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Marija Luic

Explore the profile of Marija Luic including associated specialties, affiliations and a list of published articles. Areas
Snapshot
Articles 21
Citations 159
Followers 0
Related Specialties
Biochemistry
Chemistry
Science
Top 10 Co-Authors
Agnieszka Bzowska
Zoran Stefanic
Ivana Lescic Asler
Marta Narczyk
Beata Wielgus-Kutrowska
Goran Mikleusevic
Branimir Bertosa
Nives Ivic
Dusica Vujaklija
Sasa Kazazic
Published In
FEBS J
Int J Biol Macromol
Acta Crystallogr D Biol Crystallogr
J Enzyme Inhib Med Chem
J Mol Biol
Affiliations
Soon will be listed here.
Recent Articles
1.
The pursuit of new alternative ways to eradicate Helicobacter pylori continues: Detailed characterization of interactions in the adenylosuccinate synthetase active site
Bubic A, Narczyk M, Petek A, Wojtys M, Maksymiuk W, Wielgus-Kutrowska B, et al.
Int J Biol Macromol . 2022 Dec; 226:37-50. PMID: 36470440
Purine nucleotide synthesis is realised only through the salvage pathway in pathogenic bacterium Helicobacter pylori. Therefore, the enzymes of this pathway, among them also the adenylosuccinate synthetase (AdSS), present potential...
2.
Interactions of 2,6-substituted purines with purine nucleoside phosphorylase from in solution and in the crystal, and the effects of these compounds on cell cultures of this bacterium
Narczyk M, Wojtys M, Asler I, Zinic B, Luic M, Jagusztyn-Krynicka E, et al.
J Enzyme Inhib Med Chem . 2022 Apr; 37(1):1083-1097. PMID: 35437103
represents a global health threat with around 50% of the world population infected. Due to the increasing number of antibiotic-resistant strains, new strategies for eradication of are needed. In this...
3.
A comprehensive method for determining cellular uptake of purine nucleoside phosphorylase and adenylosuccinate synthetase inhibitors by H. pylori
Wojtys M, Jazwiec R, Kazazic S, Asler I, Knezevic P, Aleksic Sabo V, et al.
Appl Microbiol Biotechnol . 2021 Sep; 105(20):7949-7967. PMID: 34562116
Due to the growing number of Helicobacter pylori strains resistant to currently available antibiotics, there is an urgent need to design new drugs utilizing different molecular mechanisms than those that...
4.
Crystallographic snapshots of ligand binding to hexameric purine nucleoside phosphorylase and kinetic studies give insight into the mechanism of catalysis
Stefanic Z, Narczyk M, Mikleusevic G, Kazazic S, Bzowska A, Luic M
Sci Rep . 2018 Oct; 8(1):15427. PMID: 30337572
Purine nucleoside phosphorylase (PNP) catalyses the cleavage of the glycosidic bond of purine nucleosides using phosphate instead of water as a second substrate. PNP from Escherichia coli is a homohexamer,...
5.
In the quest for new targets for pathogen eradication: the adenylosuccinate synthetase from the bacterium Helicobacter pylori
Bubic A, Mrnjavac N, Stuparevic I, Lyczek M, Wielgus-Kutrowska B, Bzowska A, et al.
J Enzyme Inhib Med Chem . 2018 Sep; 33(1):1405-1414. PMID: 30191734
Adenylosuccinate synthetase (AdSS) is an enzyme at regulatory point of purine metabolism. In pathogenic organisms which utilise only the purine salvage pathway, AdSS asserts itself as a promising drug target....
6.
Helicobacter pylori purine nucleoside phosphorylase shows new distribution patterns of open and closed active site conformations and unusual biochemical features
Narczyk M, Bertosa B, Papa L, Vukovic V, Asler I, Wielgus-Kutrowska B, et al.
FEBS J . 2018 Feb; 285(7):1305-1325. PMID: 29430816
Databases: The atomic coordinates and structure factors have been deposited in the Protein Data Bank: with accession codes 6F52 (HpPNPapo_1), 6F5A (HpPNPapo_2), 6F5I (HpPNPapo_3), 5LU0 (HpPNP_PO4), 6F4W (HpPNP_FA) and 6F4X...
7.
Crystal structure of dipeptidyl peptidase III from the human gut symbiont Bacteroides thetaiotaomicron
Sabljic I, Mestrovic N, Vukelic B, Macheroux P, Gruber K, Luic M, et al.
PLoS One . 2017 Nov; 12(11):e0187295. PMID: 29095893
Bacteroides thetaiotaomicron is a dominant member of the human intestinal microbiome. The genome of this anaerobe encodes more than 100 proteolytic enzymes, the majority of which have not been characterized....
8.
Structural characterization of purine nucleoside phosphorylase from human pathogen Helicobacter pylori
Stefanic Z, Mikleusevic G, Luic M, Bzowska A, Asler I
Int J Biol Macromol . 2017 Mar; 101:518-526. PMID: 28336275
Microaerophilic bacterium Helicobacer pylori is a well known human pathogen involved in the development of many diseases. Due to the evergrowing infection rate and increase of H. pylori antibiotic resistence,...
9.
Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor
Lalic J, Posavec Marjanovic M, Palazzo L, Perina D, Sabljic I, Zaja R, et al.
J Biol Chem . 2016 Sep; 291(44):23175-23187. PMID: 27634042
ADP-ribosylation is a post-translational modification that can alter the physical and chemical properties of target proteins and that controls many important cellular processes. Macrodomains are evolutionarily conserved structural domains that...
10.
New Insights into Active Site Conformation Dynamics of E. coli PNP Revealed by Combined H/D Exchange Approach and Molecular Dynamics Simulations
Kazazic S, Bertosa B, Luic M, Mikleusevic G, Tarnowski K, Dadlez M, et al.
J Am Soc Mass Spectrom . 2015 Sep; 27(1):73-82. PMID: 26337516
The biologically active form of purine nucleoside phosphorylase (PNP) from Escherichia coli (EC 2.4.2.1) is a homohexamer unit, assembled as a trimer of dimers. Upon binding of phosphate, neighboring monomers...