WorldCat Identities

Goličnik, Marko 1973-

Overview
Works: 67 works in 71 publications in 2 languages and 125 library holdings
Roles: Author, Editor, Thesis advisor, Other, Illustrator
Publication Timeline
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Most widely held works by Marko Goličnik
Izbrana poglavja iz biokemije 1 : gradivo za seminarje( Book )

2 editions published between 2010 and 2012 in Slovenian and held by 11 WorldCat member libraries worldwide

Book of abstracts by Slovensko biokemijsko društvo( Book )

2 editions published between 2009 and 2013 in English and held by 10 WorldCat member libraries worldwide

The 12th Meeting of the Slovenian Biochemical Society with International Participation in Bled, Slovenia, was organised by the Slovenian Biochemical Society together with the University of Ljubljana, Faculty of Medicine, Institute of Biochemistry. The Croatian Society of Biochemistry and Molecular Biology, Hungarian Biochemical Society and Serbian Biochemical Society joined us and participated at the meeting with the FEBS3+ session. This session was specially honoured by the presence of the Secretary General of the FEBS, Prof. Václav Pačes
Vaje iz biokemije 1 : laboratorijski praktikum( Book )

2 editions published between 2010 and 2012 in Slovenian and held by 10 WorldCat member libraries worldwide

Biokemija I by Tomaž Makovec( Book )

1 edition published in 2007 in Slovenian and held by 6 WorldCat member libraries worldwide

Temelji biokemije : laboratorijski praktikum : študijsko gradivo za študente medicine in dentalne medicine( Book )

1 edition published in 2016 in Slovenian and held by 6 WorldCat member libraries worldwide

Matematični problemi v biokemiji : primeri rešenih nalog s teoretičnim dodatkom : študijsko gradivo za študente medicine by Marko Goličnik( Book )

1 edition published in 2015 in Slovenian and held by 5 WorldCat member libraries worldwide

Sistemska biologija cirkadiane ure v jetrih miši : doktorsko delo = Systems biology of the circadian clock in mouse liver : doctoral thesis by Anja Korenčič( Book )

1 edition published in 2012 in Slovenian and held by 4 WorldCat member libraries worldwide

Mehanizem kooperativnih pojavov pri holinesterazah = Mechanisms of cooperative phenomena by cholinesterases : doktorsko delo by Marko Goličnik( Book )

1 edition published in 2002 in Slovenian and held by 4 WorldCat member libraries worldwide

Spoznajmo zgradbo in delovanje celice : biologija za gimnazije 1 by Peter Veranič( Book )

1 edition published in 2012 in Slovenian and held by 4 WorldCat member libraries worldwide

Temelji biokemije : več kot 800 testnih nalog izbirnega tipa by Marko Goličnik( Book )

1 edition published in 2009 in Slovenian and held by 3 WorldCat member libraries worldwide

A thermodynamic approach to exploration of physostigmine action mechanism on electric eel acetylcholinesterase by Marko Goličnik( )

2 editions published between 2003 and 2006 in English and held by 2 WorldCat member libraries worldwide

Metallic fluoride complexes as phosphate analogues for structural and mechanistic studies of phosphoryl group transfer enzymes by Marko Goličnik( )

1 edition published in 2010 in English and held by 2 WorldCat member libraries worldwide

There have been intensive efforts to try to understand the details of phosphoryl transfer reactions extending from nonenzymatic (or enzyme model) systems to the mechanisms of the enzyme catalysed reactions. As phosphate analogues, few metallic fluorides AlFx, BeFx and MgFx affect the activity of avariety of phosphoryl transfer enzymes, and it is accepted that these small inorganic complexes are useful chemical probes for structural and mechanistic studies in enzymology because they are able to mimic phosphoryl group in ground state (BeFx) as well as in transition state (AlFx, Mg-Fx). Al3+ and Be2+tend to form stable complexes with different fluoride anions (x=1 to 4) spontaneously in aqueous solution but Mg2+ does not. BeFx geometry is strictlytetrahedral resembling the phosphate ground state when bound to an acyl group of protein active site (phosphorylated acyl groups are unstable otherwise), or the Michaelis complex when BeFx concominantly with nucleoside diphosphate replaces gamma-phosphate group in nucleoside triphosphate sites. AlFx and MgFx are identified as enzymatic analogues of phosphoryl transition state where both are able to form different coordination geometries within theenzyme active sites: trigonal bipyramidal (AlF3 and MgF3- ) or octahedral (AlF4- or Mg-F42- ). The geometry and charge of MgF3- are the best suited to mimicking the trigonal planar PO3- moiety of phosphoryl transfer transition state but MgF3- does not, unlike aluminum and beryllium fluoride complexes, exists in solution and can be assembled and stabilized in suitable active siteonly. Therefore it is particularly interesting to characterize as a potentially highly accurate transition state analogue and may be the best reagent of choice for studying phosphoryl transfer reactions in future
Estimation of kinetic parameters for enzyme-Inhibition reaction models using direct time-dependent equations for reactant concentrations by Marko Goličnik( )

1 edition published in 2012 in English and held by 2 WorldCat member libraries worldwide

To facilitate the determination of a reaction type and its kinetics constants for reversible inhibitors of Michaelis-Mententype enzymes using progress-curveanalysis, I present here an explicit equation for direct curve fitting to full time-course data of inhibited enzyme-catalyzed reactions. Thisalgebraic expression involves certain elementary functions where their values are readily available using any standard nonlinear regression program. Hence this allows easy analysis of experimentally observed kinetics without any data conversion prior to fitting. Its implementation gives correct parameter estimates that are in very good agreement with results obtained using both the numerically integrated Michaelis-Menten rate equation or its exact closed-form solution which is expressed in terms of the Lambert W function
Progress-curve analysis through integrated rate equations and its use to study cholinesterase reaction dynamics by Marko Goličnik( )

1 edition published in 2014 in English and held by 1 WorldCat member library worldwide

Michaelis and Menten found the direct mathematical analysis of their studied enzyme-catalyzed reaction unrealistic 100 years ago, and hence, they avoided this problem by correct adaptation and analysis of the experiment, i.e., differentiation of the progress-curve data into rates. However, the most elegant and ideal simplification of the evaluation of kinetics parameters from progress curves can be performed when the algebraic integration of the rate equation results in an explicit mathematical equation that describes the dynamics of the model system of the reaction. Recently, it was demonstrated that such an alternative approach can be considered for enzymes that obey the generalized MichaelisMenten reaction dynamics, although its use is now still limited for cholinesterases, which show kinetics that deviate from saturation-like hyperbolic behavior at high concentrations of charged substrates. However, a mathematical approach is reviewed here that might provide an alternative to the decades-old problem of data analysis of cholinesterase-catalyzed reactions, through the more complex Webb integrated rate equation
Detection of phosphorylation states by intermolecular sensitization of lanthanide-peptide conjugates( )

1 edition published in 2012 in English and held by 1 WorldCat member library worldwide

The luminescence of a designed peptide equipped with a coordinatively-unsaturated lanthanide complex is modulated by the phosphorylation state of a serine residue in the sequence. While the phosphorylated state is weakly emissive, even in the presence of an external antenna, removal of the phosphate allows coordination of the sensitizer to the metal, yielding a highly emissive supramolecular complex
"Die Kinetik der Invertinwirkung" of L. Michaelis and M. L. Menten revisited after 100 years : closed-form solutions of genuine invertase-reaction dynamics by Marko Goličnik( )

1 edition published in 2013 in English and held by 1 WorldCat member library worldwide

On the Lambert W function and its utility in biochemical kinetics by Marko Goličnik( )

1 edition published in 2012 in English and held by 1 WorldCat member library worldwide

This article presents closed-form analytic solutions to three illustrative problems in biochemical kinetics that have usually been considered solvable only by various numerical methods. The problems solved concern two enzyme-catalyzed reaction systems that obey diversely modified Michaelis-Menten rate equations, and biomolecule surface binding that is limited by mass transport. These problems involve the solutions of transcendental equations that include products of variables and their logarithms. Such equations are solvable by the use of the Lambert W(x) function. Thus, these standard kinetics examples are solved in terms of W(x) to show the applicability of this commonly unknown function to the biochemicalcommunity. Hence, this review first of all describes the mathematical definition and properties of the W(x) function and its numerical evaluations, together with analytical approximations, and then it describes the use of the W(x) function in biochemical kinetics. Other applications of the function in various engineering sciences are also cited, although not described
Optimization of PON1 arylesterase activity measurement( )

1 edition published in 2016 in English and held by 1 WorldCat member library worldwide

Kinetics of ethopropazine binding to butyrylcholinesterase in the absence and presence of acetylthiocholine( )

1 edition published in 2004 in English and held by 1 WorldCat member library worldwide

 
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