Golicnik M

General

Full name : Golicnik Marko

First name : Marko

Mail : Institute of Biochemistry, Medical Faculty, University of Ljubljana, Vrazov trg 2, 1000 Ljubljana

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Country : Slovenia

Email : marko.golicnik@mf.uni-lj.si

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References (35)

Title : Enzyme Databases in the Era of Omics and Artificial Intelligence - Presern_2023_Int.J.Mol.Sci_24_
Author(s) : Presern U , Golicnik M
Ref : Int J Mol Sci , 24 : , 2023
Abstract :
PubMedSearch : Presern_2023_Int.J.Mol.Sci_24_
PubMedID: 38069254

Title : Substrate-dependent inactivation of recombinant paraoxonase 1 during catalytic dihydrocoumarin turnover and the protective properties of surfactants - Smerkolj_2023_Chem.Biol.Interact_14ChEPon_382_110563
Author(s) : Smerkolj J , Stojan J , Bavec A , Golicnik M
Ref : Chemico-Biological Interactions , 382 :110563 , 2023
Abstract :
PubMedSearch : Smerkolj_2023_Chem.Biol.Interact_14ChEPon_382_110563
PubMedID: 37286155

Title : iFIT: An automated web tool for determining enzyme-kinetic parameters based on the high-curvature region of progress curves - Petric_2022_Acta.Chim.Slov_69_478
Author(s) : Petric B , Golicnik M , Bavec A
Ref : Acta Chim Slov , 69 :478 , 2022
Abstract :
PubMedSearch : Petric_2022_Acta.Chim.Slov_69_478
PubMedID: 35861063

Title : The Removal of Time-Concentration Data Points from Progress Curves Improves the Determination of K(m): The Example of Paraoxonase 1 - Petric_2022_Molecules_27_
Author(s) : Petric B , Golicnik M , Bavec A
Ref : Molecules , 27 : , 2022
Abstract :
PubMedSearch : Petric_2022_Molecules_27_
PubMedID: 35209091

Title : The Structure and Function of Paraoxonase-1 and Its Comparison to Paraoxonase-2 and -3 - Taler-Vercic_2020_Molecules_25_
Author(s) : Taler-Vercic A , Golicnik M , Bavec A
Ref : Molecules , 25 : , 2020
Abstract :
PubMedSearch : Taler-Vercic_2020_Molecules_25_
PubMedID: 33348669

Title : Evaluation of the paraoxonase-1 kinetic parameters of the lactonase activity by nonlinear fit of progress curves - Golicnik_2020_J.Enzyme.Inhib.Med.Chem_35_261
Author(s) : Golicnik M , Bavec A
Ref : J Enzyme Inhib Med Chem , 35 :261 , 2020
Abstract :
PubMedSearch : Golicnik_2020_J.Enzyme.Inhib.Med.Chem_35_261
PubMedID: 31790606

Title : Interactions of Paraoxonase-1 with Pharmacologically Relevant Carbamates - Bosak_2020_Molecules_25_
Author(s) : Bosak A , Bavec A , Konte T , Sinko G , Kovarik Z , Golicnik M
Ref : Molecules , 25 : , 2020
Abstract :
PubMedSearch : Bosak_2020_Molecules_25_
PubMedID: 31947900

Title : Time-course of human cholinesterases-catalyzed competing substrate kinetics - Mukhametgalieva_2019_Chem.Biol.Interact_310_108702
Author(s) : Mukhametgalieva AR , Aglyamova AR , Lushchekina SV , Golicnik M , Masson P
Ref : Chemico-Biological Interactions , 310 :108702 , 2019
Abstract :
PubMedSearch : Mukhametgalieva_2019_Chem.Biol.Interact_310_108702
PubMedID: 31247192

Title : Transition-State Interactions in a Promiscuous Enzyme: Sulfate and Phosphate Monoester Hydrolysis by Pseudomonas aeruginosa Arylsulfatase - van Loo_2019_Biochemistry_58_1363
Author(s) : van Loo B , Berry R , Boonyuen U , Mohamed MF , Golicnik M , Hengge AC , Hollfelder F
Ref : Biochemistry , 58 :1363 , 2019
Abstract :
PubMedSearch : van Loo_2019_Biochemistry_58_1363
PubMedID: 30810299

Title : Progress-Curve Analysis Through Integrated Rate Equations and Its Use to Study Cholinesterase Reaction Dynamics - Golicnik_2014_J.Mol.Neurosci_53_330
Author(s) : Golicnik M
Ref : Journal of Molecular Neuroscience , 53 :330 , 2014
Abstract :
PubMedSearch : Golicnik_2014_J.Mol.Neurosci_53_330
PubMedID: 24078521

Title : Exploring the aryl esterase catalysis of paraoxonase-1 through solvent kinetic isotope effects and phosphonate-based isosteric analogues of the tetrahedral reaction intermediate - Bavec_2014_Biochimie_106_184
Author(s) : Bavec A , Knez D , Makovec T , Stojan J , Gobec S , Golicnik M
Ref : Biochimie , 106 :184 , 2014
Abstract :
PubMedSearch : Bavec_2014_Biochimie_106_184
PubMedID: 25180809

Title : The integrated Michaelis-Menten rate equation: deja vu or vu jade? - Golicnik_2013_J.Enzyme.Inhib.Med.Chem_28_879
Author(s) : Golicnik M
Ref : J Enzyme Inhib Med Chem , 28 :879 , 2013
Abstract :
PubMedSearch : Golicnik_2013_J.Enzyme.Inhib.Med.Chem_28_879
PubMedID: 22630075

Title : Estimation of kinetic parameters for enzyme-inhibition reaction models using direct time-dependent equations for reactant concentrations - Golicnik_2012_Acta.Chim.Slov_59_207
Author(s) : Golicnik M
Ref : Acta Chim Slov , 59 :207 , 2012
Abstract :
PubMedSearch : Golicnik_2012_Acta.Chim.Slov_59_207
PubMedID: 24061194

Title : Detection of phosphorylation states by intermolecular sensitization of lanthanide-peptide conjugates - Pazos_2012_Chem.Commun.(Camb)_48_9534
Author(s) : Pazos E , Golicnik M , Mascarenas JL , Vazquez ME
Ref : Chem Commun (Camb) , 48 :9534 , 2012
Abstract :
PubMedSearch : Pazos_2012_Chem.Commun.(Camb)_48_9534
PubMedID: 22899319

Title : An alternative explicit model expression equivalent to the integrated michaelis-menten equation and its application to nonlinear saturation pharmacokinetics - Golicnik_2011_Ther.Drug.Monit_33_362
Author(s) : Golicnik M
Ref : Ther Drug Monit , 33 :362 , 2011
Abstract :
PubMedSearch : Golicnik_2011_Ther.Drug.Monit_33_362
PubMedID: 21516057

Title : Exact and approximate solutions for the decades-old Michaelis-Menten equation: Progress-curve analysis through integrated rate equations - Golicnik_2011_Biochem.Mol.Biol.Educ_39_117
Author(s) : Golicnik M
Ref : Biochem Mol Biol Educ , 39 :117 , 2011
Abstract :
PubMedSearch : Golicnik_2011_Biochem.Mol.Biol.Educ_39_117
PubMedID: 21445903

Title : Explicit analytic approximations for time-dependent solutions of the generalized integrated Michaelis-Menten equation - Golicnik_2011_Anal.Biochem_411_303
Author(s) : Golicnik M
Ref : Analytical Biochemistry , 411 :303 , 2011
Abstract :
PubMedSearch : Golicnik_2011_Anal.Biochem_411_303
PubMedID: 21241654

Title : Explicit reformulations of the Lambert W-omega function for calculations of the solutions to one-compartment pharmacokinetic models with Michaelis-Menten elimination kinetics - Golicnik_2011_Eur.J.Drug.Metab.Pharmacokinet_36_121
Author(s) : Golicnik M
Ref : Eur J Drug Metab Pharmacokinet , 36 :121 , 2011
Abstract :
PubMedSearch : Golicnik_2011_Eur.J.Drug.Metab.Pharmacokinet_36_121
PubMedID: 21533844

Title : Explicit reformulations of time-dependent solution for a Michaelis-Menten enzyme reaction model - Golicnik_2010_Anal.Biochem_406_94
Author(s) : Golicnik M
Ref : Analytical Biochemistry , 406 :94 , 2010
Abstract :
PubMedSearch : Golicnik_2010_Anal.Biochem_406_94
PubMedID: 20599638

Title : Effects of acetylcholinesterase gene silencing on its activity in cultured human skeletal muscle - Mis_2006_J.Mol.Neurosci_30_31
Author(s) : Mis K , Mars T , Golicnik M , Jevsek M , Grubic Z
Ref : Journal of Molecular Neuroscience , 30 :31 , 2006
Abstract :
PubMedSearch : Mis_2006_J.Mol.Neurosci_30_31
PubMedID: 17192616

Title : Expression and distribution of acetylcholinesterase among the cellular components of the neuromuscular junction formed in human myotube in vitro - Mis_2005_Chem.Biol.Interact_157-158_29
Author(s) : Mis K , Mars T , Jevsek M , Strasek H , Golicnik M , Brecelj J , Komel R , King MP , Miranda AF , Grubic Z
Ref : Chemico-Biological Interactions , 157-158 :29 , 2005
Abstract :
PubMedSearch : Mis_2005_Chem.Biol.Interact_157-158_29
PubMedID: 16256091

Title : Rational polynomial equation as an unbiased approach for the kinetic studies of Drosophila melanogaster acetylcholinesterase reaction mechanism - Stojan_2004_Biochim.Biophys.Acta_1703_53
Author(s) : Stojan J , Golicnik M , Fournier D
Ref : Biochimica & Biophysica Acta , 1703 :53 , 2004
Abstract :
PubMedSearch : Stojan_2004_Biochim.Biophys.Acta_1703_53
PubMedID: 15588702

Title : Comparison of two reaction schemes for the hydrolysis of acetylthiocholine by butyrylcholinesterase. -
Author(s) : Simeon-Rudolf V , Sinko G , Stuglin A , Stojan J , Golicnik M
Ref : Cholinergic Mechanisms, CRC Press :701 , 2004
PubMedID:

Title : Kinetics of ethopropazine binding to butyrylcholinesterase in the absence and presence of acetylthiocholine -
Author(s) : Reiner E , Sinko G , Bosak A , Simeon-Rudolf V , Radic Z , Taylor P , Stojan J , Golicnik M
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :187 , 2004
PubMedID:

Title : Poster (19) Kinetics of ethopropazine binding to butyrylcholinesterase in the absence and presence of acetylthiocholine. -
Author(s) : Reiner E , Sinko G , Stuglin A , Simeon-Rudolf V , Radic Z , Taylor P , Stojan J , Golicnik M
Ref : In: Cholinesterases in the Second Millennium: Biomolecular and Pathological Aspects , (Inestrosa NC, Campos EO) P. Universidad Catolica de Chile-FONDAP Biomedicina :330 , 2004
PubMedID:

Title : Significance of parameters in various kinetic schemes for cholinesterases. -
Author(s) : Stojan J , Golicnik M
Ref : Cholinergic Mechanisms, CRC Press :721 , 2004
PubMedID:

Title : Generalized theoretical and practical treatment of the kinetics of an enzyme-catalyzed reaction in the presence of an enzyme equimolar irreversible inhibitor - Golicnik_2003_J.Chem.Inf.Comput.Sci_43_1486
Author(s) : Golicnik M , Stojan J
Ref : J Chem Inf Comput Sci , 43 :1486 , 2003
Abstract :
PubMedSearch : Golicnik_2003_J.Chem.Inf.Comput.Sci_43_1486
PubMedID: 14502482

Title : Kinetic Model of Ethopropazine Interaction with Horse Serum Butyrylcholinesterase and Its Docking into the Active Site - Golicnik_2002_Arch.Biochem.Biophys_398_23
Author(s) : Golicnik M , Sinko G , Simeon-Rudolf V , Grubic Z , Stojan J
Ref : Archives of Biochemistry & Biophysics , 398 :23 , 2002
Abstract :
PubMedSearch : Golicnik_2002_Arch.Biochem.Biophys_398_23
PubMedID: 11811945

Title : Transient kinetic approach to the study of acetylcholinesterase reversible inhibition by eseroline - Golicnik_2002_J.Enzyme.Inhib.Med.Chem_17_279
Author(s) : Golicnik M , Stojan J
Ref : J Enzyme Inhib Med Chem , 17 :279 , 2002
Abstract :
PubMedSearch : Golicnik_2002_J.Enzyme.Inhib.Med.Chem_17_279
PubMedID: 12683744

Title : Acceleration of Drosophila melanogaster acetylcholinesterase methanesulfonylation: peripheral ligand D-tubocurarine enhances the affinity for small methanesulfonylfluoride - Golicnik_2002_Chem.Biol.Interact_139_145
Author(s) : Golicnik M , Fournier D , Stojan J
Ref : Chemico-Biological Interactions , 139 :145 , 2002
Abstract :
PubMedSearch : Golicnik_2002_Chem.Biol.Interact_139_145
PubMedID: 11823003

Title : On a nonelementary progress curve equation and its application in enzyme kinetics - Golicnik_2002_J.Chem.Inf.Comput.Sci_42_157
Author(s) : Golicnik M
Ref : J Chem Inf Comput Sci , 42 :157 , 2002
Abstract :
PubMedSearch : Golicnik_2002_J.Chem.Inf.Comput.Sci_42_157
PubMedID: 11911683

Title : Multi-step analysis as a tool for kinetic parameter estimation and mechanism discrimination in the reaction between tight-binding fasciculin 2 and electric eel acetylcholinesterase - Golicnik_2002_Biochim.Biophys.Acta_1597_164
Author(s) : Golicnik M , Stojan J
Ref : Biochimica & Biophysica Acta , 1597 :164 , 2002
Abstract :
PubMedSearch : Golicnik_2002_Biochim.Biophys.Acta_1597_164
PubMedID: 12009416

Title : Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion - Stojan_2002_Eur.J.Biochem_269_1154
Author(s) : Stojan J , Golicnik M , Froment MT , Estour F , Masson P
Ref : European Journal of Biochemistry , 269 :1154 , 2002
Abstract :
PubMedSearch : Stojan_2002_Eur.J.Biochem_269_1154
PubMedID: 11856351

Title : Interaction of Drosophila acetylcholinesterases with D-tubocurarine: an explanation of the activation by an inhibitor - Golicnik_2001_Biochemistry_40_1214
Author(s) : Golicnik M , Fournier D , Stojan J
Ref : Biochemistry , 40 :1214 , 2001
Abstract :
PubMedSearch : Golicnik_2001_Biochemistry_40_1214
PubMedID: 11170446

Title : Progress curves analysis as an alternative for exploration of activation-inhibition phenomena in cholinesterases - Golicnik_2001_J.Enzyme.Inhib_16_391
Author(s) : Golicnik M
Ref : J Enzyme Inhib , 16 :391 , 2001
Abstract :
PubMedSearch : Golicnik_2001_J.Enzyme.Inhib_16_391
PubMedID: 11916145