about
Evolutionary alteration of ALOX15 specificity optimizes the biosynthesis of antiinflammatory and proresolving lipoxinsUnderstanding how cAMP-dependent protein kinase can catalyze phosphoryl transfer in the presence of Ca2+ and Sr2+: a QM/MM study.A QM/MM study of Kemptide phosphorylation catalyzed by protein kinase A. The role of Asp166 as a general acid/base catalyst.Insights into the mechanism of binding of arachidonic acid to mammalian 15-lipoxygenases.Thermodynamics, kinetics, and dynamics of the two alternative aniomesolytic fragmentations of C-O bonds: an electrochemical and theoretical study.Testing electronic structure methods for describing intermolecular H...H interactions in supramolecular chemistry.Electronic structure study of the initiation routes of the dimethyl sulfide oxidation by OH.A fast radical chain mechanism in the polyfluoroalkoxylation of aromatics through NO2 group displacement. Mechanistic and theoretical studies.How the substrate D-glutamate drives the catalytic action of Bacillus subtilis glutamate racemase.Formation pathways of DMSO(2) in the addition channel of the OH-initiated DMS oxidation: A theoretical study.An insight into the regiospecificity of linoleic acid peroxidation catalyzed by mammalian 15-lipoxygenases.Formation pathways of DMSO from DMS-OH in the presence of O(2) and NO(x): A theoretical study.Influence of the enzyme phosphorylation state and the substrate on PKA enzyme dynamics.On the ionization state of the substrate in the active site of glutamate racemase. A QM/MM study about the importance of being zwitterionic.Variational transition-state theory study of the dimethyl sulfoxide (DMSO) and OH reaction.Inhibition of Mammalian 15-Lipoxygenase by Three Ebselen-like Drugs. A QM/MM and MM/PBSA Comparative Study.Mutagenesis of Sequence Determinants of Truncated Porcine ALOX15 Induces Changes in the Reaction Specificity by Altering the Catalytic Mechanism of Initial Hydrogen Abstraction.Is Regioselectivity in the Enzyme-Catalyzed Hydroperoxidation of Arachidonic Acid Necessarily Determined by Hydrogen Abstraction? The Case of Rabbit Leu597Ala/Ile663Ala ALOX15 Mutant.Computational insight into the catalytic implication of head/tail-first orientation of arachidonic acid in human 5-lipoxygenase: consequences for the positional specificity of oxygenation.A PM3/d specific reaction parameterization for iron atom in the hydrogen abstraction catalyzed by soybean lipoxygenase-1.Searching for Saddle Points by Using the Nudged Elastic Band Method: An Implementation for Gas-Phase Systems.Dependence of the rate constants on the treatment of internal rotation modes: the reaction OH + CH3SH --> CH3S + H2O as an example.Ligand-induced formation of transient dimers of mammalian 12/15-lipoxygenase: a key to allosteric behavior of this class of enzymes?A QM/MM study of the associative mechanism for the phosphorylation reaction catalyzed by protein kinase A and its D166A mutant.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.Theoretical Study of the Mechanism of the Hydride Transfer between Ferredoxin–NADP+ Reductase and NADP+: The Role of Tyr303Understanding the Mechanism of the Hydrogen Abstraction from Arachidonic Acid Catalyzed by the Human Enzyme 15-Lipoxygenase-2. A Quantum Mechanics/Molecular Mechanics Free Energy SimulationA Molecular Dynamics Simulation of the Binding Modes ofd-Glutamate andd-Glutamine to Glutamate RacemaseHow Can Linoleic Acid Be the Preferential Substrate of the Enzyme 15-Lipoxygenase-1? A QM/MM ApproachIntroducing Mutations to Modify the C13/C9 Ratio in Linoleic Acid Oxygenations Catalyzed by Rabbit 15-Lipoxygenase: A QM/MM and MD StudyRegio- and Stereospecificity in the Oxygenation of Arachidonic Acid Catalyzed by Leu597 Mutants of Rabbit 15-Lipoxygenase: A QM/MM StudyOn the Regio- and Stereospecificity of Arachidonic Acid Peroxidation Catalyzed by Mammalian 15-Lypoxygenases: A Combined Molecular Dynamics and QM/MM StudySubstrate binding to mammalian 15-lipoxygenaseEnzyme dynamics and tunneling enhanced by compression in the hydrogen abstraction catalyzed by soybean lipoxygenase-1A theoretical analysis of rate constants and kinetic isotope effects corresponding to different reactant valleys in lactate dehydrogenaseKinetic study on the reaction of OH radical with dimethyl sulfide in the absence of oxygenNew insights into the reaction mechanism catalyzed by the glutamate racemase enzyme: pH titration curves and classical molecular dynamics simulationsComparative study of the prereactive protein kinase A Michaelis complex with kemptide substrateReaction mechanism of the mandelate anion racemization catalyzed by mandelate racemase enzyme: a QM/MM molecular dynamics free energy studyCanonical variational transition-state theory study of the CF3CH2CH3 + OH reaction
P50
Q37142660-32A7DD4B-4547-468D-B381-7007BE8973D1Q38853392-AE476A78-F016-4BC0-A769-2804551DCB47Q41655364-9B61341F-2BC3-4997-87F6-8A19EFC1031AQ43080378-A61A2EA9-38BD-4623-8134-AA33DAF75BFEQ43969067-03B1E6D1-18F3-4A5B-8605-A98FB6CE47B4Q44667067-82B8914D-DA11-4208-93C0-7B69F7D0BC29Q45279322-5C87D5EE-66C0-457E-BF5D-57707FFC6D69Q45282071-EF36B1AC-04DD-4FFD-A055-EB10A17846C4Q46116955-32BD053D-4ACF-496E-AA21-6466167E2787Q46203566-47F3B453-875B-4A92-84FF-B51C3FA7C0CFQ46417182-9AFDC5FA-FE44-4A4B-9F91-2D3BF52820E5Q46529360-4CFA835D-5D05-40B3-A5A7-78B4C011FCDDQ46836609-02B94A88-4F0E-4993-A701-2CC973931980Q46888627-B43C15EC-9D75-42B8-9B9C-ACF5844DFB59Q46888639-B3B23574-A0A1-4487-96C1-1EB97345A29BQ47356260-CFBE1C6B-35F2-4881-AA29-01AA53C2202DQ47445739-29138E94-B9CE-47EC-9D06-ED98AAF4A377Q48294141-AD403A72-3F57-4117-B139-83BAC2741A19Q51595757-2BEA692F-FE12-40FA-8630-7F9B91BBD48BQ51923677-1F97A061-BE45-4A31-8B0B-DDC87E5DDAEAQ51938708-12D13A16-E81F-4291-ABCD-CAFA55AF5335Q52019483-0C3572DA-50A2-49E2-8C11-C69B7D09E176Q52890990-6A47908C-307C-4C76-A7B3-F97D9D350717Q54329542-F8C323C0-8799-4EA1-A09C-F58C0B81A390Q54635173-AF049F3B-E181-45A9-AB55-E28565E67FA2Q57874563-7D03B4F0-9E19-4458-879B-4003EE414B72Q58096431-A8013878-3201-487F-AFC0-8971EA338CE4Q58616189-965683CC-7831-4E0A-86EE-DD08D219FB73Q60860079-896F3F92-BE1C-4380-90BB-D050FF912BAEQ60860084-DE428B2A-4AF7-4CB3-8C40-140D305CF1A6Q60860085-AB1744E3-E802-42FC-979E-0C0081A36BD2Q60860087-8BD05B10-FFC5-48FB-9809-C6C37E8FCD7DQ60860104-6C176791-9E1B-4B2D-A23B-B7720AB2E0A7Q79392653-6C9C5489-D226-44A4-9820-2BA1C8B428A9Q79440419-2B7B26D0-2CBB-4AE2-AC7F-961FB55482A0Q79446050-BC4FBA75-7AD7-4123-8A8C-1CB8813043A6Q79740011-E0276D7C-7FD4-4E1F-B575-1CD93335F9A2Q79846741-F70D2911-6DC3-4E31-B636-B61343554F2BQ79944852-50AB5B43-BDBD-43B8-82CE-24B7E159F31DQ80202452-108C1697-E8F7-47E9-86DD-EF59FB614F33
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Àngels González-Lafont
@ast
Àngels González-Lafont
@en
Àngels González-Lafont
@es
Àngels González-Lafont
@nl
Àngels González-Lafont
@sl
type
label
Àngels González-Lafont
@ast
Àngels González-Lafont
@en
Àngels González-Lafont
@es
Àngels González-Lafont
@nl
Àngels González-Lafont
@sl
prefLabel
Àngels González-Lafont
@ast
Àngels González-Lafont
@en
Àngels González-Lafont
@es
Àngels González-Lafont
@nl
Àngels González-Lafont
@sl
P214
P106
P1580
P214
P2456
P31
P496
0000-0003-0729-2483
P7859
viaf-305875883