A weakly bound chloride in Helicobacter pylori apoflavodoxin Physical Chemistry Chemical Physics. 17: 28635-28646. DOI: 10.1039/C5Cp04504E |
0.359 |
|
| 2015 |
Estrada J, Echenique P, Sancho J. Predicting stabilizing mutations in proteins using Poisson-Boltzmann based models: Study of unfolded state ensemble models and development of a successful binary classifier based on residue interaction energies Physical Chemistry Chemical Physics. 17: 31044-31054. DOI: 10.1039/C5Cp04348D |
0.414 |
|
| 2015 |
Martínez-Oliván J, Arias-Moreno X, Hurtado-Guerrero R, Carrodeguas JA, Miguel-Romero L, Marina A, Bruscolini P, Sancho J. The closed conformation of the LDL receptor is destabilized by the low Ca++ concentration but favored by the high Mg++ concentration in the endosome Febs Letters. 589: 3534-3540. DOI: 10.1016/J.Febslet.2015.10.014 |
0.328 |
|
| 2015 |
Romero CM, Abella JS, Velázquez A, Sancho J. Thermal denaturation of α-chymotrypsinogen A in presence of polyols at pH 2.0 and pH 3.0 Journal of Thermal Analysis and Calorimetry. 120: 489-499. DOI: 10.1007/S10973-014-4374-2 |
0.377 |
|
| 2014 |
Martínez-Oliván J, Rozado-Aguirre Z, Arias-Moreno X, Angarica VE, Velázquez-Campoy A, Sancho J. Low-density lipoprotein receptor is a calcium/magnesium sensor - role of LR4 and LR5 ion interaction kinetics in low-density lipoprotein release in the endosome. The Febs Journal. 281: 2638-58. PMID 24720672 DOI: 10.1111/Febs.12811 |
0.302 |
|
| 2014 |
Espinosa Angarica V, Angulo A, Giner A, Losilla G, Ventura S, Sancho J. PrionScan: an online database of predicted prion domains in complete proteomes. Bmc Genomics. 15: 102. PMID 24498877 DOI: 10.1186/1471-2164-15-102 |
0.362 |
|
| 2014 |
Martínez-Oliván J, Arias-Moreno X, Velazquez-Campoy A, Millet O, Sancho J. LDL receptor/lipoprotein recognition: endosomal weakening of ApoB and ApoE binding to the convex face of the LR5 repeat. The Febs Journal. 281: 1534-46. PMID 24447298 DOI: 10.1111/Febs.12721 |
0.309 |
|
| 2013 |
Abian O, Vega S, Sancho J, Velazquez-Campoy A. Allosteric inhibitors of the NS3 protease from the hepatitis C virus. Plos One. 8: e69773. PMID 23936097 DOI: 10.1371/Journal.Pone.0069773 |
0.332 |
|
| 2013 |
Espinosa Angarica V, Ventura S, Sancho J. Discovering putative prion sequences in complete proteomes using probabilistic representations of Q/N-rich domains. Bmc Genomics. 14: 316. PMID 23663289 DOI: 10.1186/1471-2164-14-316 |
0.401 |
|
| 2013 |
Sancho J. The stability of 2-state, 3-state and more-state proteins from simple spectroscopic techniques... plus the structure of the equilibrium intermediates at the same time. Archives of Biochemistry and Biophysics. 531: 4-13. PMID 23142683 DOI: 10.1016/J.Abb.2012.10.014 |
0.436 |
|
| 2012 |
Angarica VE, Sancho J. Protein dynamics governed by interfaces of high polarity and low packing density. Plos One. 7: e48212. PMID 23110216 DOI: 10.1371/Journal.Pone.0048212 |
0.408 |
|
| 2012 |
MartÃnez-Júlvez M, Rojas AL, Olekhnovich I, Espinosa Angarica V, Hoffman PS, Sancho J. Structure of RdxA--an oxygen-insensitive nitroreductase essential for metronidazole activation in Helicobacter pylori. The Febs Journal. 279: 4306-17. PMID 23039228 DOI: 10.1111/Febs.12020 |
0.382 |
|
| 2012 |
García-Fandiño R, Bernadó P, Ayuso-Tejedor S, Sancho J, Orozco M. Defining the nature of thermal intermediate in 3 state folding proteins: apoflavodoxin, a study case. Plos Computational Biology. 8: e1002647. PMID 22927805 DOI: 10.1371/Journal.Pcbi.1002647 |
0.409 |
|
| 2012 |
Torreblanca R, Lira-Navarrete E, Sancho J, Hurtado-Guerrero R. Structural and mechanistic basis of the interaction between a pharmacological chaperone and human phenylalanine hydroxylase. Chembiochem. 13: 1266-1269. PMID 22549968 DOI: 10.1002/Cbic.201200188 |
0.326 |
|
| 2012 |
Graña-Montes R, Groot NSd, Castillo V, Sancho J, Velazquez-Campoy A, Ventura S. Contribution of Disulfide Bonds to Stability, Folding, and Amyloid Fibril Formation: The PI3-SH3 Domain Case Antioxidants & Redox Signaling. 16: 1-15. PMID 21797671 DOI: 10.1089/Ars.2011.3936 |
0.421 |
|
| 2011 |
Abian O, Alfonso P, Velazquez-Campoy A, Giraldo P, Pocovi M, Sancho J. Therapeutic strategies for Gaucher disease: Miglustat (NB-DNJ) as a pharmacological chaperone for glucocerebrosidase and the different thermostability of velaglucerase alfa and imiglucerase Molecular Pharmaceutics. 8: 2390-2397. PMID 21988669 DOI: 10.1021/Mp200313E |
0.365 |
|
| 2011 |
Ayuso-Tejedor S, Abián O, Velázquez-Campoy A, Sancho J. Mechanism of FMN Binding to the Apoflavodoxin from Helicobacter pylori. Biochemistry. 50: 8703-8711. PMID 21910456 DOI: 10.1021/Bi201025Y |
0.394 |
|
| 2011 |
Pérez-Llarena FJ, Kerff F, Abián O, Mallo S, Fernández MC, Galleni M, Sancho J, Bou G. Distant and new mutations in CTX-M-1 beta-lactamase affect cefotaxime hydrolysis. Antimicrobial Agents and Chemotherapy. 55: 4361-4368. PMID 21730121 DOI: 10.1128/Aac.00298-11 |
0.315 |
|
| 2011 |
Arias-Moreno X, Abian O, Vega S, Sancho J, Velazquez-Campoy A. Protein-cation interactions: structural and thermodynamic aspects. Current Protein & Peptide Science. 12: 325-38. PMID 21401523 DOI: 10.2174/138920311795906664 |
0.437 |
|
| 2011 |
Ayuso-Tejedor S, García-Fandiño R, Orozco M, Sancho J, Bernadó P. Structural analysis of an equilibrium folding intermediate in the apoflavodoxin native ensemble by small-angle X-ray scattering. Journal of Molecular Biology. 406: 604-19. PMID 21216251 DOI: 10.1016/J.Jmb.2010.12.027 |
0.433 |
|
| 2011 |
Ayuso-Tejedor S, Abián O, Sancho J. Underexposed polar residues and protein stabilization Protein Engineering Design & Selection. 24: 171-177. PMID 20937603 DOI: 10.1093/Protein/Gzq072 |
0.378 |
|
| 2011 |
Albis A, Lozano JM, Sancho J, Romero CM. Influence of calcium on the thermal stabilization of bovine α-lactalbumin by selected polyols Journal of Thermal Analysis and Calorimetry. 104: 37-44. DOI: 10.1007/S10973-010-1156-3 |
0.326 |
|
| 2010 |
Stevens RC, Sancho J, Martinez A. Rescue of misfolded proteins and stabilization by small molecules. Methods in Molecular Biology (Clifton, N.J.). 648: 313-24. PMID 20700723 DOI: 10.1007/978-1-60761-756-3_22 |
0.41 |
|
| 2010 |
Ayuso-Tejedor S, Angarica VE, Bueno M, Campos LA, Abián O, Bernadó P, Sancho J, Jiménez MA. Design and structure of an equilibrium protein folding intermediate: a hint into dynamical regions of proteins. Journal of Molecular Biology. 400: 922-34. PMID 20553732 DOI: 10.1016/J.Jmb.2010.05.050 |
0.465 |
|
| 2010 |
Ayuso-Tejedor S, Nishikori S, Okuno T, Ogura T, Sancho J. FtsH cleavage of non-native conformations of proteins. Journal of Structural Biology. 171: 117-124. PMID 20457259 DOI: 10.1016/J.Jsb.2010.05.001 |
0.449 |
|
| 2010 |
Alías M, Ayuso-Tejedor S, Fernández-Recio J, Cativiela C, Sancho J. Helix propensities of conformationally restricted amino acids. Non-natural substitutes for helix breaking proline and helix forming alanine Organic and Biomolecular Chemistry. 8: 788-792. PMID 20135035 DOI: 10.1039/B919671D |
0.697 |
|
| 2010 |
Arias-Moreno X, Cuesta-Lopez S, Millet O, Sancho J, Velazquez-Campoy A. Thermodynamics of protein-cation interaction: Ca(+2) and Mg(+2) binding to the fifth binding module of the LDL receptor. Proteins. 78: 950-961. PMID 19899171 DOI: 10.1002/Prot.22619 |
0.363 |
|
| 2010 |
Contreras-Moreira B, Sancho J, Angarica VE. Comparison of DNA binding across protein superfamilies. Proteins. 78: 52-62. PMID 19731374 DOI: 10.1002/Prot.22525 |
0.367 |
|
| 2009 |
Estrada J, Bernadó P, Blackledge M, Sancho J. ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensemble. Bmc Bioinformatics. 10: 104. PMID 19356231 DOI: 10.1186/1471-2105-10-104 |
0.369 |
|
| 2009 |
Romero CM, Albis A, Lozano JM, Sancho J. Thermodynamic study of the influence of polyols and glucose on the thermal stability of holo-bovine α-lactalbumin Journal of Thermal Analysis and Calorimetry. 98: 165-171. DOI: 10.1007/S10973-009-0138-9 |
0.38 |
|
| 2008 |
Arias-Moreno X, Velazquez-Campoy A, Rodríguez JC, Pocoví M, Sancho J. Mechanism of Low Density Lipoprotein (LDL) Release in the Endosome IMPLICATIONS OF THE STABILITY AND Ca2+ AFFINITY OF THE FIFTH BINDING MODULE OF THE LDL RECEPTOR Journal of Biological Chemistry. 283: 22670-22679. PMID 18574243 DOI: 10.1074/Jbc.M802153200 |
0.325 |
|
| 2008 |
Cremades N, Sancho J. Molten globule and native state ensemble of Helicobacter pylori flavodoxin: can crowding, osmolytes or cofactors stabilize the native conformation relative to the molten globule? Biophysical Journal. 95: 1913-1927. PMID 18441031 DOI: 10.1529/Biophysj.108.130153 |
0.413 |
|
| 2008 |
Arias-Moreno X, Arolas JL, Aviles FX, Sancho J, Ventura S. Scrambled isomers as key intermediates in the oxidative folding of ligand binding module 5 of the low density lipoprotein receptor. The Journal of Biological Chemistry. 283: 13627-37. PMID 18343813 DOI: 10.1074/Jbc.M800755200 |
0.431 |
|
| 2008 |
Cremades N, Velazquez-Campoy A, Freire E, Sancho J. The flavodoxin from Helicobacter pylori: structural determinants of thermostability and FMN cofactor binding. Biochemistry. 47: 627-39. PMID 18095659 DOI: 10.1021/Bi701365E |
0.398 |
|
| 2008 |
Cremades N, Bueno M, Neira JL, Velázquez-Campoy A, Sancho J. Conformational stability of Helicobacter pylori flavodoxin: fit to function at pH 5. Journal of Biological Chemistry. 283: 2883-2895. PMID 17998211 DOI: 10.1074/Jbc.M705677200 |
0.396 |
|
| 2007 |
Martínez-Júlvez M, Cremades N, Bueno M, Pérez-Dorado I, Maya C, Cuesta-López S, Prada D, Falo F, Hermoso JA, Sancho J. Common conformational changes in flavodoxins induced by FMN and anion binding: The structure of Helicobacter pylori apoflavodoxin Proteins. 69: 581-594. PMID 17623845 DOI: 10.1002/Prot.21410 |
0.398 |
|
| 2007 |
Bueno M, Camacho CJ, Sancho J. SIMPLE estimate of the free energy change due to aliphatic mutations: superior predictions based on first principles. Proteins. 68: 850-62. PMID 17523191 DOI: 10.1002/Prot.21453 |
0.378 |
|
| 2007 |
St Maurice M, Cremades N, Croxen MA, Sisson G, Sancho J, Hoffman PS. Flavodoxin:quinone reductase (FqrB): a redox partner of pyruvate:ferredoxin oxidoreductase that reversibly couples pyruvate oxidation to NADPH production in Helicobacter pylori and Campylobacter jejuni. Journal of Bacteriology. 189: 4764-73. PMID 17468253 DOI: 10.1128/Jb.00287-07 |
0.309 |
|
| 2007 |
Romero CM, Lozano JM, Sancho J, Giraldo GI. Thermal stability of beta-lactoglobulin in the presence of aqueous solution of alcohols and polyols. International Journal of Biological Macromolecules. 40: 423-8. PMID 17141862 DOI: 10.1016/J.Ijbiomac.2006.10.003 |
0.326 |
|
| 2006 |
Cuesta-López S, Falo F, Sancho J. Computational diagnosis of protein conformational diseases: short molecular dynamics simulations reveal a fast unfolding of r-LDL mutants that cause familial hypercholesterolemia. Proteins. 66: 87-95. PMID 17044057 DOI: 10.1002/Prot.21181 |
0.424 |
|
| 2006 |
Bernadó P, Blackledge M, Sancho J. Sequence-specific solvent accessibilities of protein residues in unfolded protein ensembles Biophysical Journal. 91: 4536-4543. PMID 17012314 DOI: 10.1529/Biophysj.106.087528 |
0.432 |
|
| 2006 |
Bueno M, Campos LA, Estrada J, Sancho J. Energetics of aliphatic deletions in protein cores. Protein Science : a Publication of the Protein Society. 15: 1858-72. PMID 16877708 DOI: 10.1110/Ps.062274906 |
0.399 |
|
| 2006 |
Cremades N, Sancho J, Freire E. The native-state ensemble of proteins provides clues for folding, misfolding and function. Trends in Biochemical Sciences. 31: 494-6. PMID 16870449 DOI: 10.1016/J.Tibs.2006.07.001 |
0.407 |
|
| 2006 |
López-Llano J, Campos LA, Sancho J. α‐helix stabilization by alanine relative to glycine: Roles of polar and apolar solvent exposures and of backbone entropy Proteins. 64: 769-778. PMID 16755589 DOI: 10.1002/Prot.21041 |
0.437 |
|
| 2006 |
Bueno M, Ayuso-Tejedor S, Sancho J. Do proteins with similar folds have similar transition state structures? A diffuse transition state of the 169 residue apoflavodoxin. Journal of Molecular Biology. 359: 813-824. PMID 16647718 DOI: 10.1016/J.Jmb.2006.03.067 |
0.386 |
|
| 2006 |
Bueno M, Cremades N, Neira JL, Sancho J. Filling small, empty protein cavities: structural and energetic consequences. Journal of Molecular Biology. 358: 701-712. PMID 16563433 DOI: 10.1016/J.Jmb.2006.02.060 |
0.435 |
|
| 2006 |
Sancho J. Flavodoxins: sequence, folding, binding, function and beyond Cellular and Molecular Life Sciences. 63: 855-864. PMID 16465441 DOI: 10.1007/S00018-005-5514-4 |
0.433 |
|
| 2006 |
Campos LA, Sancho J. Native-specific stabilization of flavodoxin by the FMN cofactor: structural and thermodynamical explanation. Proteins. 63: 581-594. PMID 16444751 DOI: 10.1002/Prot.20855 |
0.444 |
|
| 2006 |
López-Llano J, Campos LA, Bueno M, Sancho J. Equilibrium Φ-Analysis of a Molten Globule: The 1-149 Apoflavodoxin Fragment Journal of Molecular Biology. 356: 354-366. PMID 16364364 DOI: 10.1016/J.Jmb.2005.10.086 |
0.472 |
|
| 2005 |
Machicado C, López-Llano J, Cuesta-López S, Bueno M, Sancho J. Design of Ligand Binding to an Engineered Protein Cavity Using Virtual Screening and Thermal Up-shift Evaluation Journal of Computer-Aided Molecular Design. 19: 421-443. PMID 16231201 DOI: 10.1007/S10822-005-7969-7 |
0.383 |
|
| 2005 |
Lidón-Moya MC, Barrera FN, Bueno M, Pérez-Jiménez R, Sancho J, Mateu MG, Neira JL. An extensive thermodynamic characterization of the dimerization domain of the HIV-1 capsid protein. Protein Science : a Publication of the Protein Society. 14: 2387-404. PMID 16131662 DOI: 10.1110/Ps.041324305 |
0.329 |
|
| 2005 |
Alfonso P, PampÃn S, Estrada J, RodrÃguez-Rey JC, Giraldo P, Sancho J, Pocovà M. Miglustat (NB-DNJ) works as a chaperone for mutated acid beta-glucosidase in cells transfected with several Gaucher disease mutations. Blood Cells, Molecules & Diseases. 35: 268-76. PMID 16039881 DOI: 10.1016/J.Bcmd.2005.05.007 |
0.342 |
|
| 2005 |
Cremades N, Bueno M, Toja M, Sancho J. Towards a new therapeutic target: Helicobacter pylori flavodoxin. Biophysical Chemistry. 115: 267-276. PMID 15752617 DOI: 10.1016/J.Bpc.2004.12.045 |
0.338 |
|
| 2005 |
Campos LA, Cuesta-López S, López-Llano J, Falo F, Sancho J. A Double-Deletion Method to Quantifying Incremental Binding Energies in Proteins from Experiment: Example of a Destabilizing Hydrogen Bonding Pair Biophysical Journal. 88: 1311-1321. PMID 15556980 DOI: 10.1529/Biophysj.104.050203 |
0.386 |
|
| 2004 |
Nogues I, Campos LA, Sancho J, Gomez-Moreno C, Mayhew SG, Medina M. Role of neighboring FMN side chains in the modulation of flavin reduction potentials and in the energetics of the FMN:apoprotein interaction in Anabaena flavodoxin. Biochemistry. 43: 15111-15121. PMID 15568803 DOI: 10.1021/Bi0483256 |
0.763 |
|
| 2004 |
Campos LA, Bueno M, Lopez-Llano J, Jiménez MA, Sancho J. Structure of stable protein folding intermediates by equilibrium phi-analysis: the apoflavodoxin thermal intermediate. Journal of Molecular Biology. 344: 239-55. PMID 15504414 DOI: 10.1016/J.Jmb.2004.08.081 |
0.451 |
|
| 2004 |
Campos LA, Garcia-Mira MM, Godoy-Ruiz R, Sanchez-Ruiz JM, Sancho J. 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: 223-237. PMID 15504413 DOI: 10.1016/J.Jmb.2004.09.047 |
0.461 |
|
| 2004 |
López-Llano J, Maldonado S, Jain S, Lostao A, Godoy-Ruiz R, Sanchez-Ruiz JM, Cortijo M, Fernández-Recio J, Sancho J. 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. PMID 15317817 DOI: 10.1074/Jbc.M405791200 |
0.741 |
|
| 2004 |
López-Llano J, Maldonado S, Bueno M, Lostao A, Angeles-Jiménez M, Lillo MP, Sancho J. The long and short flavodoxins: I. The role of the differentiating loop in apoflavodoxin structure and FMN binding. The Journal of Biological Chemistry. 279: 47177-83. PMID 15317816 DOI: 10.1074/Jbc.M405792200 |
0.412 |
|
| 2003 |
Lostao A, Daoudi F, Irún MP, Ramon A, Fernández-Cabrera C, Romero A, Sancho J. How FMN binds to anabaena apoflavodoxin: a hydrophobic encounter at an open binding site. The Journal of Biological Chemistry. 278: 24053-61. PMID 12682068 DOI: 10.1074/Jbc.M301049200 |
0.392 |
|
| 2003 |
Campos LA, Sancho J. The active site of pepsin is formed in the intermediate conformation dominant at mildly acidic pH Febs Letters. 538: 89-95. PMID 12633859 DOI: 10.1016/S0014-5793(03)00152-2 |
0.365 |
|
| 2003 |
Bes MT, Sancho J, Peleato ML, Medina M, Gómez‐Moreno C, Fillat MF. Purification of colored photosynthetic proteins for understanding protein isolation principles Biochemistry and Molecular Biology Education. 31: 119-122. DOI: 10.1002/Bmb.2003.494031020202 |
0.322 |
|
| 2002 |
Sancho J, Bueno M, Campos LA, Fernández-Recio J, López J, Machicado C, Pedroso I, Toja M. The 'relevant' stability of proteins with equilibrium intermediates. The Scientific World Journal. 2: 1209-1215. PMID 12805903 DOI: 10.1100/Tsw.2002.196 |
0.736 |
|
| 2002 |
Machicado C, Bueno M, Sancho J. Predicting the structure of protein cavities created by mutation Protein Engineering. 15: 669-675. PMID 12364581 DOI: 10.1093/Protein/15.8.669 |
0.361 |
|
| 2002 |
Pedroso I, Irun MP, Machicado C, Sancho J. Four-state equilibrium unfolding of an scFv antibody fragment. Biochemistry. 41: 9873-9884. PMID 12146953 DOI: 10.1021/Bi025742E |
0.354 |
|
| 2002 |
Maldonado S, Irún MP, Campos LA, Rubio JA, Luquita A, Lostao A, Wang R, García-Moreno E B, Sancho J. Salt-induced stabilization of apoflavodoxin at neutral pH is mediated through cation-specific effects. Protein Science : a Publication of the Protein Society. 11: 1260-73. PMID 11967382 DOI: 10.1110/Ps.2980102 |
0.439 |
|
| 2002 |
Casaus JL, Navarro JA, Hervás M, Lostao A, De la Rosa MA, Gómez-Moreno C, Sancho J, Medina M. Anabaena sp. PCC 7119 flavodoxin as electron carrier from photosystem I to ferredoxin-NADP+ reductase. Role of Trp(57) and Tyr(94). The Journal of Biological Chemistry. 277: 22338-44. PMID 11950835 DOI: 10.1074/Jbc.M112258200 |
0.747 |
|
| 2001 |
Balme A, Hervás M, Campos LA, Sancho J, De la Rosa MA, Navarro JA. A comparative study of the thermal stability of plastocyanin, cytochrome c(6) and Photosystem I in thermophilic and mesophilic cyanobacteria. Photosynthesis Research. 70: 281-9. PMID 16252173 DOI: 10.1023/A:1014761524242 |
0.337 |
|
| 2001 |
Irún MP, Maldonado S, Sancho J. Stabilization of apoflavodoxin by replacing hydrogen-bonded charged Asp or Glu residues by the neutral isosteric Asn or Gln. Protein Engineering. 14: 173-81. PMID 11342714 DOI: 10.1093/Protein/14.3.173 |
0.398 |
|
| 2001 |
Langdon GM, Jiménez MA, Genzor CG, Maldonado S, Sancho J, Rico M. Anabaena apoflavodoxin hydrogen exchange: on the stable exchange core of the alpha/beta(21345) flavodoxin-like family. Proteins. 43: 476-88. PMID 11340663 DOI: 10.1002/Prot.1059 |
0.393 |
|
| 2001 |
Irún MP, Garcia-Mira MM, Sanchez-Ruiz JM, Sancho J. Native hydrogen bonds in a molten globule: the apoflavodoxin thermal intermediate. Journal of Molecular Biology. 306: 877-888. PMID 11243795 DOI: 10.1006/Jmbi.2001.4436 |
0.363 |
|
| 2000 |
Lostao A, Harrous ME, Daoudi F, Romero A, Parody-Morreale A, Sancho J. Dissecting the Energetics of the Apoflavodoxin-FMN Complex Journal of Biological Chemistry. 275: 9518-9526. PMID 10734100 DOI: 10.1074/Jbc.275.13.9518 |
0.377 |
|
| 1999 |
Medina M, Lostao A, Sancho J, Gómez-Moreno C, Cammack R, Alonso PJ, Martínez JI. Electron-nuclear double resonance and hyperfine sublevel correlation spectroscopic studies of flavodoxin mutants from Anabaena sp. PCC 7119. Biophysical Journal. 77: 1712-1720. PMID 10465780 DOI: 10.1016/S0006-3495(99)77017-7 |
0.35 |
|
| 1999 |
Fernández-Recio J, Romero A, Sancho J. Energetics of a hydrogen bond (charged and neutral) and of a cation-pi interaction in apoflavodoxin. Journal of Molecular Biology. 290: 319-330. PMID 10388575 DOI: 10.1006/Jmbi.1999.2863 |
0.344 |
|
| 1998 |
Maldonado S, Lostao A, Irún MP, Férnandez-Recio J, Gustavo Genzor C, Begoña González E, Rubio JA, Luquita A, Daoudi F, Sancho J. Apoflavodoxin: structure, stability, and FMN binding. Biochimie. 80: 813-20. PMID 9893940 DOI: 10.1016/S0300-9084(00)88876-8 |
0.484 |
|
| 1998 |
Maldonado S, Jiménez MA, Langdon GM, Sancho J. Cooperative stabilization of a molten globule apoflavodoxin fragment. Biochemistry. 37: 10589-96. PMID 9692948 DOI: 10.1021/Bi980368X |
0.417 |
|
| 1998 |
Fernández-Recio J, Sancho J. Intrahelical side chain interactions in α-helices: poor correlation between energetics and frequency Febs Letters. 429: 99-103. PMID 9657391 DOI: 10.1016/S0014-5793(98)00569-9 |
0.408 |
|
| 1997 |
Lostao A, Gómez-Moreno C, Mayhew SG, Sancho J. Differential Stabilization of the Three FMN Redox Forms by Tyrosine 94 and Tryptophan 57 in Flavodoxin from Anabaena and Its Influence on the Redox Potentials Biochemistry. 36: 14334-14344. PMID 9398151 DOI: 10.1021/Bi971384H |
0.436 |
|
| 1997 |
Fernández-Recio J, Vázquez A, Civera C, Sevilla P, Sancho J. The Tryptophan/Histidine interaction in α-helices Journal of Molecular Biology. 267: 184-197. PMID 9096217 DOI: 10.1006/Jmbi.1996.0831 |
0.439 |
|
| 1996 |
Genzor CG, Beldarraín A, Gómez-Moreno C, López-Lacomba JL, Cortijo M, Sancho J. Conformational stability of apoflavodoxin. Protein Science : a Publication of the Protein Society. 5: 1376-88. PMID 8819170 DOI: 10.1002/Pro.5560050716 |
0.385 |
|
| 1996 |
Genzor CG, Perales-Alcón A, Sancho J, Romero A. Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin Nature Structural & Molecular Biology. 3: 329-332. PMID 8599758 DOI: 10.1038/Nsb0496-329 |
0.357 |
|
| 1994 |
Kippen AD, Sancho J, Fersht AR. Folding of barnase in parts. Biochemistry. 33: 3778-3786. PMID 8142379 DOI: 10.1021/Bi00178A039 |
0.557 |
|
| 1993 |
Vuilleumier S, Sancho J, Loewenthal R, Fersht AR. Circular Dichroism Studies of Barnase and Its Mutants: Characterization of the Contribution of Aromatic Side Chains Biochemistry. 32: 10303-10313. PMID 8399173 DOI: 10.1021/Bi00090A005 |
0.559 |
|
| 1993 |
Loewenthal R, Sancho J, Reinikainen T, Fersht AR. Long-range surface charge-charge interactions in proteins. Comparison of experimental results with calculations from a theoretical method. Journal of Molecular Biology. 232: 574-583. PMID 8345524 DOI: 10.1006/Jmbi.1993.1412 |
0.532 |
|
| 1993 |
Fersht AR, Matouschek A, Sancho J, Serrano L, Vuilleumier S. Pathway of protein folding. Faraday Discussions. 183-93. PMID 1290932 DOI: 10.1039/Fd9929300183 |
0.409 |
|
| 1992 |
Willaert K, Loewenthal R, Sancho J, Froeyen M, Fersht A, Engelborghs Y. Determination of the excited-state lifetimes of the tryptophan residues in barnase, via multifrequency phase fluorometry of tryptophan mutants. Biochemistry. 31: 711-716. PMID 1731927 DOI: 10.1021/Bi00118A011 |
0.513 |
|
| 1992 |
Loewenthal R, Sancho J, Fersht AR. Histidine-aromatic interactions in barnase. Elevation of histidine pKa and contribution to protein stability. Journal of Molecular Biology. 224: 759-770. PMID 1569555 DOI: 10.1016/0022-2836(92)90560-7 |
0.45 |
|
| 1992 |
Sancho J, Neira JL, Fersht AR. An N-terminal fragment of barnase has residual helical structure similar to that in a refolding intermediate. Journal of Molecular Biology. 224: 749-758. PMID 1569554 DOI: 10.1016/0022-2836(92)90559-3 |
0.394 |
|
| 1992 |
Sancho J, Fersht AR. Dissection of an enzyme by protein engineering. The N and C-terminal fragments of barnase form a native-like complex with restored enzymic activity. Journal of Molecular Biology. 224: 741-747. PMID 1569553 DOI: 10.1016/0022-2836(92)90558-2 |
0.563 |
|
| 1992 |
Serrano L, Neira JL, Sancho J, Fersht AR. Effect of alanine versus glycine in alpha-helices on protein stability. Nature. 356: 453-5. PMID 1557131 DOI: 10.1038/356453A0 |
0.591 |
|
| 1992 |
Sancho J, Serrano L, Fersht AR. Histidine residues at the N- and C-termini of alpha-helices: perturbed pKas and protein stability. Biochemistry. 31: 2253-8. PMID 1540580 DOI: 10.1021/Bi00123A006 |
0.568 |
|
| 1992 |
Serrano L, Sancho J, Hirshberg M, Fersht AR. Alpha-helix stability in proteins. I. Empirical correlations concerning substitution of side-chains at the N and C-caps and the replacement of alanine by glycine or serine at solvent-exposed surfaces. Journal of Molecular Biology. 227: 544-59. PMID 1404368 DOI: 10.1016/0022-2836(92)90906-Z |
0.542 |
|
| 1991 |
Loewenthal R, Sancho J, Fersht AR. Fluorescence spectrum of barnase: contributions of three tryptophan residues and a histidine-related pH dependence. Biochemistry. 30: 6775-6779. PMID 2065058 DOI: 10.1021/Bi00241A021 |
0.536 |
|
| 1991 |
Sancho J, Gómez-Moreno C. Interaction of ferredoxin-NADP+ reductase from Anabaena with its substrates. Archives of Biochemistry and Biophysics. 288: 231-238. PMID 1910307 DOI: 10.1016/0003-9861(91)90189-P |
0.36 |
|
| 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 |
0.729 |
|
| 1990 |
Sancho J, Medina M, Gómez‐Moreno C. Arginyl groups involved in the binding of Anabaena ferredoxin–NADP+ reductase to NADP+ and to ferredoxin Febs Journal. 187: 39-48. PMID 2105214 DOI: 10.1111/J.1432-1033.1990.Tb15275.X |
0.357 |
|
| 1989 |
Pueyo JJ, Sancho J, Edmondson DE, Gomez-Moreno C. Preparation and properties of a cross-linked complex between ferredoxin-NADP+ reductase and flavodoxin European Journal of Biochemistry. 183: 539-544. PMID 2506011 DOI: 10.1111/J.1432-1033.1989.Tb21082.X |
0.315 |
|
| 1988 |
Sancho J, Peleato ML, Gomez-Moreno C, Edmondson DE. Purification and properties of ferredoxin-NADP+ oxidoreductase from the nitrogen-fixing cyanobacteria Anabaena variabilis Archives of Biochemistry and Biophysics. 260: 200-207. PMID 3124746 DOI: 10.1016/0003-9861(88)90441-9 |
0.314 |
|
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