{"id":121,"date":"2023-02-28T22:34:25","date_gmt":"2023-02-28T20:34:25","guid":{"rendered":"https:\/\/webs.uab.cat\/dmrqb\/?page_id=121"},"modified":"2026-10-09T23:20:18","modified_gmt":"2026-10-09T21:20:18","slug":"mireia-garcia-viloca","status":"publish","type":"page","link":"https:\/\/webs.uab.cat\/molbiomed\/mireia-garcia-viloca\/","title":{"rendered":"Mireia Garcia Viloca"},"content":{"rendered":"\n
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Titular d’universitat<\/p>\n\n\n\n

\"ORCID\"<\/a>    \"ResearchGate\"<\/a><\/p>\n<\/div>\n\n\n\n

Mireia Garcia Viloca<\/strong> va n\u00e9ixer a Barcelona el 1972. Llicenciada en Ci\u00e8ncies Qu\u00edmiques i Doctora en Ci\u00e8ncies Qu\u00edmiques per la Universitat Aut\u00f2noma de Barcelona (UAB) el 1995 i el 2000, respectivament. Des de l’any 2001 fins a l’any 2003 va poder treballar com a investigadora postdoctoral amb una beca de la Fundaci\u00f3 Fulbright a la Universitat de Minnesota sota la direcci\u00f3 del Dr. Jiali Gao. L’any 2003 va poder incorporar-se a l’Institut de Biotecnologia I Biomedicina (IBB, UAB) com a Investigadora Ram\u00f3n y Cajal fins al 2007 quan va ser contractada com a professora Agregada al Departament de Qu\u00edmica. Aquell mateix any l’ANEP va concedir-li el premi a traject\u00f2ria cient\u00edfica destacada. Finalment, l’any 2010 aconsegu\u00ed la pla\u00e7a de professora titular a la UAB. Al llarg dels seus anys com a investigadora ha dirigit 5 tesis doctorals i ha publicat 55 treballs cient\u00edfics en revistes internacionals.<\/p>\n\n\n\n

La seva recerca va ser l’inici de la Qu\u00edmica Te\u00f2rica aplicada a sistemes biol\u00f2gics al grup d’investigaci\u00f3. Va ser la primera a descriure un model QM\/MM per una reacci\u00f3 enzim\u00e0tica a la UAB. En incorporar-se a l’IBB va comen\u00e7ar a estudiar reaccions enzim\u00e0tiques complexes reguladores del metabolisme cel\u00b7lular. L’estudi va centrar-se en l’estudi de prote\u00efnes quinases amb rellev\u00e0ncia significativa en moltes malalties com la diabetis i el c\u00e0ncer. Actualment, treballa a una de les l\u00ednies principals del grup de recerca, estudiant el mecanisme d’activaci\u00f3 dels processos de resoluci\u00f3 inflamat\u00f2ria activats pel receptor LGR6.<\/p>\n<\/div>\n<\/div>\n<\/div><\/div>\n\n\n\n

\u00daltimes publicacions<\/h2>\n\n\n\n
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Protein Science 2026, 35, e70625<\/p>\n<\/div>\n\n\n\n

Omega\u20103 DHA as a blank canvas: A molecular approximation to how lipid mediators modulate LGR6 in inflammation resolution<\/h3>\n\n\n\n
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Llegeix l’article \u2192<\/a><\/div>\n<\/div>\n<\/div>\n\n\n\n
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ACS Omega 2022, 7, 25186-25199<\/p>\n<\/div>\n\n\n\n

Molecular Insights into the Regulation of 3-Phosphoinositide-Dependent Protein Kinase 1: Modeling the Interaction between the Kinase and the Pleckstrin Homology Domains<\/h3>\n\n\n\n
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Llegeix l’article \u2192<\/a><\/div>\n<\/div>\n<\/div>\n\n\n\n
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Phys. Chem. Chem. Phys. 2017, 19, 10377-10394<\/p>\n<\/div>\n\n\n\n

Understanding how cAMP-dependent protein kinase can catalyze phosphoryl transfer in the presence of Ca2+ and Sr2+: a QM\/MM study<\/h3>\n\n\n\n
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Llegeix l’article \u2192<\/a><\/div>\n<\/div>\n<\/div>\n<\/div>\n\n\n\n

Totes les publicacions 59 articles<\/span><\/h2>\n\n\n\n

Veure totes les publicacions del grup \u2192<\/a><\/p>\n\n\n\n

2026<\/h3>\n\n\n\n

Omega\u20103 DHA as a blank canvas: A molecular approximation to how lipid mediators modulate LGR6 in inflammation resolution<\/a> \u2014 Protein Science 2026, 35, e70625<\/em><\/p>\n\n\n\n

2022<\/h3>\n\n\n\n

Molecular Insights into the Regulation of 3-Phosphoinositide-Dependent Protein Kinase 1: Modeling the Interaction between the Kinase and the Pleckstrin Homology Domains<\/a> \u2014 ACS Omega 2022, 7, 25186-25199<\/em><\/p>\n\n\n\n

2017<\/h3>\n\n\n\n

Understanding how cAMP-dependent protein kinase can catalyze phosphoryl transfer in the presence of Ca2+ and Sr2+: a QM\/MM study<\/a> \u2014 Phys. Chem. Chem. Phys. 2017, 19, 10377-10394<\/em><\/p>\n\n\n\n

2015<\/h3>\n\n\n\n

A QM\/MM study of Kemptide phosphorylation catalyzed by protein kinase A. The role of Asp166 as a general acid\/base catalyst<\/a> \u2014 Phys. Chem. Chem. Phys. 2015, 17, 3497-3511<\/em><\/p>\n\n\n\n

SP20 Phosphorylation Reaction Catalyzed by Protein Kinase A: QM\/MM Calculations Based on Recently Determined Crystallographic Structures<\/a> \u2014 ACS Catal. 2015, 5, 4897-4912<\/em><\/p>\n\n\n\n

2014<\/h3>\n\n\n\n

A QM\/MM study of the associative mechanism for the phosphorylation reaction catalyzed by protein kinase A and its D166A mutant<\/a> \u2014 J Comput Aided Mol Des 2014, 28, 1077-1091<\/em><\/p>\n\n\n\n

Com ajuden els \u00e0toms a aprendre qu\u00edmica i quines dificultats generen? \u2014 Educaci\u00f3 Qu\u00edmica 2014<\/em><\/p>\n\n\n\n

2012<\/h3>\n\n\n\n

Influence of the enzyme phosphorylation state and the substrate on PKA enzyme dynamics<\/a> \u2014 Biophysical Chemistry 2012, 161, 17-28<\/em><\/p>\n\n\n\n

Theoretical Analysis of the Catalytic Mechanism of Helicobacter pylori Glutamate Racemase<\/a> \u2014 J. Phys. Chem. B 2012, 116, 12406-12414<\/em><\/p>\n\n\n\n

Theoretical Study of the Mechanism of the Hydride Transfer between Ferredoxin-NADP(+) Reductase and NADP(+): The Role of Tyr303<\/a> \u2014 J. Am. Chem. Soc. 2012, 134, 20544-20553<\/em><\/p>\n\n\n\n

2011<\/h3>\n\n\n\n

Temperature dependence of the kinetic isotope effects in thymidylate synthase. a theoretical study<\/a> \u2014 J. Am. Chem. Soc. 2011, 133, 6692-6702<\/em><\/p>\n\n\n\n

A QM\/MM study of the phosphoryl transfer to the Kemptide substrate catalyzed by protein kinase A. The effect of the phosphorylation state of the protein on the mechanism<\/a> \u2014 Phys. Chem. Chem. Phys. 2011, 13, 530-539<\/em><\/p>\n\n\n\n

2010<\/h3>\n\n\n\n

The Mechanism of the Hydride Transfer between Anabaena Tyr303Ser FNRrd\/FNRox and NADP+\/H. A Combined Pre-Steady-State Kinetic\/Ensemble-Averaged Transition State Theory with Multidimensional Tunneling Study \u2014 Journal of Physical Chemistry B 2010<\/em><\/p>\n\n\n\n

Mechanism of the Hydride Transfer between Anabaena Tyr303Ser FNRrd\/FNRox and NADP(+)\/H. A Combined Pre-Steady-State Kinetic\/Ensemble-Averaged Transition-State Theory with Multidimensional Tunneling Study<\/a> \u2014 J. Phys. Chem. B 2010, 114, 3368-3379<\/em><\/p>\n\n\n\n

2009<\/h3>\n\n\n\n

Critical role of substrate conformational change in the proton transfer process catalyzed by 4-oxalocrotonate tautomerase<\/a> \u2014 J. Am. Chem. Soc. 2009, 131, 2687-2698<\/em><\/p>\n\n\n\n

Benchmark calculations on models of the phosphoryl transfer reaction catalyzed by protein kinase A<\/a> \u2014 Theor Chem Acc 2009, 124, 197-215<\/em><\/p>\n\n\n\n

How the Substrate D-Glutamate Drives the Catalytic Action of Bacillus subtilis Glutamate Racemase<\/a> \u2014 J. Am. Chem. Soc. 2009, 131, 3509-3521<\/em><\/p>\n\n\n\n

2007<\/h3>\n\n\n\n

Comparative study of the prereactive protein kinase A Michaelis complex with Kemptide substrate<\/a> \u2014 J Comput Aided Mol Des 2007, 21, 603-615<\/em><\/p>\n\n\n\n

New insights into the reaction mechanism catalyzed by the glutamate racemase enzyme: PH titration curves and classical molecular dynamics simulations<\/a> \u2014 J. Phys. Chem. B 2007, 111, 2385-2397<\/em><\/p>\n\n\n\n

PHYS 303-Using statistical mechanics with quantum mechanics for enzymes and nanoparticles \u2014 Abstracts of Papers of the American Chemical Society 2007<\/em><\/p>\n\n\n\n

2006<\/h3>\n\n\n\n

Path integral simulations of proton transfer reactions in aqueous solution using combined QM\/MM potentials<\/a> \u2014 J. Chem. Theory Comput. 2006, 2, 236-245<\/em><\/p>\n\n\n\n

A theoretical analysis of rate constants and kinetic isotope effects corresponding to different reactant valleys in lactate dehydrogenase<\/a> \u2014 J. Am. Chem. Soc. 2006, 128, 16851-16863<\/em><\/p>\n\n\n\n

Enzyme dynamics and tunneling enhanced by compression in the hydrogen abstraction catalyzed by soybean lipoxygenase-1<\/a> \u2014 J. Phys. Chem. B 2006, 110, 24708-24719<\/em><\/p>\n\n\n\n

On the ionization state of the substrate in the active site of glutamate racemase. A QM\/MM study about the importance of being zwitterionic<\/a> \u2014 J. Phys. Chem. A 2006, 110, 717-725<\/em><\/p>\n\n\n\n

2005<\/h3>\n\n\n\n

Nonperfect synchronization of reaction center rehybridization in the transition state of the hydride transfer catalyzed by dihydrofolate reductase<\/a> \u2014 J. Am. Chem. Soc. 2005, 127, 14879-14886<\/em><\/p>\n\n\n\n

A QM\/MM exploration of the potential energy surface of pyruvate to lactate transformation catalyzed by LDH. Improving the accuracy of semiempirical descriptions<\/a> \u2014 J. Chem. Theory Comput. 2005, 1, 750-761<\/em><\/p>\n\n\n\n

A molecular dynamics simulation of the binding modes of D-glutamate and D-Glutamine to glutamate racemase<\/a> \u2014 J. Chem. Theory Comput. 2005, 1, 737-749<\/em><\/p>\n\n\n\n

2004<\/h3>\n\n\n\n

Solvent and protein effects on the vibrational frequency shift and energy relaxation of the azide ligand in carbonic anhydrase<\/a> \u2014 J. Phys. Chem. B 2004, 108, 13501-13512<\/em><\/p>\n\n\n\n

Dynamics of an Enzymatic Substitution Reaction in Haloalkane Dehalogenase<\/a> \u2014 J. Am. Chem. Soc. 2004, 126, 1369-1376<\/em><\/p>\n\n\n\n

Ensemble-averaged variational transition state theory with optimized multidimensional tunneling for enzyme kinetics and other condensed-phase reactions<\/a> \u2014 Int J of Quantum Chemistry 2004, 100, 1136-1152<\/em><\/p>\n\n\n\n

Generalized Hybrid Orbital for the Treatment of Boundary Atoms in Combined QM\/MM Calculations Using the PM3 Model. \u2014 Theoretical Chemistry Accounts 2004<\/em><\/p>\n\n\n\n

How enzymes work: Analysis by modern rate theory and computer simulations.<\/a> \u2014 Science 2004, 303, 186-195<\/em><\/p>\n\n\n\n

Sensitivity of molecular dynamics simulations to the choice of the X-ray structure used to model an enzymatic reaction<\/a> \u2014 Protein Science 2004, 13, 2341-2354<\/em><\/p>\n\n\n\n

Generalized hybrid orbital for the treatment of boundary atoms in combined quantum mechanical and molecular mechanical calculations using the semiempirical parameterized model 3 method<\/a> \u2014 Theor Chem Acc 2004, 111, 280-286<\/em><\/p>\n\n\n\n

2003<\/h3>\n\n\n\n

Chemical kinetics of systems with complex reaction paths: Ensemble-averaged variational transition state theory with multidimensional tunneling \u2014 Abstracts of Papers of the American Chemical Society 2003<\/em><\/p>\n\n\n\n

Free energy surface, reaction paths, and kinetic isotope effect of short-chain Acyl-CoA dehydrogenase<\/a> \u2014 J. Phys. Chem. B 2003, 107, 9567-9578<\/em><\/p>\n\n\n\n

Hydride transfer catalyzed by xylose isomerase: Mechanism and quantum effects<\/a> \u2014 J Comput Chem 2003, 24, 177-190<\/em><\/p>\n\n\n\n

Importance of substrate and cofactor polarization in the active site of dihydrofolate reductase<\/a> \u2014 Journal of Molecular Biology 2003, 327, 549-560<\/em><\/p>\n\n\n\n

Reaction-path energetics and kinetics of the hydride transfer reaction catalyzed by dihydrofolate reductase<\/a> \u2014 Biochemistry 2003, 42, 13558-13575<\/em><\/p>\n\n\n\n

Semiempirical QM\/MM potential with simple valence bond (SVB) for enzyme reactions. Application to the nucleophilic addition reaction in haloalkane dehalogenase<\/a> \u2014 Theoretical Chemistry Accounts: Theory, Computation, and Modeling (Theoretica Chimica Acta) 2003, 109, 133-139<\/em><\/p>\n\n\n\n

2002<\/h3>\n\n\n\n

Quantum Dynamics of Hydride Transfer Catalyzed by Bimetallic Electrophilic Catalysis: Synchronous Motion of Mg2+ and H- in Xylose Isomerase<\/a> \u2014 J. Am. Chem. Soc. 2002, 124, 7268-7269<\/em><\/p>\n\n\n\n

The Incorporation of Quantum Effects in Enzyme Kinetics Modeling<\/a> \u2014 Acc. Chem. Res. 2002, 35, 341-349<\/em><\/p>\n\n\n\n

On the modulation of the substrate activity for the racemization catalyzed by mandelate racemase enzyme. A QM\/MM study<\/a> \u2014 Phys. Chem. Chem. Phys. 2002, 4, 5365-5371<\/em><\/p>\n\n\n\n

The search for stationary points on a quantum mechanical\/molecular mechanical potential-energy surface<\/a> \u2014 Theoretical Chemistry Accounts: Theory, Computation, and Modeling (Theoretica Chimica Acta) 2002, 107, 147-153<\/em><\/p>\n\n\n\n

Calculation of solvation energies and enzyme dynamics for carbohydrates \u2014 Abstracts of Papers American Chemical Society 2002<\/em><\/p>\n\n\n\n

Dynamics, pathways, and tunneling in enzymatic reactions: A modern perspective of enzyme action \u2014 Abstracts of Papers American Chemical Society 2002<\/em><\/p>\n\n\n\n

Ensemble-averaged variational transition state theory with multidimensional tunneling \u2014 Abstracts of Papers American Chemical Society 2002<\/em><\/p>\n\n\n\n

2001<\/h3>\n\n\n\n

Canonical Variational Theory for Enzyme Kinetics with the Protein Mean Force and Multidimensional Quantum Mechanical Tunneling Dynamics. Theory and Application to liver Alcohol Dehydrogenase<\/a> \u2014 J. Phys. Chem. B 2001, 105, 11326-11340<\/em><\/p>\n\n\n\n

Inclusion of quantum-mechanical vibrational energy in reactive potentials of mean force<\/a> \u2014 The Journal of Chemical Physics 2001, 114, 9953-9958<\/em><\/p>\n\n\n\n

The 1H NMR chemical shift for the hydroxy proton of 4-(dimethylamino)-2′-hydroxychalcone in chloroform: A theoretical approach to its inverse dependence on the temperature \u2014 Org. Lett. 2001<\/em><\/p>\n\n\n\n

A QM\/MM study of the racemization of vinylglycolate catalyzed by mandelate racemase enzyme<\/a> \u2014 J. Am. Chem. Soc. 2001, 123, 709-721<\/em><\/p>\n\n\n\n

The H-1 NMR chemical shift for the hydroxy proton of 4-(dimethylamino)-2 ‘-hydroxychalcone in chloroform: A theoretical approach to its inverse dependence on the temperature<\/a> \u2014 Org. Lett. 2001, 3, 589-592<\/em><\/p>\n\n\n\n

Quantum dynamics study of hydride transfer reaction in xylose isomerase \u2014 Abstracts of Papers American Chemical Society 2001<\/em><\/p>\n\n\n\n

1999<\/h3>\n\n\n\n

Molecular Dynamics Simulations Can Reproduce the Subtle Differences in NADP and NHDP Binding to Isocitrate Dehydrogenase<\/a> \u2014 Int. J. Quant. Chem. 1999, 75, 231-243<\/em><\/p>\n\n\n\n

Asymmetry of the hydrogen bond of hydrogen phthalate anion in solution. A QM\/MM study<\/a> \u2014 J. Am. Chem. Soc. 1999, 121, 9198-9207<\/em><\/p>\n\n\n\n

1998<\/h3>\n\n\n\n

Temperature dependence of proton NMR chemical shift as a criterion to identify low-barrier hydrogen bonds<\/a> \u2014 J. Am. Chem. Soc. 1998, 120, 10203-10209<\/em><\/p>\n\n\n\n

1997<\/h3>\n\n\n\n

Is an extremely low-field proton signal in the NMR spectrum conclusive evidence for a low-barrier hydrogen bond?<\/a> \u2014 J. Phys. Chem. A 1997, 101, 8727-8733<\/em><\/p>\n\n\n\n

On pK(a) matching as a requirement to form a low-barrier hydrogen bond. A theoretical study in gas phase<\/a> \u2014 J. Phys. Chem. A 1997, 101, 3880-3886<\/em><\/p>\n\n\n\n

Theoretical study of the low-barrier hydrogen bond in the hydrogen maleate anion in the gas phase. Comparison with normal hydrogen bonds<\/a> \u2014 J. Am. Chem. Soc. 1997, 119, 1081-1086<\/em><\/p>\n","protected":false},"excerpt":{"rendered":"

Titular d’universitat      Mireia Garcia Viloca va n\u00e9ixer a Barcelona el 1972. Llicenciada en Ci\u00e8ncies Qu\u00edmiques i Doctora en Ci\u00e8ncies Qu\u00edmiques per la Universitat Aut\u00f2noma de Barcelona (UAB) el 1995 i el 2000, respectivament. Des de l’any 2001 fins a l’any 2003 va poder treballar com a investigadora postdoctoral amb una beca de la Fundaci\u00f3 Fulbright […]<\/p>\n","protected":false},"author":2580,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-121","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/webs.uab.cat\/molbiomed\/wp-json\/wp\/v2\/pages\/121","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/webs.uab.cat\/molbiomed\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/webs.uab.cat\/molbiomed\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/webs.uab.cat\/molbiomed\/wp-json\/wp\/v2\/users\/2580"}],"replies":[{"embeddable":true,"href":"https:\/\/webs.uab.cat\/molbiomed\/wp-json\/wp\/v2\/comments?post=121"}],"version-history":[{"count":17,"href":"https:\/\/webs.uab.cat\/molbiomed\/wp-json\/wp\/v2\/pages\/121\/revisions"}],"predecessor-version":[{"id":3448,"href":"https:\/\/webs.uab.cat\/molbiomed\/wp-json\/wp\/v2\/pages\/121\/revisions\/3448"}],"wp:attachment":[{"href":"https:\/\/webs.uab.cat\/molbiomed\/wp-json\/wp\/v2\/media?parent=121"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}