Year |
Citation |
Score |
2020 |
Fernández A. Artificial intelligence teaches drugs to target proteins by tackling the induced folding problem. Molecular Pharmaceutics. PMID 32551659 DOI: 10.1021/Acs.Molpharmaceut.0C00470 |
0.325 |
|
2019 |
Fernández A. Artificial Intelligence Steering Molecular Therapy in the Absence of Information on Target Structure and Regulation. Journal of Chemical Information and Modeling. PMID 31738539 DOI: 10.1021/Acs.Jcim.9B00651 |
0.327 |
|
2019 |
Fernández A. Protein structural defects enable pharmaceutical targeting while functionalizing the M2 proton channel. Biochemical and Biophysical Research Communications. PMID 31023526 DOI: 10.1016/J.Bbrc.2019.04.094 |
0.318 |
|
2016 |
Fernández A. Non-Debye frustrated hydration steers biomolecular association: Interfacial tension for the drug designer. Febs Letters. PMID 27616564 DOI: 10.1002/1873-3468.12418 |
0.351 |
|
2015 |
Fernández A. Packing defects functionalize soluble proteins. Febs Letters. 589: 967-73. PMID 25771861 DOI: 10.1016/J.Febslet.2015.03.002 |
0.312 |
|
2015 |
Fernandez A. Evolutionary Roots of Proteomic Complexity and Lessons for the Drug Designer Journal of Pharmacogenomics and Pharmacoproteomics. 6. DOI: 10.4172/2153-0645.1000E145 |
0.352 |
|
2014 |
Fernández A. Communication: Chemical functionality of interfacial water enveloping nanoscale structural defects in proteins. The Journal of Chemical Physics. 140: 221102. PMID 24929366 DOI: 10.1063/1.4882895 |
0.312 |
|
2014 |
Montes de Oca J, Rodriguez Fris A, Appignanesi G, Fernández A. Productive induced metastability in allosteric modulation of kinase function. The Febs Journal. 281: 3079-91. PMID 24823615 DOI: 10.1111/Febs.12844 |
0.305 |
|
2014 |
Fernández A. Water promotes the sealing of nanoscale packing defects in folding proteins. Journal of Physics. Condensed Matter : An Institute of Physics Journal. 26: 202101. PMID 24769440 DOI: 10.1088/0953-8984/26/20/202101 |
0.35 |
|
2013 |
Fernández A. The principle of minimal episteric distortion of the water matrix and its steering role in protein folding. The Journal of Chemical Physics. 139: 085101. PMID 24007038 DOI: 10.1063/1.4818874 |
0.345 |
|
2012 |
Fernández A. Communication: Nanoscale electrostatic theory of epistructural fields at the protein-water interface. The Journal of Chemical Physics. 137: 231101. PMID 23267464 DOI: 10.1063/1.4772603 |
0.323 |
|
2012 |
Accordino SR, Fris JAR, Appignanesi GA, Fernández A. A unifying motif of intermolecular cooperativity in protein associations European Physical Journal E. 35: 59. PMID 22791307 DOI: 10.1140/Epje/I2012-12059-0 |
0.333 |
|
2012 |
Fernández A. Epistructural tension promotes protein associations. Physical Review Letters. 108: 188102. PMID 22681121 DOI: 10.1103/Physrevlett.108.188102 |
0.35 |
|
2012 |
Accordino SR, Morini MA, Sierra MB, Fris JA, Appignanesi GA, Fernández A. Wrapping mimicking in drug-like small molecules disruptive of protein-protein interfaces. Proteins. 80: 1755-65. PMID 22422633 DOI: 10.1002/Prot.24069 |
0.333 |
|
2012 |
Fernández A. Communication: epistructural thermodynamics of soluble proteins. The Journal of Chemical Physics. 136: 091101. PMID 22401421 DOI: 10.1063/1.3691890 |
0.372 |
|
2012 |
Fernández A, Fraser C, Scott LR. Purposely engineered drug-target mismatches for entropy-based drug optimization. Trends in Biotechnology. 30: 1-7. PMID 21907435 DOI: 10.1016/J.Tibtech.2011.07.003 |
0.305 |
|
2010 |
Schulz E, Frechero M, Appignanesi G, Fernández A. Sub-nanoscale surface ruggedness provides a water-tight seal for exposed regions in soluble protein structure. Plos One. 5. PMID 20862253 DOI: 10.1371/Journal.Pone.0012844 |
0.352 |
|
2010 |
Fernández A, Berry RS. Golden rule for buttressing vulnerable soluble proteins. Journal of Proteome Research. 9: 2643-8. PMID 20364868 DOI: 10.1021/Pr100089T |
0.336 |
|
2009 |
Fernández A, Chen J. Human capacitance to dosage imbalance: coping with inefficient selection. Genome Research. 19: 2185-92. PMID 19819908 DOI: 10.1101/Gr.094441.109 |
0.419 |
|
2009 |
Fernández A, Bazán S, Chen J. Taming the induced folding of drug-targeted kinases. Trends in Pharmacological Sciences. 30: 66-71. PMID 19097649 DOI: 10.1016/J.Tips.2008.11.001 |
0.44 |
|
2008 |
Despa F, Fernández A, Scott LR, Berry RS. Hydration profiles of amyloidogenic molecular structures. Journal of Biological Physics. 34: 577-90. PMID 19669515 DOI: 10.1007/S10867-008-9122-Z |
0.311 |
|
2008 |
Fernández A, Zhang X, Chen J. Folding and wrapping soluble proteins exploring the molecular basis of cooperativity and aggregation. Progress in Molecular Biology and Translational Science. 83: 53-87. PMID 19186252 DOI: 10.1016/S0079-6603(08)00602-8 |
0.489 |
|
2008 |
Fernández A, Crespo A. Protein wrapping: a molecular marker for association, aggregation and drug design. Chemical Society Reviews. 37: 2373-82. PMID 18949110 DOI: 10.1039/B804150B |
0.351 |
|
2008 |
Crespo A, Zhang X, Fernández A. Redesigning kinase inhibitors to enhance specificity. Journal of Medicinal Chemistry. 51: 4890-8. PMID 18680272 DOI: 10.1021/Jm800453A |
0.307 |
|
2008 |
Chen J, Liang H, Fernández A. Protein structure protection commits gene expression patterns. Genome Biology. 9: R107. PMID 18606003 DOI: 10.1186/Gb-2008-9-7-R107 |
0.418 |
|
2008 |
Crespo A, Fernández A. Induced disorder in protein-ligand complexes as a drug-design strategy. Molecular Pharmaceutics. 5: 430-7. PMID 18278867 DOI: 10.1021/Mp700148H |
0.309 |
|
2008 |
Liang H, Plazonic KR, Chen J, Li WH, Fernández A. Protein under-wrapping causes dosage sensitivity and decreases gene duplicability. Plos Genetics. 4: e11. PMID 18208334 DOI: 10.1371/Journal.Pgen.0040011 |
0.448 |
|
2007 |
Fernández A, Sanguino A, Peng Z, Ozturk E, Chen J, Crespo A, Wulf S, Shavrin A, Qin C, Ma J, Trent J, Lin Y, Han HD, Mangala LS, Bankson JA, et al. An anticancer C-Kit kinase inhibitor is reengineered to make it more active and less cardiotoxic. The Journal of Clinical Investigation. 117: 4044-54. PMID 18060038 DOI: 10.1172/Jci32373 |
0.397 |
|
2007 |
Pietrosemoli N, Crespo A, Fernandez A. Dehydration propensity of order-disorder intermediate regions in soluble proteins. Journal of Proteome Research. 6: 3519-26. PMID 17672484 DOI: 10.1021/Pr070208K |
0.347 |
|
2007 |
Fernández A, Chen J, Crespo A. Solvent-exposed backbone loosens the hydration shell of soluble folded proteins. The Journal of Chemical Physics. 126: 245103. PMID 17614591 DOI: 10.1063/1.2745795 |
0.476 |
|
2007 |
Chen J, Zhang X, Fernández A. Molecular basis for specificity in the druggable kinome: sequence-based analysis. Bioinformatics (Oxford, England). 23: 563-72. PMID 17255140 DOI: 10.1093/Bioinformatics/Btl666 |
0.443 |
|
2006 |
Maddipati S, Fernández A. Feature-similarity protein classifier as a ligand engineering tool. Biomolecular Engineering. 23: 307-15. PMID 17110166 DOI: 10.1016/J.Bioeng.2006.09.004 |
0.31 |
|
2006 |
Fernández A, Scott R, Berry RS. Packing defects as selectivity switches for drug-based protein inhibitors. Proceedings of the National Academy of Sciences of the United States of America. 103: 323-8. PMID 16387853 DOI: 10.1073/Pnas.0509351102 |
0.316 |
|
2005 |
Fernández A, Tawfik DS, Berkhout B, Sanders R, Kloczkowski A, Sen T, Jernigan B. Protein promiscuity: drug resistance and native functions--HIV-1 case. Journal of Biomolecular Structure & Dynamics. 22: 615-24. PMID 15842167 DOI: 10.1080/07391102.2005.10531228 |
0.329 |
|
2004 |
Fernández A. Buffering the entropic cost of hydrophobic collapse in protein chains. The Journal of Chemical Physics. 121: 11501-2. PMID 15634110 DOI: 10.1063/1.1814079 |
0.318 |
|
2004 |
Fernández A, Berry RS. Molecular dimension explored in evolution to promote proteomic complexity. Proceedings of the National Academy of Sciences of the United States of America. 101: 13460-5. PMID 15347802 DOI: 10.1073/Pnas.0405585101 |
0.336 |
|
2004 |
Fernández A, Rogale K, Scott R, Scheraga HA. Inhibitor design by wrapping packing defects in HIV-1 proteins. Proceedings of the National Academy of Sciences of the United States of America. 101: 11640-5. PMID 15289598 DOI: 10.1073/Pnas.0404641101 |
0.302 |
|
2004 |
Fernández A. Functionality of wrapping defects in soluble proteins: what cannot be kept dry must be conserved. Journal of Molecular Biology. 337: 477-83. PMID 15003461 DOI: 10.1016/J.Jmb.2004.01.050 |
0.339 |
|
2004 |
Fernández A, Scott R, Berry RS. The nonconserved wrapping of conserved protein folds reveals a trend toward increasing connectivity in proteomic networks. Proceedings of the National Academy of Sciences of the United States of America. 101: 2823-7. PMID 14978274 DOI: 10.1073/Pnas.0308295100 |
0.35 |
|
2004 |
Fernández A, Rogale K. Sequence-space selection of cooperative model proteins Journal of Physics A. 37. DOI: 10.1088/0305-4470/37/18/L02 |
0.323 |
|
2004 |
Rogale K, Fernández A. Protein folding: a good structure protector is also a good structure seeker Physics Letters A. 321: 263-266. DOI: 10.1016/J.Physleta.2003.12.047 |
0.345 |
|
2003 |
Fernández A, Scott R. Dehydron: a structurally encoded signal for protein interaction. Biophysical Journal. 85: 1914-28. PMID 12944304 DOI: 10.1016/S0006-3495(03)74619-0 |
0.366 |
|
2003 |
Fernández A, Scott LR. Adherence of packing defects in soluble proteins. Physical Review Letters. 91: 018102. PMID 12906578 DOI: 10.1103/Physrevlett.91.018102 |
0.314 |
|
2003 |
Fernández A. Oncogenic mutations and packing defects in protein structure. Journal of Biomolecular Structure & Dynamics. 21: 9-14. PMID 12854955 DOI: 10.1080/07391102.2003.10506901 |
0.335 |
|
2003 |
Fernández A, Kardos J, Scott LR, Goto Y, Berry RS. Structural defects and the diagnosis of amyloidogenic propensity. Proceedings of the National Academy of Sciences of the United States of America. 100: 6446-51. PMID 12743379 DOI: 10.1073/Pnas.0731893100 |
0.332 |
|
2003 |
Fernández A, Berry RS. Proteins with H-bond packing defects are highly interactive with lipid bilayers: Implications for amyloidogenesis. Proceedings of the National Academy of Sciences of the United States of America. 100: 2391-6. PMID 12591960 DOI: 10.1073/Pnas.0335642100 |
0.319 |
|
2003 |
Fernández A, Kardos J, Goto Y. Protein folding: could hydrophobic collapse be coupled with hydrogen-bond formation? Febs Letters. 536: 187-92. PMID 12586361 DOI: 10.1016/S0014-5793(03)00056-5 |
0.3 |
|
2003 |
Fernández A, Shen MY, Colubri A, Sosnick TR, Berry RS, Freed KF. Large-scale context in protein folding: villin headpiece. Biochemistry. 42: 664-71. PMID 12534278 DOI: 10.1021/Bi026510I |
0.346 |
|
2003 |
Fernández A, Scheraga HA. Insufficiently dehydrated hydrogen bonds as determinants of protein interactions. Proceedings of the National Academy of Sciences of the United States of America. 100: 113-8. PMID 12518060 DOI: 10.1073/Pnas.0136888100 |
0.33 |
|
2003 |
Fernández A, Scott LR. Under-wrapped soluble proteins as signals triggering membrane morphology Journal of Chemical Physics. 119: 6911-6915. DOI: 10.1063/1.1605734 |
0.318 |
|
2003 |
Fernández A, Scott LR, Scheraga HA. Amino Acid Residues at Protein-Protein Interfaces: Why Is Propensity so Different from Relative Abundance? Journal of Physical Chemistry B. 107: 9929-9932. DOI: 10.1021/Jp0348124 |
0.347 |
|
2002 |
Fernández A, Belinky A, Boland Mde L. Protein folding: where is the paradox? Journal of Biomolecular Structure & Dynamics. 20: 331-2. PMID 12437371 DOI: 10.1080/07391102.2002.10506851 |
0.302 |
|
2002 |
Fernández A, Berry RS. Extent of hydrogen-bond protection in folded proteins: a constraint on packing architectures. Biophysical Journal. 83: 2475-81. PMID 12414681 DOI: 10.1016/S0006-3495(02)75258-2 |
0.32 |
|
2002 |
Fernández A, de las Mercedes Boland M. Solvent environment conducive to protein aggregation. Febs Letters. 529: 298-301. PMID 12372617 DOI: 10.1016/S0014-5793(02)03392-6 |
0.334 |
|
2002 |
Fernández A. Desolvation shell of hydrogen bonds in folded proteins, protein complexes and folding pathways. Febs Letters. 527: 166-70. PMID 12220654 DOI: 10.1016/S0014-5793(02)03204-0 |
0.349 |
|
2002 |
Sosnick TR, Berry RS, Colubri A, Fernández A. Distinguishing foldable proteins from nonfolders: when and how do they differ? Proteins. 49: 15-23. PMID 12211012 DOI: 10.1002/Prot.10193 |
0.363 |
|
2002 |
Fernández A, Sosnick TR, Colubri A. Dynamics of hydrogen bond desolvation in protein folding. Journal of Molecular Biology. 321: 659-75. PMID 12206781 DOI: 10.1016/S0022-2836(02)00679-4 |
0.334 |
|
2002 |
Fernández A. Insufficient hydrogen-bond desolvation and prion-related disease. European Journal of Biochemistry / Febs. 269: 4165-8. PMID 12199693 DOI: 10.1046/J.1432-1033.2002.03116.X |
0.322 |
|
2002 |
Fernández A, Colubri A. Pathway heterogeneity in protein folding. Proteins. 48: 293-310. PMID 12112697 DOI: 10.1002/Prot.10155 |
0.379 |
|
2002 |
Fernández A. How do we probe ubiquitin's pathway heterogeneity? Journal of Biomolecular Structure & Dynamics. 19: 949-60. PMID 12023798 DOI: 10.1080/07391102.2002.10506799 |
0.328 |
|
2002 |
Fernández A. Time-resolved backbone desolvation and mutational hot spots in folding proteins. Proteins. 47: 447-57. PMID 12001223 DOI: 10.1002/Prot.10109 |
0.374 |
|
2002 |
Colubri A, Fernández A. Pathway diversity and concertedness in protein folding: an ab-initio approach. Journal of Biomolecular Structure & Dynamics. 19: 739-64. PMID 11922833 DOI: 10.1080/07391102.2002.10506782 |
0.383 |
|
2002 |
Fernández A. Protein folding: is hierarchical versus nonhierarchical a productive issue? Journal of Biomolecular Structure & Dynamics. 19: 735-7. PMID 11922832 DOI: 10.1080/07391102.2002.10506781 |
0.314 |
|
2002 |
Fernández A. Protein design from in silico dynamic information: the emergence of the 'turn-dock-lock' motif. Protein Engineering. 15: 1-6. PMID 11842231 DOI: 10.1093/Protein/15.1.1 |
0.342 |
|
2002 |
Fernández A. Local solvent dielectrics and destabilization of solvent-exposed states in folding proteins Physica a-Statistical Mechanics and Its Applications. 316: 77-86. DOI: 10.1016/S0378-4371(02)01026-9 |
0.359 |
|
2002 |
Fernández A. Evolving solvent contexts in protein folding: modeling the self-protecting chain Physica a-Statistical Mechanics and Its Applications. 308: 80-88. DOI: 10.1016/S0378-4371(02)00605-2 |
0.344 |
|
2002 |
Fernández A, Colubri A, Berry RS. Three-body correlations in protein folding: the origin of cooperativity Physica a-Statistical Mechanics and Its Applications. 307: 235-259. DOI: 10.1016/S0378-4371(01)00586-6 |
0.344 |
|
2002 |
Fernández A. The protective shell of a hydrogen bond: a motif in protein folding pathways Physics Letters A. 302: 144-148. DOI: 10.1016/S0375-9601(02)01118-0 |
0.31 |
|
2002 |
Fernández A. Intramolecular modulation of electric fields in folding proteins Physics Letters A. 299: 217-220. DOI: 10.1016/S0375-9601(02)00609-6 |
0.321 |
|
2001 |
Fernández A, Colubri A, Appignanesi G. Semiempirical prediction of protein folds. Physical Review E. 64: 21901. PMID 11497614 DOI: 10.1103/Physreve.64.021901 |
0.37 |
|
2001 |
Fernández A, Ramsden JJ. On adsorption-induced denaturation of folded proteins. Journal of Biological Physics and Chemistry. 1: 81-84. DOI: 10.4024/12Fe01L.01.02 |
0.342 |
|
2001 |
Fernández A. Protein folding: coming to terms with cooperativity Journal of Biological Physics and Chemistry. 1: 10-11. DOI: 10.4024/05Fe01R.01.01 |
0.334 |
|
2001 |
Fernández A. Cooperative walks in a cubic lattice: Protein folding as a many-body problem Journal of Chemical Physics. 115: 7293-7297. DOI: 10.1063/1.1405447 |
0.364 |
|
2001 |
Fernández A, Appignanesi G. Ribonucleic acid folder: The earliest moves of a good structure seeker Journal of Chemical Physics. 114: 9184-9191. DOI: 10.1063/1.1370072 |
0.312 |
|
2001 |
Fernández A, Appignanesi GA, Colubri A. Finding the collapse-inducing nucleus in a folding protein Journal of Chemical Physics. 114: 8678-8684. DOI: 10.1063/1.1368134 |
0.355 |
|
2001 |
Fernández A, Colubri A, Berry RS. Topologies to geometries in protein folding: Hierarchical and nonhierarchical scenarios Journal of Chemical Physics. 114: 5871-5887. DOI: 10.1063/1.1350660 |
0.354 |
|
2001 |
Fernández A. Conformation-dependent environments in folding proteins Journal of Chemical Physics. 114: 2489-2502. DOI: 10.1063/1.1338507 |
0.337 |
|
2001 |
Fernández A, Colubri A, Appignanesi G, Burastero T. Coarse semiempirical solution to the protein folding problem Physica a-Statistical Mechanics and Its Applications. 293: 358-384. DOI: 10.1016/S0378-4371(00)00613-0 |
0.37 |
|
2001 |
Fernández A. Protein folding cooperativity in the correlated lattice Physics Letters A. 290: 101-105. DOI: 10.1016/S0375-9601(01)00627-2 |
0.332 |
|
2001 |
Berry RS, Fernandez A, Kostov K. Connecting cluster dynamics and protein folding European Physical Journal D. 16: 47-50. DOI: 10.1007/S100530170057 |
0.315 |
|
2000 |
Fernández A, Colubri A, Berry RS. Topology to geometry in protein folding: beta-lactoglobulin. Proceedings of the National Academy of Sciences of the United States of America. 97: 14062-6. PMID 11114189 DOI: 10.1073/Pnas.260359997 |
0.343 |
|
2000 |
Fernández A, Colubri A. Renormalized Hamiltonian for a peptide chain: Digitalizing the protein folding problem Journal of Mathematical Physics. 41: 2593-2603. DOI: 10.1063/1.533314 |
0.328 |
|
2000 |
Fernández A, Kostov KS, Berry RS. Coarsely resolved topography along protein folding pathways The Journal of Chemical Physics. 112: 5223-5229. DOI: 10.1063/1.481077 |
0.355 |
|
2000 |
Fernández A, Berry RS. Self-organization and mismatch tolerance in protein folding: General theory and an application The Journal of Chemical Physics. 112: 5212-5222. DOI: 10.1063/1.481076 |
0.376 |
|
2000 |
Fernández A. Digitalizing the backbone torsional dynamics of a folding protein Physical Chemistry Chemical Physics. 2: 1375-1384. DOI: 10.1039/A908626I |
0.337 |
|
1999 |
Fernández A, Burastero T, Salthú R, Tablar A. Energy-level statistics in the fine conformational resolution of RNA folding dynamics. Physical Review E. 60: 5888-5893. PMID 11970489 DOI: 10.1103/Physreve.60.5888 |
0.353 |
|
1999 |
Fernández A, Colubri A. Nucleation theory for helix unfolding in peptide chains. Physical Review E. 60: 4645-4651. PMID 11970326 DOI: 10.1103/Physreve.60.4645 |
0.339 |
|
1999 |
Fernández A, Salthú R, Cendra H. Discretized torsional dynamics and the folding of an RNA chain. Physical Review E. 60: 2105-2119. PMID 11970003 DOI: 10.1103/Physreve.60.2105 |
0.384 |
|
1999 |
Fernández A. Folding a protein by discretizing its backbone torsional dynamics. Physical Review E. 59: 5928-5939. PMID 11969574 DOI: 10.1103/Physreve.59.5928 |
0.376 |
|
1999 |
Fernández A, Colubri A, Burastero T, Tablar A. How large should proteins be? The minimal size of a good structure seeker Physical Chemistry Chemical Physics. 1: 4347-4354. DOI: 10.1039/A903594J |
0.382 |
|
1999 |
Fernández A. Coarse graining the soft-mode dynamics of a folding protein Physical Chemistry Chemical Physics. 1: 861-869. DOI: 10.1039/A807864E |
0.376 |
|
1998 |
Fernández A, Niel B, Burastero T. The RNA folding problem: a variational problem within an adiabatic approximation. Biophysical Chemistry. 74: 89-98. PMID 9760721 DOI: 10.1016/S0301-4622(98)00168-9 |
0.359 |
|
1998 |
Fernández A, Colubri A. Microscopic dynamics from a coarsely defined solution to the protein folding problem Journal of Mathematical Physics. 39: 3167-3187. DOI: 10.1063/1.532246 |
0.357 |
|
1998 |
Fernández A. The Lagrangian Structure of Long-Time Torsional Dynamics Leading to RNA Folding Journal of Statistical Physics. 92: 237-267. DOI: 10.1023/A:1023051804215 |
0.367 |
|
1998 |
Appignanesi G, Fernández A. A variational approach to relaxation in ultrametric spaces Physica a-Statistical Mechanics and Its Applications. 256: 359-368. DOI: 10.1016/S0378-4371(98)00195-2 |
0.346 |
|
1998 |
Fernández A, Colubri A. Semiempirical variational approach to RNA folding Physica a-Statistical Mechanics and Its Applications. 248: 336-352. DOI: 10.1016/S0378-4371(97)00527-X |
0.363 |
|
1998 |
Fernández A, Burastero T. Coarsely defined solution to the protein folding problem Il Nuovo Cimento D. 20: 1891-1910. DOI: 10.1007/Bf03036605 |
0.38 |
|
1996 |
Fernández A, Belinky A. Sequentially folded SV-11 RNA: metastability is relevant to biological function. Biophysical Chemistry. 61: 101-105. PMID 8956484 DOI: 10.1016/S0301-4622(96)02189-8 |
0.317 |
|
1996 |
Fernández A, Appignanesi G. Magnesium-aided folding of group I ribozymes with a minimal loss of entropy Biophysical Chemistry. 61: 51-58. PMID 8855359 DOI: 10.1016/0301-4622(96)02190-4 |
0.327 |
|
1996 |
Fernández A, Cendra H. In vitro RNA folding: the principle of sequential minimization of entropy loss at work Biophysical Chemistry. 58: 335-339. PMID 8820414 DOI: 10.1016/0301-4622(95)00134-4 |
0.342 |
|
1996 |
Fernández A. Statistical folding dynamics for random heteropolymers Journal of Physics A. 29. DOI: 10.1088/0305-4470/29/20/004 |
0.3 |
|
1996 |
Appignanesi GA, Fernández A. Cooperativity along kinetic pathways in RNA folding Journal of Physics A. 29: 6265-6280. DOI: 10.1088/0305-4470/29/19/012 |
0.343 |
|
1996 |
Fernández A, Belinky A. Information generation and the loss of conformational entropy during RNA folding Journal of Physics A. 29. DOI: 10.1088/0305-4470/29/17/003 |
0.325 |
|
1996 |
Fernández A. The expediency of RNA folding as revealed by the maximization in information content Physica a-Statistical Mechanics and Its Applications. 233: 226-234. DOI: 10.1016/S0378-4371(96)00236-1 |
0.317 |
|
1996 |
Cendra H, Fernández A, Reartes W. A geometric framework for polymer folding Journal of Mathematical Chemistry. 19: 331-336. DOI: 10.1007/Bf01166723 |
0.306 |
|
1996 |
Fernández A, Appignanesi G. An action principle for biopolymer folding in vitro : A new perspective on the design of expeditiously-folded RNA molecules Journal of Mathematical Chemistry. 20: 95-116. DOI: 10.1007/Bf01165158 |
0.359 |
|
1995 |
Fernández A, Arias H, Guerín D. Folding RNA with the minimal loss of entropy Physical Review E. 52. DOI: 10.1103/Physreve.52.R1299 |
0.337 |
|
1995 |
Fernández A, Appignanesi G, Cendra H. What size RNA loop holds bulk solvent Chemical Physics Letters. 242: 460-464. DOI: 10.1016/0009-2614(95)00776-Z |
0.333 |
|
1995 |
Fernández A, Rabitz H. Statistical mechanics on the space of kinetic folding pathways Il Nuovo Cimento D. 17: 983-991. DOI: 10.1007/Bf02456786 |
0.336 |
|
1995 |
Fernández A. Towards an action principle governing biopolymer folding in vitro Journal of Mathematical Chemistry. 17: 401-410. DOI: 10.1007/Bf01165758 |
0.318 |
|
1995 |
Fernández A. The statistical mechanics of kinetically‐controlled RNA folding pathways Annalen Der Physik. 507: 600-620. DOI: 10.1002/Andp.19955070606 |
0.352 |
|
1994 |
Fernández A. Describing RNA sequential folding by dynamic coarse graining of the extended conformation space. Physical Review E. 50: 2435-2438. PMID 9962276 DOI: 10.1103/Physreve.50.R2435 |
0.306 |
|
1994 |
Fernández A. Stress localization in the RNA backbone: a mechanical footprint for predicting base-backbone tertiary contacts. Journal of Theoretical Biology. 166: 443-452. PMID 7513774 DOI: 10.1006/Jtbi.1994.1039 |
0.33 |
|
1994 |
Fernandez A. Ascribing weights to folding histories: explaining the expediency of biopolymer folding Journal of Physics A. 27: 6039-6052. DOI: 10.1088/0305-4470/27/18/014 |
0.323 |
|
1994 |
Fernández A. A measure on the space of RNA folding pathways: towards a new scheme of statistical inference Physica a-Statistical Mechanics and Its Applications. 210: 403-414. DOI: 10.1016/0378-4371(94)90088-4 |
0.349 |
|
1994 |
Fernández A. Memorizing all significant foldings of a random RNA chain Physica a-Statistical Mechanics and Its Applications. 203: 359-368. DOI: 10.1016/0378-4371(94)90004-3 |
0.343 |
|
1993 |
Fernández A. A dynamical model for ribozyme function based on the sequential folding of pre-mRNA transcripts. Journal of Biochemistry. 113: 22-28. PMID 8454569 DOI: 10.1093/Oxfordjournals.Jbchem.A123997 |
0.333 |
|
1993 |
Fernandez A, Lewin AS, Rabitz H. Structure-induced strain determining the internal cyclization site in the yeast cobI5 autocatalytic intron: Theory and experimental tests Journal of Theoretical Biology. 164: 121-133. PMID 8264241 DOI: 10.1006/Jtbi.1993.1143 |
0.321 |
|
1993 |
Fernández A. Learning to fold RNA with parallel processors Physica a-Statistical Mechanics and Its Applications. 201: 557-572. DOI: 10.1016/0378-4371(93)90128-Q |
0.317 |
|
1993 |
Fernández A, Tovar LGM. Coarse-grained dynamics for proton exchange in RNA Chemical Physics Letters. 208: 148-152. DOI: 10.1016/0009-2614(93)89053-K |
0.31 |
|
1993 |
Fernández A, Belinky A. Learning to fold a random RNA chain Chemical Physics Letters. 212: 201-204. DOI: 10.1016/0009-2614(93)87130-U |
0.345 |
|
1992 |
Fernández A. Computation of the fraction of RNA sequences that fold sequentially into a unique free-energy minimum. Physical Review A. 46. PMID 9908778 DOI: 10.1103/Physreva.46.R4524 |
0.337 |
|
1992 |
Fernández A. Folding pathway leading to the most stable conformation of a random RNA chain. Physical Review A. 45. PMID 9907019 DOI: 10.1103/Physreva.45.R8348 |
0.348 |
|
1992 |
Fernández A. A parallel computation revealing the role of the in vivo environment in shaping the catalytic structure of a mitochondrial RNA transcript. Journal of Theoretical Biology. 157: 487-503. PMID 1281246 DOI: 10.1016/S0022-5193(05)80665-4 |
0.34 |
|
1992 |
Fernández A. Modulation of the stability of a replication complex and its effect on the rate of chain elongation: extending the notion of processivity Chemical Physics Letters. 192: 294-298. DOI: 10.1016/0009-2614(92)85468-P |
0.326 |
|
1992 |
Fernández A. Structural organization of an RNA catalyst with the random energy model as a reference frame International Journal of Theoretical Physics. 31: 983-993. DOI: 10.1007/Bf00675089 |
0.313 |
|
1992 |
Fernández A. Relaxation timescales for conformational substates in disordered polymers Annalen Der Physik. 504: 61-65. DOI: 10.1002/Andp.19925040111 |
0.313 |
|
1991 |
Fernández A. Phenotypic traits and regulatory role of RNA folding in molecular selection. Zeitschrift FüR Naturforschung C. 46: 656-662. PMID 1776996 DOI: 10.1515/Znc-1991-7-824 |
0.326 |
|
1991 |
Fernández A. Early base-pair fluctuations and the activation of mRNA splicing Physica a-Statistical Mechanics and Its Applications. 173: 522-531. DOI: 10.1016/0378-4371(91)90377-O |
0.318 |
|
1991 |
Fernández A. Functional metastable structures in RNA replication Physica a-Statistical Mechanics and Its Applications. 176: 499-513. DOI: 10.1016/0378-4371(91)90227-4 |
0.326 |
|
1991 |
Fernández A. Excluded volume effects on the kinetic assembling of a structural motif for RNA catalysis Chemical Physics Letters. 183: 499-504. DOI: 10.1016/0009-2614(91)80165-T |
0.326 |
|
1990 |
Fernández A, Shakhnovich EI. Activation-energy landscape for metastable RNA folding. Physical Review A. 42: 3657-3659. PMID 9904458 DOI: 10.1103/Physreva.42.3657 |
0.352 |
|
1990 |
Fernández A. Kinetic assembling of the biologically active secondary structure for CAR, the target sequence for the Rev protein of HIV-1 Archives of Biochemistry and Biophysics. 280: 421-424. PMID 2195997 DOI: 10.1016/0003-9861(90)90352-Y |
0.349 |
|
1990 |
Fernández A. Spectrum of relaxation time scales for metastable RNA folding Physica a-Statistical Mechanics and Its Applications. 165: 352-360. DOI: 10.1016/0378-4371(90)90004-C |
0.311 |
|
1989 |
Fernández A. Metastable RNA folding and the enhancement of autocatalytic activity. Naturwissenschaften. 76: 525-526. PMID 2482446 DOI: 10.1007/Bf00374128 |
0.302 |
|
1989 |
Fernández A. The microscopic origin of cooperativity and its effect on long-lifetime kinetic modes for template-free RNA synthesis Journal of the Chemical Society, Faraday Transactions. 85: 1377-1390. DOI: 10.1039/F29898501377 |
0.317 |
|
1988 |
Fernández A. Stochastic dynamical constraints in de novo RNA replication Journal of Theoretical Biology. 134: 419-430. PMID 2474725 DOI: 10.1016/S0022-5193(88)80048-1 |
0.326 |
|
1988 |
Fernández A. Correlation of subsystems at the onset of a centre manifold organization Journal of the Chemical Society, Faraday Transactions. 84: 1741-1746. DOI: 10.1039/F29888401741 |
0.306 |
|
1985 |
Sinanoglu O, Fernández A. Solvophobic forces and molecular surface area changes in drug-biomolecule associations as with actinomycin-deoxyguanosine in a wide range of methanol/water mixtures. Biophysical Chemistry. 21: 167-71. PMID 17007769 DOI: 10.1016/0301-4622(85)80003-X |
0.631 |
|
1985 |
Fernández A, Sinanoglu O. Denaturation of proteins in methanol/water mixtures. Biophysical Chemistry. 21: 163-6. PMID 17007768 DOI: 10.1016/0301-4622(85)80002-8 |
0.642 |
|
1985 |
Sinanoglu O, Fernández A. The denaturation maxima of proteins and of drug-biomolecule complex formation in a wide range of methanol/water mixtures. Solvophobic theory predictions as compared to experiments. Biophysical Chemistry. 21: 157-62. PMID 17007767 DOI: 10.1016/0301-4622(85)80001-6 |
0.646 |
|
1985 |
Fernández A, Sinanoglu O. Subordination of the fast-relaxing degree of freedom in the center manifold of the Belousov-Zhabotinsky system. Physical Review. a, General Physics. 31: 2736-2737. PMID 9895820 DOI: 10.1103/Physreva.31.2736 |
0.617 |
|
1985 |
Fernández A, Sinanoglu O. A Reactive System with Diffusive Transport Displaying Two Different Symmetry-Breaking Dissipative Structures Zeitschrift Fur Naturforschung - Section a Journal of Physical Sciences. 40: 611-618. DOI: 10.1515/Zna-1985-0612 |
0.633 |
|
1984 |
Fernández A, Sinanoğlu O. Spatial-temporal dissipative structures arising in open reactive systems with a negative feedback loop. Bio Systems. 17: 3-9. PMID 6743791 DOI: 10.1016/0303-2647(84)90010-8 |
0.618 |
|
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