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Institute of Biochemistry
Faculty of Medicine

University of Ljubljana
Vrazov trg 2
SI 1000, Ljubljana

Tel: +386-1-543-7640
Fax: +386-1-543-7641

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Laboratory for enzyme research



2014 I 2013 I 2012 I 2011 I 2010 I 2009 I 2008 I 2007 I 2006 I 2005 I 2004 I 2003 I 2002 I 2001 I 2000 I up to 2000


  • 157. Bavec A, Insulin, other hypoglycemic drugs, and glucagon, in Side Effects of Drugs Annual (2014), Volume 36, 645-657, ed. Ray Sidhartha, Elsevier.
  • 156. Bavec A, Kinase Activity Studied in Living Cells Using an Immunoassay. J. Chem. Edu. (2014) 91, 2171–2173.
  • 155. Bavec A, Knez D, Makovec T, Stojan J, Gobec S, Goličnik M. Exploring the aryl esterase catalysis of paraoxonase-1 through solvent kinetic isotope effects and phosphonate-based isosteric analogues of the tetrahedral reaction intermediate. Biochimie (2014) 106, 184–186.
  • 154. Brus B, Košak U, Turk S, Pišlar A, Coquelle N, Kos J, Stojan J, Colletier JP, Gobec S. Discovery, biological evaluation, and crystal structure of a novel nanomolar selective butyrylcholinesterase inhibitor. J Med Chem (2014, in press)
  • 153. Jawallapersand P, Mashele SS, Kovačič L, Stojan J, Komel R, Pakala SB, Kraševec N, Syed K. Cytochrome P450 Monooxygenase CYP53 family in fungi: comparative structural and evolutionary analysis and its role as a common alternative anti-fungal drug target. PLoS One (2014) 9, e107209.
  • 152. Goličnik M. Progress-curve analysis through integrated rate equations, and its use to study cholinesterase reaction dynamics. J Mol Neurosci (2014) 53, 330-334.
  • 151. Korošec B, Sova M, Turk S, Kraševec N, Novak M, Lah L, Stojan J, Podobnik B, Berne S, Zupanec N, Bunc M, Gobec S, Komel R. Antifungal activity of cinnamic acid derivatives involves inhibition of benzoate 4-hydroxylase (CYP53). J Appl Microbiol (2014) 116, 955-966.
  • 150. Bavec A. (Poly)peptide-based therapy for diabetes mellitus: insulins versus incretins. Life Sci (2014) 99, 7-13.
  • 149. Zupancic T, Stojan J, Lane EB, Komel R, Bedina-Zavec A, Liovic M. Intestinal cell barrier function in vitro is severely compromised by keratin 8 and 18 mutations identified in patients with inflammatory bowel disease. PLoS One (2014) 9, e99398.


  • 148. Goličnik M. Solution of the Webb equation for kinetics of cholinesterase substrate inhibition/activation using the adomian decomposition method. MATCH Commun Math Comput Chem (2013) 70, in print
  • 147. Bavec A. Mono-ADP-ribosyltransferase as a potential pharmacological drug target in the GLP-1 based therapy of obesity and diabetes mellitus type 2. Acta Chim Slov (2013) 60: 237-42.
  • 146. Skedelj V, Perdih A, Brvar M, Kroflič A, Dubbée V, Savage V, O'Neill AJ, Solmajer T, Bešter-Rogač M, Blanot D, Hugonnet JE, Magnet S, Arthur M, Mainardi JL, Stojan J, Zega A. Discovery of the first inhibitors of bacterial enzyme d-aspartate ligase from Enterococcus faecium (Aslfm) Eur J Med Chem (2013) 28: 208-220.
  • 145. Goličnik M. The integrated Michaelis-Menten rate equation : déja` vu or vu ja`dé? J Enzyme Inhib Med Chem (2013) 28: 879-893.
  • 144. Goličnik M. "Die Kinetik der Invertinwirkung" of L. Michaelis and M. L. Menten revisited after 100 years : closed-form solutions of genuine invertase-reaction dynamics. MATCH Commun Math Comput Chem (2013) 70, 63-72.
  • 143. Prosenc U, Korenčič A, Košir R, Goličnik M, Sassone Corsi P, Rozman D. Inducible cAMP Early Repressor regulates Period 1 gene of the hepatic and adrenal clocks. J Biol Chem (2013) 288, 10318-10327.
  • 142. Belič A, Ačimovič J, Naik A, Goličnik M. Analysis of the steady-state relations and control-algorithm characterisation in a mathematical model of cholesterol biosynthesis. Simulation modelling practice and theory (2013) 18-27.
  • 141. Stojan J. The significance of low substrate concentration measurements for mechanistic interpretation in cholinesterases. Chem-Biol Interact (2013) 203, 44-50.


  • 140. Goličnik M. On the Lambert W function and its utility in biochemical kinetics. Biochem Eng J (2012) 63, 116-123.
  • 139. Pazos E, Goličnik M, Mascarenas JL, Vazquez ME. Detection of phosphorylation states by intermolecular sensitization of lanthanide-peptide conjugates. Chem Commun (2012) 48, 9534-9536.
  • 138. Goličnik M. Estimation of kinetic parameters for enzyme-Inhibition reaction models using direct time-dependent equations for reactant concentrations. Acta Chim Slov (2012) 59, 207-211.
  • 137. Goličnik M. Alternative algebraic rate-integration approach for progress-curve analysis of enzyme kinetics. Eng Life Sci (2012) 12, 104-108.
  • 136. Korenčič A, Bordyugov G, Košir R, Rozman D, Goličnik M, Herzel H. The interplay of cis-regulatory elements rules circadian rhythms in mouse liver. PloS One (2012) 7, 1-13.
  • 135. Cassetta A, Krastanova I, Kristan K, Brunskole Švegelj M, Lamba D, Lanišnik Rižner T, Stojan J. Insights into subtle conformational differences in the substrate-binding loop of fungal 17ß-hydroxysteroid dehydrogenase: a combined structural and kinetic approach. Biochem J (2012) 441, 151-160.
  • 134. Bartolucci C, Stojan J, Yu QS, Greig NH, Lamba D. Kinetics of Torpedo californica acetylcholinesterase inhibition by bisnorcymserine and crystal structure of the complex with its leaving group. Biochem J (2012) 444, 269-277.
  • 133. Berne S, Podobnik B, Zupanec N, Novak M, Kraševec N, Turk S, Korošec B, Lah L, Šuligoj E, Stojan J, Gobec S, Komel R. Virtual screening yields inhibitors of novel antifungal drug target, benzoate 4-monooxygenase. J Chem Inf Mod (2012) 52, 3053-3063.
  • 132. Brunskole Švegelj M, Stojan J, Lanišnik Rižner T. The role of Ala231 and Trp227 in the substrate specificities of fungal 17ß-hydroxysteroid dehydrogenase and trihydroxynaphthalene reductase: steroids versus smaller substrates. J Steroid Biochem Mol Biol (2012) 129, 91-98.
  • 131. Deželak M, Bavec A. Glucagon like-peptide-1 receptor is covalently modified by endogenous mono-ADP-ribosyltransferase. Mol Biol Rep (2012) 39, 4375-4381.
  • 130. Anko M, Majhenc J, Kogej K, Sillard R, Langel Ü, Anderluh G, Zorko M. Influence ofstearyl and trifluoromethylquinoline modifications of the cell penetrating peptide TP10 on its interaction with a lipid membrane. Biochim Biophys Acta, Biomembr (2012) 1818, 915-924.
  • 129. Howl J, Matou-Nasri S, West DC, Zorko M. Bioportide: an emergent concept of bioactive cell-penetrating peptides. Cell Mol Life Sci (2012) 69, 2951-2966.


  • 128. Goličnik M. Explicit analytic approximations for time-dependent solutions of the generalized integrated Michaelis-Menten equation. Anal biochem (2011) 411, 303-305.
  • 127. Ačimovič J, Košir R, Kastelec D, Perše M, Majdič G, Rozman D, Košmelj K, Goličnik M. Circadian rhythm of cholesterol synthesis in mouse liver : a statistical analysis of the post-squalene metabolites in wild-type and Crem-knockout mice. Biochem Biophys Res Commun (2011) 408, 635-641.
  • 126. Goličnik M. Evaluation of enzyme kinetic parameters using explicit analytic approximationsto the solution of the Michaelis-Menten equation. Biochem Eng J (2011) 53, 234-238.
  • 125. Goličnik M. Exact and approximate solutions for the decades-old Michaelis-Menten equation: progress-curve analysis through integrated rate equations. Biochem Mol Biol Educ (2011) 39, 117-125.
  • 124. Goličnik M. Explicit reformulations of the Lambert W-omega function for calculations of the solutions to one-compartment pharmacokinetic models with Michaelis-Menten elimination kinetics. Eur J Drug Metab Pharmakokinet (2011) 36, 121-127.
  • 123. Goličnik M. An alternative explicit model expression equivalent to the integrated Michaelis-Menten equation and its application to nonlinear saturation pharmacokinetics. Ther Drug Monit (2011) 33, 362-365.
  • 122. Šinko G, Kovarik Z, Reiner E, Simeon Rudolf V, Stojan J. Mechanism of stereoselective interaction between butyrylcholinesterase and ethopropazine enantiomers. Biochimie (2011) 93, 1797-1806.
  • 121. Brunskole Švegelj M, Turk S, Brus B, Srojan J, Lanišnik Rižner T, Gobec S. Novel inhibitors of trihydroxynaphthalene reductase with antifungal activity identified by ligand-based and structure-based virtual screening. J Chem Inf Mod (2011) 51, 1716-1724.
  • 120. Lah L, Podobnik B, Novak M, Korošec B, Berne S, Vogelsang M, Kraševec N, Zupanec N, Stojan J, Bohlmann J, Komel R. The versatility of the fungal cytochrome P450 monooxygenase system is instrumental in xenobiotic detoxification. Mol Microbiol (2011) 85, 1374-1389.
  • 119. Bevc S, Konc J, Stojan J, Hodošček M, Penca M, Praprotnik M, Janežič Dušanka. ENZO: a web tool for derivation and evaluation of kinetic models of enzyme catalyzed reactions. PloS One (2011) 6, e22265.
  • 118. Bavec A. Structure, function and regulation of group IV phospholipase A2 family. Acta Chim Slov (2011) 58, 195-202.
  • 117. Deželak M, Bavec A. Third intracellular loop of glucagon like-peptide-1 receptor is coupled with endogenous mono-ADP-ribosyltransferase - Novel type of receptor regulation?. Eur J Pharmacol (2011) 666, 35-42.


  • 116. Langel, Ü, Cravatt BF, Gräslund A, Heijne G von, Land T, Niessen S, ZorkoM. Introduction to peptides and proteins. Boca Raton; London; New York: CRC Press, 2010.
  • 115. Goličnik M. Explicit reformulations of time-dependent solution for a Michaelis-Menten enzyme reaction model. Anal Biochem (2010) 406, 94-96.
  • 114. Goličnik M. Metallic fluoride complexes as phosphate analogues for structural and mechanistic studies of phosphoryl group transfer enzymes. Acta Chim Slov (2010) 57, 272-287.
  • 113. Košir R, Ačimovič J, Goličnik M, Perše M, Majdič G, Fink M, Rozman D. Determination of reference genes for circadian studies in different tissues and mouse strains. BMC Mol Biol (2010) 11, 60.
  • 112. Frasco MF, Eržen Ida, Stojan J, Guilhermino L. Localization and properties of cholinesterases in the common prawn (Palaemon serratus): a kinetic-histochemical study. Biol Bull (2010) 218, 1-5.
  • 111. Stojan J. Non-productive binding of butyryl(thio)choline in the active site of vertebrate acetylcholinesterase. Chem-Biol Interact (2010) 187, 128-134.
  • 110. Bavec A. Constructing glucagon like peptide-1 receptor fused with derivatives of GFP for visualizing protein-protein interaction in living cells. Mol Biol Rep (2010) 6, 2749-2755.


  • 109. Goličnik M, Olguin LF, Feng G, Baxter NJ, Waltho JP, Williams NH, Hollfelder F. Kinetic analysis of beta-phosphoglucomutase and its inhibition by magnesium fluoride. J Am Chem Soc (2009) 131, 1575-1588.
  • 108. Ačimovič J, Lovgrem Sandblom A, Monostory K, Rozman D, Goličnik M, Lutjohann D, Bjorkhem I. Combined gas chromatographic/mass spectrometric analysis of cholesterol precursors and plant sterols in cultured cells. J Chromatography B (2009), 877, 2081-2086.
  • 107. Hansmann T, Sanson B, Stojan J, Weik M, Marty JL, Fournier D. Kinetic insight into the mechanism of cholinesterasterase inhibition by aflatoxin B1 to develop biosensors. Biosens Bioelectron (2009) 24, 2119-2124.
  • 106. Corbel V, Stankiewicz M, Pennetier C, Fournier D, Stojan J, Girard E, Dimitrov M, Molgo J, Hougard JM, Lapied B. Evidence for inhibition of cholinesterases in insect and mammalian nervous systems by the insect repellent deet. BMC Biology (2009) 7, str. 47 [1-11].
  • 105. Brunskole Švegelj M, Zorko K, Kerbler V, Martens S, Stojan J, Gobec S, Lanišnik Rižner T. Trihydroxynaphthalene reductase of Curvularia lunata-A target for flavonoid action?. Chem-Biol Interact (2009) 178, 259-267.
  • 104. Stojan J, Brunskole Švegelj M, Lanišnik Rižner T. Simultaneous binding of coenzyme and two ligand molecules into the active siteof fungal trihydroxynaphthalene reductase. Chem-Biol Interact (2009) 178, 268-273.
  • 103. Kristan K, Brunskole Švegelj M, Stojan J, Lanišnik Rižner T. Two homologous fungal carbonyl reductases with different substrate specificities. Chem-Biol Interact (2009) 178, 295-302.
  • 102. Brunskole Švegelj M, Kristan K, Stojan J, Lanišnik Rižner T. Mutations that affect coenzyme binding and dimer formation of fungal 17beta-hydroxysteroid dehydrogenase. Mol Cell Endocrinol (2009) 301, 47-50.
  • 101. Brunskole Švegelj M, Lanišnik Rižner T, Stojan J. Enzymes of the short-chain dehydrogenase/reductase superfamily s new pharmacological targets. Farm Vestn (2009) 60, 159-164.
  • 100. Brunskole Švegelj M, Lanišnik Rižner T, Stojan J. Antimycotics : current and novel strategies for treatment of fungal infections. Farm Vvestn (2009) 60, 295-302.
  • 99. Anko M, Zorko M. Cell-penetrating peptides and their application. Farm Vestn (2009) 60, 307-312.
  • 98. Bavec A, Ličar A. Functional characterization of N-terminally GFP-tagged GLP-1 receptor. J Biomed Biotechnol (2009) 498149, 1-10.


  • 97. Ačimovič J, Fink M, Pompon D, Bjorkhem I, Hirayama J, Sassone Corsi P, Goličnik M, Rozman D. CREM modulates the circadian expression of CYP51, HMGCR, and cholesterogenesis in the liver. Biochem Biophys Res Commun (2008) 376, 206-210.
  • 96. Stojan J, Ladurantie C, Siadat OR, Paquereau L, Fournier D. Evidence for subdomain flexibility in Drosophila melanogaster acetylcholinesterase. Biochemistry (2008) 47, 5599-5607.
  • 95. Brunskole Švegelj M, Štefane B, Zorko K, Anderluh M, Stojan J, Lanišnik Rižner T, Gobec S. Towards the first inhibitors of trihydroxynaphthalene reductase from Curvularia lunataČ Synthesis of artificial substrate, homology modelling and initial screening. Bioorg Med Chem (2008) 16, 5881-5889.
  • 94. Stojan J. Kinetic evaluation of multiple initial rate data by simultaneous analysis with two equations. Chem-Biol Interact (2008) 175, 242-248.
  • 93. Nachon F, Stojan J, Fournier D. Insights into substrate and product traffic in the Drosophila melanogaster acetylcholinesterase active site gorge by enlarging a back channel. FEBS J (2008) 275, 2654-2664.
  • 92. Podobnik B, Stojan J, Lah L, Kraševec N, Seliškar M, Lanišnik Rižner T, Rozman D, Komel R. CYP53A15 of Cochiobolus lunatus, a target for natural antifungal compounds. J Med Chem (2008) 51, 3480-3486.
  • 91. Arsov Z, Nemec M, Schara MV, Johansson H, Langel Ü, Zorko M. Cholesterol prevents interaction of the cell-penetrating peptide transportan with model lipid membranes. J Pept Sci (2008) 14, 1303-1308.
  • 90. Brunskole Švegelj M, Lanišnik Rižner T, Stojan J. Enzymes involved in fungal melanin biosynthesis - potential targets for the development of new antimicotic drugs. Farm Vestn (2008) 59, 21-25.
  • 89. Stojan R, Stojan Ž, Stojan J. Cholinesterases: structure, mechanism and inhibition by natural and synthetic poisons. Med Razgl (2008) 47, 293-307.


  • 88. Hällbrink M, Pooga M, Metsis M, Kogerman P, Valkna A, Meikas A, Lindgren M, Gräslund A, Budihna M, Zorko M. Cell-selective delivery system : [patent number] EP 1 516 184 B1 : application number: 03760107.7. Paris: European Patent Office, 1.8. 2007.
  • 87. Massa C, Clausen M, Stojan J, Lamba D, Campa C. Study of the mode of action of a polygalacturonase from the phytopathogen Burkholderia cepacia. Biochem J (2007) 407, 207-217.
  • 86. Kristan K, Adamski J, Lanišnik Rižner T, Stojan J. His164 regulates accessibility to the active site in fungal 17beta-hydroxysteroid dehydrogenase. Biochimie (2007) 89, 63-71.
  • 85. Frasco MF, Colletier JP, Weik M, Carvalho F, Guilhermino L, Stojan J, Fournier D. Mechanisms of cholinesterase inhibition by inorganic mercury. FEBS J (2007) 274, 1849-1861.
  • 84. Kristan K, Stojan J, Adamski J, Lanišnik Rižner T. Rational design of novel mutants of fungal 17beta-hydroxysteroid dehydrogenase. J Biotechnol (2007) 129, 123-130.
  • 83. Fekonja O, Zorec Karlovšek M, El Kharbili M, Fournier D, Stojan J. Inhibition and protection of cholinesterases by methanol and ethanol. J Enzyme Inhib Med Chem (2007) 22, 407-415.
  • 82. Bavec A, Jiang Y, Langel Ü, Zorko M. Role of cysteine 341 and arginine 348 of GLP-1 receptor in G-protein coupling. Mol Biol Rep (2007) 34, 53-60.


  • 81. Baxter NJ, Olguin LF, Goličnik M. A Trojan horse transition state analogue generated by MgF3- formation in an enzyme active site. Proc Natl Acad Sci USA (2006) 103, 14732-14737.
  • 80. Miš K, Marš T, Goličnik M, Jevšek M, Grubič Z. Effects of acetylcholinesterase gene silencing on its activity in cultured human skeletal muscle. J Mol Neurosci (2006) 30, 31-32.
  • 79. Colletier JP, Fournier D, Greenblatt HM, Stojan J, Sussman J, Zaccai G, Silman I, Weik M. Structural insights into substrate traffic and inhibition in acetylcholinesterase. EMBO J (2006) 25, 2746-2756.
  • 78. Stojan J. Enzyme kinetics and molecular modeling complement each other at study of reaction mechanisms. Informatica medica slovenica (2006) 11, 60-65.
  • 77. Mariggiò S, Bavec A, Natale E, Zizza P, Salmona M, Corda D, Di Girolamo M. G[alpha](13) mediates activation of the cytosolic phospholipase A(2)[alpha] through fine regulation of ERK phosphorylation. Cell Signal (2006) 18, 2200-2208.
  • 76. Štempelj M, Bavec A, Ferjan I. Regulation of nerve growth factor induced histamine and arachidonic acid release from rat mast cells by cannabinoids. Inflamm Res (2006) 55, S9-S10.
  • 75. Jan J, Vrecl M, Pogačnik A, Gašperšič D, Zorko M. Distribution of organochlorine pollutants in ovine dental tissue and bone. Environ Toxicol Pharmacol (2006) 21, 103-107.
  • 74. Štempelj M, Zorko M, Peternel L, Urleb U, Ferjan I. Histamine release, an undesired effect of thrombin inhibitors with basic character, is mediated through direct activation of Gi proteins. Eur J Pharmacol (2006) 538, 182-187.


  • 73. Miš K, Marš T, Jevšek M, Strašek H, Goličnik M, Brecelj J, Komel R, King MP, Miranda AF, Grubič Z. Expression and distribution of acetylcholinesterase among the cellular components of the neuromuscular junction formed in human myotube in vitro. Chem-Biol Interact (2005) 157/158, 29-35.
  • 72. Kristan K, Deluca D, Adamski J, Stojan J, Lanišnik Rižner T. Dimerization and enzymatic activity of fungal 17beta-hydroxysteroid dehydrogenase from the short-chain dehydrogenase/reductase superfamily. BMC Biochem (2005) 6, 1-10.
  • 71. Stojan J. Rational polynomial equation helps to select among homeomorphic kinetic models for cholinesterase reaction mechanism. Chem-Biol Interact (2005) 157-158, 173-179.
  • 70. Kristan K, Stojan J, Moller G, Adamski J, Lanišnik Rižner T. Coenzyme specificity in fungal 17ß-hydroxysteroid dehydrogenase. Mol Cell Endocrinol (2005) 241, 80-87.
  • 69. Kristan K, Krajnc K, Konc J, Gobec S, Stojan J, Lanišnik Rižner T. Phytoestrogens as inhibitors of fungal 17ß-hydroxysteroid dehydrogenase. Steroids (2005) 70, 626-635.
  • 68. Cassetta A, Budefeld T, Lanišnik Rižner T, Kristan K, Stojan J, Lamba D. Crystallization, X-ray diffraction analysis and phasing of 17ß-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus. Acta crystallographica. Section F (2005) F61, 1032-1034.
  • 67. Zorko M, Langel Ü. Cell-penetrating peptides: mechanism and kinetics of cargo delivery. Adv Drug Deliv Rev (2005) 57, 529-545.
  • 66. Arsov Z, Zorko M, Schara MV. Inhibition of erythrocyte acetylcholinesterase by n-butanol at high concentrations. Arch Biochem Biophys (2005) 437, 78-84.
  • 65. Östlund P, Budihna M, Černe K, Bavec A, Zorko M. Cell-penetrating mimics of agonist-activated G-protein coupled receptors. Int J Pept Res Therap (2005) 11, 237-247.
  • 64. Floren A, Zorko M, Stojan J, Budihna M. Multiple interaction sites of galnon trigger its biological effects. Neuropeptides (2005) 39, 547-558.


  • 63. Goličnik M, Stojan J. Slow-binding inhibition. Biochem Mol Biol Educ (2004) 32, 228-235.
  • 62. Stojan J, Goličnik M, Fournier D. Rational polynomial equation as an unbiased approach for the kinetic studies of Drosophila melanogaster acetylcholinesterase reaction mechanism. Biochim Biophys Acta, Proteins and proteomics (2004) 1703, 53-61.
  • 61. Shi MA, Lougarre A, Alies C, Fremaux I, Tang ZH, Stojan J, Fournier D. Acetylcholiensterase alterations reveal the fitness cost of mutations conferring insecticide resistance. BMC Evol Biol (2004), 4, št. 5.
  • 60. Stojan J, Brochier L, Alies C, Colletier JP, Fournier D. Inhibition of Drosophila melanogaster acetylcholinesterase by high concentations of substrate. Eur J Biochem (2004) 271, 1364-1371.
  • 59. Marinko P, Krbavčič A, Mlinšek G, Šolmajer T, Trampuš Bakija A, Stegnar M, Stojan J, Kikelj D. Novel non-covalent thrombin inhibitors incorporating P1 4,5,6,7-tetrahydrobenzothiazole arginine side chain mimetics. Eur J Med Chem (2004) 39, 257-265.
  • 58. Vilfan T, Črešnar B, Fournier D, Stojan J, Breskvar K. Characterisation and expression of a gene encoding a mutarotase from the fungus Rhizopus nigricans. FEMS Microbiol Lett (2004) 235, 101-108.
  • 57. Bavec A. Immunoassay for visualization of protein-protein interactions on Ni-nitrilotriacetate support: example of a laboratory exercise with recombinant heterotrimeric G[alpha]i2[beta]1[gamma]2 tagged by hexahistidine from sf9 cells. Biochem Mol Biol Educ (2004) 32, 258-262.
  • 56. Bavec A. Novel features of amphiphibic peptide Mas7 in signalling via heterotrimeric G-proteins. J Pept Sci (2004) 10, 691-699.
  • 55. Arsov Z, Schara MV, Zorko M, Štrancar J. The membrane lateral domain approach in the studies of lipid-protein interaction of GPI-anchored bovine erythrocyte acetylcholinesterase. Eur Biophys J (2004) 33, 715-725.


  • 54. Kristan K, Lanišnik Rižner T, Stojan J, Gerber JK, Kremmer E, Adamski J. Significance of individual amino acid residues for coenzyme and substrate specificity of 17beta-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus. Chem-Biol Interact (2003) 143/144, 493-501.
  • 53. Goličnik M, Stojan J. Generalized theoretical and practical treatment of the kinetics of an enzyme-catalyzed reaction in the presence of an enzyme equimolar irreversible inhibitor. J Chem Inf Comput Sci (2003) 43, 1486-1493.
  • 52. Čarman-Kržan M, Bavec A, Zorko M. Molecular characterization of specific H1-receptor agonists histaprodifen and its Nalpha-substituted analogues on bovine aortic H1-receptors. Naunyn Schmiedebergs Arch Pharmacol (2003) 367, 538-546.
  • 51. Bavec A, Hällbrink M, Langel Ü, Zorko M. Different role of intracellular loops of glucagon-like peptide-1 receptor in G-protein coupling. Regul Pept (2003) 111, 137-144.


  • 50. Goličnik M. On a nonelementary progress curve equation and its application in enzyme kinetics. J Chem Inf Comput Sci (2002) 42, 157-161.
  • 49. Goličnik M, Šinko G, Simeon Rudolf V, Grubič Z, Stojan J. Kinetic model of ethopropazine interaction with horse serum butyrylcholinesterase and its docking into the active site. Arch Biochem Biophys (2002) 398, 23-31.
  • 48. Goličnik M, Stojan J. 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. Biochim Biophys Acta, Prot struct mol enzymol (2002) 1597, 164-172.
  • 47. Goličnik M, Fournier D, Stojan J. Acceleration of Drosophila melanogaster acetylcholinesterase methanesulfonylation: peripheral ligand D-tubocurarine enhances the affinity for small methanesulfonylfluoride. Chem-Biol Interact (2002) 139, 145-157.
  • 46. Stojan J, Goličnik M, Froment MT, Estour F, Masson P. Concentration-dependent reversible activation-inhibition of human butyrylcholinesterase by tetraethylammonium ion. Eur J Biochem (2002) 269, 1154-1161.
  • 45. Goličnik M, Stojan J. Transient kinetic approach to the study of acetylcholinesterase reversible inhibition by eseroline. J Enzyme Inhib Med Chem (2002) 17, 279-285.
  • 44. Lenasi H, Bavec A, Zorko M. Membrane-bound progesterone receptors coupled to G proteins in the fungus Rhizopus nigricans. FEMS Microbiol Lett (2002), 213, 97-101.


  • 43. Goličnik M, Fournier D, Stojan J. Interaction of Drosophila acetylcholinesterases with D-tubocurarine: an explanation of the activation by an inhibitor. Biochemistry (2001) 40, 1214-1219.
  • 42. Goličnik M. Progress curves analysis as an alternative for exploration of activation-inhibition phenomena in cholinesterases. J Enzym Inhib (2001) 16, 391-399.
  • 41. Lanišnik Rižner T, Stojan J, Adamski J. 17beta-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus: structural and functional aspects. Chem-Biol Interact (2001) 130/2, 793-803.
  • 40. Stojan J. Slow detection reaction can mimic initial inhibition of an enzymic reaction. J Enzym Inhib (2001), letn. 16, št. 2, str. 89-94.
  • 39. Podust LM, Stojan J, Poulos TL, Waterman MR. Substrate recognition sites in 14alpha-sterol demethylase from comparative analysis of amino acid sequences and X-ray structure of Mycobacterium tuberculosis CYP51. J Inorg Biochem (2001) 87, 227-235.
  • 38. Liović M, Stojan J, Bowden PE, Gibbs D, Vahlquist A, Lane BE, Komel R. A novel keratin 5 mutation (K5V186L) in a family with EBS-K: a conservative substitution can lead to development of different disease phenotypes. J Invest Dermatol. (2001) 116, 964-969.
  • 37. Lanišnik Rižner T, Stojan J, Adamski J. Searching for the physiological function of 17beta-hydroxysteroid dehydrogenase from the fungus Cochliobolus lunatus: studies of substrate specificity and expression analysis. Mol Cell Endocrinol (2001) 171, 193-198.
  • 36. Bavec A. Structure-activity relationships of some peptide antibiotics. Med Razgl (2001) 40, 165-171.


  • 35. Lanišnik Rižner T, Adamski J, Stojan J. 17beta-hydroxysteroid dehydrogenase from Cochliobolus lunatus: model structureand substrate specificity. Arch Biochem Biophys (2000) 384, 255-262.
  • 34. Marcel V, Estrada Mondaca S, Magne F, Stojan J, Klaebe A, Fournier D. Exploration of the Drosophila acetylcholinesterase substrate activation site using a reversible inhibitor (Triton X-100) and mutated enzymes. J Biol Chem (2000) 275, 11603-11609.
  • 33. Bavec A, Podgornik A, Zorko M. Purification of GTP[gamma]S binding proteins from membranes of porcine brain using convective interaction media (CIM) supports. Acta Chim Slov (2000) 47, 371-379.
  • 32. Soomets U, Lindgren M, Gallet X, Hällbrink M, Elmquist A, Balaspiri L, Zorko M, Pooga M, Brasseur R, Langel Ü. Deletion analogues of transportan. Biochim Biophys Acta (2000) 1467, 165-176.
  • 31. Rezaei K, Saar R, Soomets U, Valkna A, Näsman J, Zorko M, Åkerman K, Schroeder T, Bartfai T, Langel Ü. Role of third intracellular loop of galanin receptor type 1 in signal transdution. Neuropeptides (2000) 34, 25-31.
  • 30. Zorko M, Gottlieb H, Žakelj-Mavrič M. Plurypotency of 17[beta]-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus. Steroids (2000), 65, 46-53.

up to 2000

  • 29. Šentjurc M, Pečar S, Stojan J, Marchot P, Radić Z, Grubić Z. Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site. Biochim Biophys Acta, Prot struct mol enzymol (1999) 1429, 349-358.
  • 28. Stojan J, Marcel V, Fournier D. Effect of tetramethylammonium, choline and edrophonium on insect acetylcholinesterase : test of a kinetic model. Chem-Biol Interact (1999), 119-120, 137-146.
  • 27. Stojan J, Marcel V, Fournier D. Inhibition of Drosophila acetylcholinesterase by 7-(methylethoxyphosphinyloxy)1-methyl-quinolinium iodide (MEPQ). Chem-Biol Interact (1999) 119-120, 147-157.
  • 26. Rozman Pungerčar J, Stojan J, Kuhelj R, Turk V, Turk B. Autocatalytic processing of recombinant human procathepsin B is a bimolecular process. FEBS Lett (1999) 459, 358-362.
  • 25. Stojan J. Homology built model of acetylcholinesterase from Drosophila melanogaster. J Enzym Inhib (1999) 14, 193-201.
  • 24. Soomets U, Mahlapuu R, Tehranian R, Jarvet J, Karelson E, Zimler M, Iverfeldt K, Zorko M, Graeslund A, Langel Ü. Regulation of GTPase and adenylate cyclase activity by amyloid beta-peptide and its fragments in rat brain tissue. Brain Res (1999) 850, 179-188.
  • 23. Bavec A, Jureus A, Cigić B, Langel Ü, Zorko M. Peptitergent PD1 affects the GTPase activity of rat brain cortical membranes. Peptides (1999) 20, 177-184.
  • 22. Hällbrink M, Saar K, Östenson CG, Soomets U, Efendic S, Howl J, Wheatley M, Zorko M, Langel Ü. Effects of vasopressin-mastoparan chimeric peptides on insulin release and G-protein activity. Regulat Pept (1999) 82, 45-51.
  • 21. Stojan J, Marcel V, Estrada Mondaca S, Klaebe A, Masson P, Fournier D. A putative kinetic model for substrate metabolisation by Drosophila acetylcholinesterase. FEBS Lett (1998) 440, 85-88.
  • 20. Stojan J. Equations for progress curves of some kinetic models of enzyme-single substrate-single slow binding modifier system. J Eenzym Inhib (1998) 13, 161-176.
  • 19. Pogačar M, Zorko M, Žakelj-Mavrič M. Substrate specificity of 17[beta]-hydroxysteroid dehydrogenase from Pleurotus ostreatus. Acta Chim Slov (1998) 45, 19-25.
  • 18. Bavec A, Soomets U, Langel Ü, Zorko M. Structural features of amphipathic peptides required for the activation of G-proteins. Acta Chim Slov (1998) 45, 27-34.
  • 17. Zorko M., Pooga M, Saar K, Razaei K, Langel Ü. Differential regulation of GTPase activity by mastoparan and galparan. Archives of Biochemistry (1998) 349, 321-328.
  • 16. Pooga M, Hällbrink M, Zorko M, Langel Ü. Cell penetration by transportan. FASEB J (1998) 12, 67-77.
  • 15. Saar K, Valkna A, Soomets U, Rezaei K, Zorko M, Zilmer M, Langel Ü. Role of the third cytoplasmic loop in signal transduction by galanin receptors. Biochem Soc Trans (1997) 25, 1036-1040.
  • 14. Stojan J, Zorko M. Kinetic characterization of all steps of the interaction between acetylcholinesterase and eserine. Biochim Biophys Acta (1997) 1337, 75-84.
  • 13. Soomets U, Hällbrink M, Zorko M, Langel Ü. From galanin and mastoparan to galparan and transportan. Current topics in peptide & protein research (1997) 2, 83-113.
  • 12. Lanišnik-Rižner T, Zorko M, Peter-Katalinić J, Strupat K, Žakelj-Mavrič M. Carbonyl reducing 17beta-hydroxysteroid dehydrogenase from the filamentous fungus Cochliobolus lunatus. Advan exp med biol () str. 569-577.
  • 11. Lanišnik-Rižner T, Žakelj-Mavrič M, Plemenitaš A, Zorko M. Purification and characterization of 17 beta-hydroxysteroid dehydrogenase fromthe filamentous fungus Cochliobolus lunatus. J Steroid Biochem Mol Biol (1996) 59, 205-214.
  • 10. Stojan J, Pavlič M. The influence of an organosulfonate on the reaction between Ellman's reagent and thiocholine. J Anal Toxicol (1994) 18, 165-167.
  • 9. Stojan J, Pavlič M. Velocity of Ellman's reaction and its implication for kinetic studies in the milisecond time range. Neurochem Res (1992) 17, 1207-1210.
  • 8. Stojan J, Pavlič M. On the inhibition of cholinesterase by D-tubocurarine. Biochim Biophys Acta (1991) 1079, 96-102.
  • 7. Pavlič M, Alif M, Božič M, Stojan J. On the stability of some enzymes under various experimental conditions. Period Biol (1991) 93, 211-215.
  • 6. Zorko M, Stojan J, Pavlič M. Mechanism of action of alkanesulfonylcorides and quaternary ammonium ligands on acetylcholinesterase. Period Biol (1991) 93, 357.
  • 5. Stojan J, Pavlič M. The influence of medium on the stability of cholinesterases. Iugosl Physiol Pharmacol Acta (1988) 24, 305-311.
  • 4. Stojan J, Pavlič M. An interpretation of a non-linear dixon plot. Vestn Slov kem druš (1987) 34, 61-70.
  • 3. Stojan J. Fitting the kinetic equation for slow-binding ligand by microcomputer. Vestn Slov kem druš (1987) 34, 233-241.
  • 2. Zorko M, Pavlič M. Multiple binding of D-tubocurarine to acetylcholinesterease. Biochem Pharmacol (1986) 35, 2287-2296.
  • 1. Zorko M, Stojan J, Pavlič M. Influence of ionic strength on the interaction between D-tubocurarine and cholinesterases. Period Biol (1986) 88, 220-222.