J. Stojan

J. Stojan, M. Goličnik, 2004, Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology.

Kinetic model of ethopropazine interaction with horse serum butyrylcholinesterase and its docking into the active site.

Z. Grubic, J. Stojan, G. Šinko, 2002, Archives of biochemistry and biophysics.

Acceleration of Drosophila melanogaster acetylcholinesterase methanesulfonylation: peripheral ligand D-tubocurarine enhances the affinity for small methanesulfonylfluoride.

D. Fournier, J. Stojan, M. Goličnik, 2002, Chemico-biological interactions.

Exploration of the Drosophila Acetylcholinesterase Substrate Activation Site Using a Reversible Inhibitor (Triton X-100) and Mutated Enzymes*

D. Fournier, S. Estrada-Mondaca, J. Stojan, 2000, The Journal of Biological Chemistry.

Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate.

J. Colletier, D. Fournier, J. Stojan, 2004, European journal of biochemistry.

Velocity of Ellman's reaction and its implication for kinetic studies in the millisecond time range

J. Stojan, M. Pavlič, 1992, Neurochemical Research.

Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion.

M. Froment, P. Masson, J. Stojan, 2002, European journal of biochemistry.

On the inhibition of cholinesterase by D-tubocurarine.

J. Stojan, M. Pavlič, M. Pavlicˇ, 1991, Biochimica et biophysica acta.

Kinetic characterization of all steps of the interaction between acetylcholinesterase and eserine.

J. Stojan, M. Zorko, 1997, Biochimica et biophysica acta.

Mechanism of stereoselective interaction between butyrylcholinesterase and ethopropazine enantiomers.

Z. Kovarik, J. Stojan, G. Šinko, 2011, Biochimie.

Multiple interaction sites of galnon trigger its biological effects

T. Bártfai, Ü. Langel, M. Wheatley, 2005, Neuropeptides.

Autocatalytic processing of recombinant human procathepsin B is a bimolecular process

V. Turk, B. Turk, J. Stojan, 1999, FEBS letters.

Acetylcholinesterase alterations reveal the fitness cost of mutations conferring insecticide resistance

D. Fournier, Zhenhua Tang, J. Stojan, 2004, BMC Evolutionary Biology.

Antifungal activity of cinnamic acid derivatives involves inhibition of benzoate 4‐hydroxylase (CYP53)

S. Turk, R. Komel, M. Bunc, 2014, Journal of applied microbiology.

Inhibition of Drosophila acetylcholinesterase by 7-(methylethoxyphosphinyloxy)1-methyl-quinolinium iodide.

D. Fournier, J. Stojan, V. Marcel, 1999, Chemico-biological interactions.

Homology built model of acetylcholinesterase from Drosophila melanogaster.

J. Stojan, 1999, Journal of enzyme inhibition.

Insights into substrate and product traffic in the Drosophila melanogaster acetylcholinesterase active site gorge by enlarging a back channel

D. Fournier, F. Nachon, J. Stojan, 2008, The FEBS journal.

Rational polynomial equation as an unbiased approach for the kinetic studies of Drosophila melanogaster acetylcholinesterase reaction mechanism.

D. Fournier, J. Stojan, M. Goličnik, 2004, Biochimica et biophysica acta.

Equations for progress curves of some kinetic models of enzyme-single substrate-single slow binding modifier system.

J. Stojan, 1998, Journal of enzyme inhibition (Print).

Analysis of Progress Curves in an Acetylcholinesterase Reaction: A Numerical Integration Treatment

Jure Stojan, J. Stojan, 1997, J. Chem. Inf. Comput. Sci..

Interaction of Drosophila acetylcholinesterases with D-tubocurarine: an explanation of the activation by an inhibitor.

D. Fournier, J. Stojan, M. Goličnik, 2001, Biochemistry.

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.

J. Stojan, M. Goličnik, 2002, Biochimica et biophysica acta.

Inhibition and protection of cholinesterases by methanol and ethanol

Jure Stojan, D. Fournier, Ota Fekonja, 2007, Journal of enzyme inhibition and medicinal chemistry.

Conformational rigidity of cholinesterases allows for the prediction of combined effects in a particular double mutant.

J. Stojan, 2016, Chemico-biological interactions.

The significance of low substrate concentration measurements for mechanistic interpretation in cholinesterases.

J. Stojan, 2013, Chemico-biological interactions.

Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site.

Z. Grubic, M. Sentjurc, Z. Radić, 1999, Biochimica et biophysica acta.

Mechanism of eserine action on the hydrolysis of butyrylthiocholine by butyrylcholinesterase.

J. Stojan, M. Pavlič, 1997, Journal of enzyme inhibition.

The influence of an organosulfonate on the reaction between Ellman's reagent and thiocholine.

J. Stojan, M. Pavlič, 1994, Journal of analytical toxicology.

Kinetic insight into the mechanism of cholinesterasterase inhibition by aflatoxin B1 to develop biosensors.

Jean-Louis Marty, Jure Stojan, J. Marty, 2009, Biosensors & bioelectronics.

Cytochrome P450 Monooxygenase CYP53 Family in Fungi: Comparative Structural and Evolutionary Analysis and Its Role as a Common Alternative Anti-Fungal Drug Target

Jure Stojan, Suresh Babu Pakala, Radovan Komel, 2014, PloS one.

The versatility of the fungal cytochrome P450 monooxygenase system is instrumental in xenobiotic detoxification

J. Bohlmann, R. Komel, S. Berne, 2011, Molecular microbiology.

Virtual Screening Yields Inhibitors of Novel Antifungal Drug Target, Benzoate 4-Monooxygenase

Samo Turk, Jure Stojan, Stanislav Gobec, 2012, J. Chem. Inf. Model..

CYP53A15 of Cochliobolus lunatus, a target for natural antifungal compounds.

Jure Stojan, Tea Lanisnik Rizner, Damjana Rozman, 2008, Journal of medicinal chemistry.

The mechanism and benefit of human butyrylcholinesterase activation by what would otherwise be inhibitors.

J. Stojan, 2019, Chemico-biological interactions.

Rapid Mechanistic Evaluation and Parameter Estimation of Putative Inhibitors in a Single-Step Progress-Curve Analysis: The Case of Horse Butyrylcholinesterase

J. Stojan, 2017, Molecules.

Kinetics of Torpedo californica acetylcholinesterase inhibition by bisnorcymserine and crystal structure of the complex with its leaving group.

N. Greig, Qian-sheng Yu, C. Bartolucci, 2012, The Biochemical journal.

Non-productive binding of butyryl(thio)choline in the active site of vertebrate acetylcholinesterase.

J. Stojan, 2010, Chemico-biological interactions.

Kinetic evaluation of multiple initial rate data by simultaneous analysis with two equations.

J. Stojan, 2008, Chemico-biological interactions.

Evidence for subdomain flexibility in Drosophila melanogaster acetylcholinesterase.

D. Fournier, L. Paquereau, J. Stojan, 2008, Biochemistry.

Crystallization, X-ray diffraction analysis and phasing of 17beta-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus.

A. Cassetta, K. Kristan, D. Lamba, 2005, Acta crystallographica. Section F, Structural biology and crystallization communications.

17β-Hydroxysteroid Dehydrogenase from Cochliobolus lunatus: Model Structure and Substrate Specificity

J. Adamski, T. Rižner, J. Stojan, 2000 .

Identification and characterization of the novel reversible and selective cathepsin X inhibitors

J. Kos, S. Gobec, D. Knez, 2017, Scientific Reports.

Rational design of novel mutants of fungal 17beta-hydroxysteroid dehydrogenase.

J. Adamski, K. Kristan, J. Stojan, 2007, Journal of biotechnology.

Searching for the physiological function of 17β-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus: studies of substrate specificity and expression analysis

J. Adamski, T. Rižner, J. Stojan, 2001, Molecular and Cellular Endocrinology.

Structural basis for inhibition of 17β-hydroxysteroid dehydrogenases by phytoestrogens: The case of fungal 17β-HSDcl

A. Cassetta, K. Kristan, D. Lamba, 2017, The Journal of Steroid Biochemistry and Molecular Biology.

The role of Ala231 and Trp227 in the substrate specificities of fungal 17β-hydroxysteroid dehydrogenase and trihydroxynaphthalene reductase: Steroids versus smaller substrates

T. Rižner, J. Stojan, M. B. Svegelj, 2012, The Journal of Steroid Biochemistry and Molecular Biology.

Insights into subtle conformational differences in the substrate-binding loop of fungal 17β-hydroxysteroid dehydrogenase: a combined structural and kinetic approach.

A. Cassetta, K. Kristan, D. Lamba, 2012, The Biochemical journal.

BMC Biochemistry BioMed Central

J. Adamski, K. Kristan, T. Rižner, 2005 .

Pyrithione-based ruthenium complexes as inhibitors of aldo-keto reductase 1C enzymes and anticancer agents.

I. Turel, J. Stojan, K. Traven, 2016, Dalton transactions.

A novel keratin 5 mutation (K5V186L) in a family with EBS-K: a conservative substitution can lead to development of different disease phenotypes.

E. Lane, R. Komel, A. Vahlquist, 2001, The Journal of investigative dermatology.

Traders in Nature: Marketing Natural Medicine in 20th-century Britain

J. Stojan, 2013 .

Ruthenium complexes show potent inhibition of AKR1C1, AKR1C2, and AKR1C3 enzymes and anti-proliferative action against chemoresistant ovarian cancer cell line

I. Turel, T. Rižner, J. Stojan, 2022, Frontiers in Pharmacology.

Towards the first inhibitors of trihydroxynaphthalene reductase from Curvularia lunata: synthesis of artificial substrate, homology modelling and initial screening.

M. Anderluh, S. Gobec, B. Štefane, 2008, Bioorganic & medicinal chemistry.

Generalized Theoretical and Practical Treatment of the Kinetics of an Enzyme-Catalyzed Reaction in the Presence of an Enzyme Equimolar Irreversible Inhibitor

Marko Goličnik, Jure Stojan, J. Stojan, 2003, J. Chem. Inf. Comput. Sci..

Simultaneous binding of coenzyme and two ligand molecules into the active site of fungal trihydroxynaphthalene reductase.

T. Rižner, J. Stojan, M. Brunskole, 2009, Chemico-biological interactions.

Trihydroxynaphthalene reductase of Curvularia lunata--a target for flavonoid action?

S. Martens, S. Gobec, J. Stojan, 2009, Chemico-biological interactions.

Substrate recognition sites in 14alpha-sterol demethylase from comparative analysis of amino acid sequences and X-ray structure of Mycobacterium tuberculosis CYP51.

T. Poulos, M. Waterman, J. Stojan, 2001, Journal of inorganic biochemistry.

Phytoestrogens as inhibitors of fungal 17β-hydroxysteroid dehydrogenase

Janez Konc, Jure Stojan, Tea Lanišnik Rižner, 2005, Steroids.

Intestinal Cell Barrier Function In Vitro Is Severely Compromised by Keratin 8 and 18 Mutations Identified in Patients with Inflammatory Bowel Disease

E. Lane, R. Komel, J. Stojan, 2014, PloS one.

Structure of recombinant human butyrylcholinesterase in complex with a coumarin-based fluorescent probe linked to sulfonamide type inhibitor.

M. Zorović, N. Coquelle, J. Colletier, 2020 .

Dimerization and enzymatic activity of fungal 17β-hydroxysteroid dehydrogenase from the short-chain dehydrogenase/reductase superfamily

J. Adamski, K. Kristan, T. Rižner, 2005, BMC Biochemistry.

Functional characterization of β2-adrenergic and insulin receptor heteromers

N. Veljkovic, L. Drinovec, S. Glišić, 2019, Neuropharmacology.

Characterisation and expression of a gene encoding a mutarotase from the fungus Rhizopus nigricans.

D. Fournier, J. Stojan, B. Črešnar, 2004, FEMS microbiology letters.

Automatic Assembly and Calibration of Models of Enzymatic Reactions Based on Ordinary Differential Equations.

D. Janežič, M. Hodošček, J. Stojan, 2021, Methods in molecular biology.

DEPTOR polymorphisms influence late complications in Type 2 diabetes patients.

S. Horvat, V. Dolžan, J. Stojan, 2019, Pharmacogenomics.

Structural insights into substrate traffic and inhibition in acetylcholinesterase

I. Silman, G. Zaccai, J. Colletier, 2006, The EMBO journal.

The versatility of the fungal cytochrome P450 monooxygenase system is instrumental in xenobiotic detoxification

J. Bohlmann, R. Komel, J. Stojan, 2011, Molecular microbiology.

Substrate-dependent inactivation of recombinant paraoxonase 1 during catalytic dihydrocoumarin turnover and the protective properties of surfactants.

J. Stojan, A. Bavec, M. Goličnik, 2023, Chemico-biological interactions.

Exploring the aryl esterase catalysis of paraoxonase-1 through solvent kinetic isotope effects and phosphonate-based isosteric analogues of the tetrahedral reaction intermediate.

S. Gobec, D. Knez, J. Stojan, 2014, Biochimie.

Acetylcholinesterase alterations reveal the fitness cost of mutations conferring insecticide resistance

D. Fournier, J. Stojan, A. Lougarre, 2004, BMC Evolutionary Biology.

The role of Ala231 and Trp227 in the substrate specificities of fungal 17β-hydroxysteroid dehydrogenase and trihydroxynaphthalene reductase: Steroids versus smaller substrates

T. Rižner, J. Stojan, M. B. Svegelj, 2012, The Journal of Steroid Biochemistry and Molecular Biology.

Pyrithione-based ruthenium complexes as inhibitors of aldo-keto reductase 1C enzymes and anticancer agents.

I. Turel, J. Stojan, K. Traven, 2016, Dalton transactions.