TY  - JOUR
AU  - Petković-Benazzouz, Marija M.
AU  - Rakić, Aleksandra
AU  - Trišović, Nemanja
AU  - Zarić, Božidarka
AU  - Janjić, Goran
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7120
AB  - Coordination effects have been considered through the most common interactions in the crystal structures of fluoro compounds (C–H/F and F/F interactions). The supramolecular profile of these effects is based on quantum-chemical calculations for the assessment of the interaction strength and electrostatic potential maps, which provide a qualitative insight into the examined effect. Coordination of aliphatic fluorides leads to an increase of the negative potential of the F atoms, and, hence, an increase in the hydrogen-bonding acceptor ability (strengthening of C–H/F interactions) and a weakening of the F/F interactions, due to an increase in repulsive interactions between the F atoms. There is no significant change in the potential of the F atoms due to coordination of C6-aromatic fluorides, as in the case of aliphatic ones. This results in slight changes in the strengths of the C–H/F and F/F interactions (coupled with parallel interaction at large offsets, PILO), in a noticeable enhancement of stacking interactions, as well as in a significant enhancement of interactions involving the π-system (F/π and C–H/π interactions). It has also been shown that a decrease in the charge of the metal ions leads to a decrease in the negative potential of the F atom and also that the nature of the metal ion has a significant influence on the value of the potential of the F atoms.
PB  - American Chemical Society (ACS)
T2  - Crystal Growth and Design
T1  - Supramolecular Perspective of Coordination Effects on Fluorine Interactions
VL  - 21
VL  - 6142
IS  - 11
SP  - 6129
DO  - 10.1021/acs.cgd.1c00584
ER  - 

@article{
author = "Petković-Benazzouz, Marija M. and Rakić, Aleksandra and Trišović, Nemanja and Zarić, Božidarka and Janjić, Goran",
year = "2021",
abstract = "Coordination effects have been considered through the most common interactions in the crystal structures of fluoro compounds (C–H/F and F/F interactions). The supramolecular profile of these effects is based on quantum-chemical calculations for the assessment of the interaction strength and electrostatic potential maps, which provide a qualitative insight into the examined effect. Coordination of aliphatic fluorides leads to an increase of the negative potential of the F atoms, and, hence, an increase in the hydrogen-bonding acceptor ability (strengthening of C–H/F interactions) and a weakening of the F/F interactions, due to an increase in repulsive interactions between the F atoms. There is no significant change in the potential of the F atoms due to coordination of C6-aromatic fluorides, as in the case of aliphatic ones. This results in slight changes in the strengths of the C–H/F and F/F interactions (coupled with parallel interaction at large offsets, PILO), in a noticeable enhancement of stacking interactions, as well as in a significant enhancement of interactions involving the π-system (F/π and C–H/π interactions). It has also been shown that a decrease in the charge of the metal ions leads to a decrease in the negative potential of the F atom and also that the nature of the metal ion has a significant influence on the value of the potential of the F atoms.",
publisher = "American Chemical Society (ACS)",
journal = "Crystal Growth and Design",
title = "Supramolecular Perspective of Coordination Effects on Fluorine Interactions",
volume = "21, 6142",
number = "11",
pages = "6129",
doi = "10.1021/acs.cgd.1c00584"
}

Petković-Benazzouz, M. M., Rakić, A., Trišović, N., Zarić, B.,& Janjić, G.. (2021). Supramolecular Perspective of Coordination Effects on Fluorine Interactions. in Crystal Growth and Design
American Chemical Society (ACS)., 21(11), 6129.
https://doi.org/10.1021/acs.cgd.1c00584

Petković-Benazzouz MM, Rakić A, Trišović N, Zarić B, Janjić G. Supramolecular Perspective of Coordination Effects on Fluorine Interactions. in Crystal Growth and Design. 2021;21(11):6129.
doi:10.1021/acs.cgd.1c00584 .

Petković-Benazzouz, Marija M., Rakić, Aleksandra, Trišović, Nemanja, Zarić, Božidarka, Janjić, Goran, "Supramolecular Perspective of Coordination Effects on Fluorine Interactions" in Crystal Growth and Design, 21, no. 11 (2021):6129,
https://doi.org/10.1021/acs.cgd.1c00584 . .

TY  - JOUR
AU  - Bajić, Vladan
AU  - Misić, Nataša
AU  - Stanković, Ivana
AU  - Zarić, Božidarka
AU  - Perry, George
PY  - 2021
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4773
AB  - Does Alzheimer Disease show a decline in cognitive functions that relate to the awareness of external reality? In this paper, we will propose a perspective that patients with increasing symptoms of AD show a change in the awareness of subjective versus objective representative axis of reality thus consequently move to a more internal like perception of reality. This paradigm shift suggests that new insights into the dynamicity of the conscious representation of reality in the AD brain may give us new clues to the very early signs of memory and self-awareness impairment that originates from, in our view the microtubules. Dialog between Adso and William, in Umberto Eco’s The Name of the Rose, Third Day: Vespers. “But how does it happen,” I said with admiration, “that you were able to solve the mystery of the library looking at it from the outside, and you were unable to solve it when you were inside?” “Thus, God knows the world, because He conceived it in His mind, as if it was from the outside, before it was created, and we do not know its rule, because we live inside it, having found it already made.
PB  - SAGE Publications Ltd
T2  - Neuroscience Insights
T1  - Alzheimer’s and Consciousness: How Much Subjectivity Is Objective?
VL  - 16
DO  - 10.1177/26331055211033869
ER  - 

@article{
author = "Bajić, Vladan and Misić, Nataša and Stanković, Ivana and Zarić, Božidarka and Perry, George",
year = "2021",
abstract = "Does Alzheimer Disease show a decline in cognitive functions that relate to the awareness of external reality? In this paper, we will propose a perspective that patients with increasing symptoms of AD show a change in the awareness of subjective versus objective representative axis of reality thus consequently move to a more internal like perception of reality. This paradigm shift suggests that new insights into the dynamicity of the conscious representation of reality in the AD brain may give us new clues to the very early signs of memory and self-awareness impairment that originates from, in our view the microtubules. Dialog between Adso and William, in Umberto Eco’s The Name of the Rose, Third Day: Vespers. “But how does it happen,” I said with admiration, “that you were able to solve the mystery of the library looking at it from the outside, and you were unable to solve it when you were inside?” “Thus, God knows the world, because He conceived it in His mind, as if it was from the outside, before it was created, and we do not know its rule, because we live inside it, having found it already made.",
publisher = "SAGE Publications Ltd",
journal = "Neuroscience Insights",
title = "Alzheimer’s and Consciousness: How Much Subjectivity Is Objective?",
volume = "16",
doi = "10.1177/26331055211033869"
}

Bajić, V., Misić, N., Stanković, I., Zarić, B.,& Perry, G.. (2021). Alzheimer’s and Consciousness: How Much Subjectivity Is Objective?. in Neuroscience Insights
SAGE Publications Ltd., 16.
https://doi.org/10.1177/26331055211033869

Bajić V, Misić N, Stanković I, Zarić B, Perry G. Alzheimer’s and Consciousness: How Much Subjectivity Is Objective?. in Neuroscience Insights. 2021;16.
doi:10.1177/26331055211033869 .

Bajić, Vladan, Misić, Nataša, Stanković, Ivana, Zarić, Božidarka, Perry, George, "Alzheimer’s and Consciousness: How Much Subjectivity Is Objective?" in Neuroscience Insights, 16 (2021),
https://doi.org/10.1177/26331055211033869 . .

TY  - JOUR
AU  - Vujačić Nikezić, Ana V.
AU  - Janjić, Goran
AU  - Bondžić, Aleksandra M.
AU  - Zarić, Božidarka
AU  - Vasic-Anicijevic, Dragana D.
AU  - Momic, Tatjana G.
AU  - Vasić, Vesna M.
PY  - 2018
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2452
AB  - The present paper deals with investigation of the interaction between selected simple structure Au(iii) ([AuCl4](-), [AuCl2(dmso)(2)](+), [AuCl2(bipy)](+)) and Pt(ii) ([PtCl2(dmso)(2)]) complexes with Na/K-ATPase as the target enzyme, using an experimental and theoretical approach. Reaction stoichiometries and binding constants for these enzyme/complex systems were determined, while kinetic measurements were used in order to reveal the type of inhibition. Based on the results obtained by quantum mechanical calculations (electrostatic surface potential (ESP), volume and surface of the complexes) the nature of the investigated complexes was characterized. By using the solvent accessible surface area (SASA) applied on specific inhibitory sites (ion channel and intracellular domains) the nature of these sites was described. Docking studies were used to determine the theoretical probability of the non-covalent metal binding site positions. Inhibition studies implied that all the investigated complexes decreased the activity of the enzyme while the kinetic analysis indicated an uncompetitive mode of inhibition for the selected complexes. Docking results suggested that the main inhibitory site of all these complexes is located in the ion translocation pathway on the extracellular side in the E2P enzyme conformation, similar to the case of cardiac glycosides, specific Na/K-ATPase inhibitors. Also, based on our knowledge, the hydrolyzed forms of [AuCl4](-) and [PtCl2(dmso)(2)] complexes were investigated for the first time by theoretical calculations in this paper. Thereby, a new inhibitory site situated between the M2 and M4 helices was revealed. Binding in this site induces conformational changes in the enzyme domains and perturbs the E1-E2P conformational equilibrium, causing enzyme inhibition.
PB  - Royal Soc Chemistry, Cambridge
T2  - Metallomics
T1  - Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites
VL  - 10
IS  - 7
SP  - 1003
EP  - 1015
DO  - 10.1039/c8mt00111a
ER  - 

@article{
author = "Vujačić Nikezić, Ana V. and Janjić, Goran and Bondžić, Aleksandra M. and Zarić, Božidarka and Vasic-Anicijevic, Dragana D. and Momic, Tatjana G. and Vasić, Vesna M.",
year = "2018",
abstract = "The present paper deals with investigation of the interaction between selected simple structure Au(iii) ([AuCl4](-), [AuCl2(dmso)(2)](+), [AuCl2(bipy)](+)) and Pt(ii) ([PtCl2(dmso)(2)]) complexes with Na/K-ATPase as the target enzyme, using an experimental and theoretical approach. Reaction stoichiometries and binding constants for these enzyme/complex systems were determined, while kinetic measurements were used in order to reveal the type of inhibition. Based on the results obtained by quantum mechanical calculations (electrostatic surface potential (ESP), volume and surface of the complexes) the nature of the investigated complexes was characterized. By using the solvent accessible surface area (SASA) applied on specific inhibitory sites (ion channel and intracellular domains) the nature of these sites was described. Docking studies were used to determine the theoretical probability of the non-covalent metal binding site positions. Inhibition studies implied that all the investigated complexes decreased the activity of the enzyme while the kinetic analysis indicated an uncompetitive mode of inhibition for the selected complexes. Docking results suggested that the main inhibitory site of all these complexes is located in the ion translocation pathway on the extracellular side in the E2P enzyme conformation, similar to the case of cardiac glycosides, specific Na/K-ATPase inhibitors. Also, based on our knowledge, the hydrolyzed forms of [AuCl4](-) and [PtCl2(dmso)(2)] complexes were investigated for the first time by theoretical calculations in this paper. Thereby, a new inhibitory site situated between the M2 and M4 helices was revealed. Binding in this site induces conformational changes in the enzyme domains and perturbs the E1-E2P conformational equilibrium, causing enzyme inhibition.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Metallomics",
title = "Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites",
volume = "10",
number = "7",
pages = "1003-1015",
doi = "10.1039/c8mt00111a"
}

Vujačić Nikezić, A. V., Janjić, G., Bondžić, A. M., Zarić, B., Vasic-Anicijevic, D. D., Momic, T. G.,& Vasić, V. M.. (2018). Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites. in Metallomics
Royal Soc Chemistry, Cambridge., 10(7), 1003-1015.
https://doi.org/10.1039/c8mt00111a

Vujačić Nikezić AV, Janjić G, Bondžić AM, Zarić B, Vasic-Anicijevic DD, Momic TG, Vasić VM. Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites. in Metallomics. 2018;10(7):1003-1015.
doi:10.1039/c8mt00111a .

Vujačić Nikezić, Ana V., Janjić, Goran, Bondžić, Aleksandra M., Zarić, Božidarka, Vasic-Anicijevic, Dragana D., Momic, Tatjana G., Vasić, Vesna M., "Interaction of Au(iii) and Pt(ii) complexes with Na/K-ATPase: experimental and theoretical study of reaction stoichiometry and binding sites" in Metallomics, 10, no. 7 (2018):1003-1015,
https://doi.org/10.1039/c8mt00111a . .

TY  - JOUR
AU  - Bondžić, Aleksandra M.
AU  - Čolović, Mirjana B.
AU  - Janjić, Goran
AU  - Zarić, Božidarka
AU  - Petrović, Sandra
AU  - Krstic, Danijela Z.
AU  - Marzo, Tiziano
AU  - Messori, Luigi
AU  - Vasić, Vesna M.
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2143
AB  - The in vitro effects of oxo-bridged binuclear gold(III) complexes, i.e., [(bipy2Me)(2)Au-2(mu-O)(2)][PF6](2) (Auoxo6), Au-2[(bipydmb-H)(2)(mu-O)][PF6] (Au(2)bipyC) and [Au-2(phen(2Me))(2)(mu-O)(2)](PF6)(2) (Au(2)phen) on Na/K-ATPase, purified from the porcine cerebral cortex, were investigated. All three studied gold complexes inhibited the enzyme activity in a concentration-dependent manner achieving IC50 values in the low micromolar range. Kinetic analysis suggested an uncompetitive mode of inhibition for Auoxo6 and Au(2)bipyC, and a mixed type one for Au(2)phen. Docking studies indicated that the inhibitory actions of all tested complexes are related to E2-P enzyme conformation binding to ion channel and intracellular part between N and P sub-domain. In addition, Au(2)phen was able to inhibit the enzyme by interacting with its extracellular part as well. Toxic effects of the gold(III) complexes were evaluated in vitro by following lactate dehydrogenase activity in rat brain synaptosomes and incidence of micronuclei and cytokinesis-block proliferation index in cultivated human lymphocytes. All investigated complexes turned out to induce cytogenetic damage consisting of a significant decrease in cell proliferation and an increase in micronuclei in a dose-dependent manner. On the other hand, lactate dehydrogenase activity, an indicator of membrane integrity/viability, was not affected by Auoxo6 and Au(2)bipyC, while Au(2)phen slightly modified its activity.
PB  - Springer, New York
T2  - Journal of Biological Inorganic Chemistry
T1  - The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach
VL  - 22
IS  - 6
SP  - 819
EP  - 832
DO  - 10.1007/s00775-017-1460-5
ER  - 

@article{
author = "Bondžić, Aleksandra M. and Čolović, Mirjana B. and Janjić, Goran and Zarić, Božidarka and Petrović, Sandra and Krstic, Danijela Z. and Marzo, Tiziano and Messori, Luigi and Vasić, Vesna M.",
year = "2017",
abstract = "The in vitro effects of oxo-bridged binuclear gold(III) complexes, i.e., [(bipy2Me)(2)Au-2(mu-O)(2)][PF6](2) (Auoxo6), Au-2[(bipydmb-H)(2)(mu-O)][PF6] (Au(2)bipyC) and [Au-2(phen(2Me))(2)(mu-O)(2)](PF6)(2) (Au(2)phen) on Na/K-ATPase, purified from the porcine cerebral cortex, were investigated. All three studied gold complexes inhibited the enzyme activity in a concentration-dependent manner achieving IC50 values in the low micromolar range. Kinetic analysis suggested an uncompetitive mode of inhibition for Auoxo6 and Au(2)bipyC, and a mixed type one for Au(2)phen. Docking studies indicated that the inhibitory actions of all tested complexes are related to E2-P enzyme conformation binding to ion channel and intracellular part between N and P sub-domain. In addition, Au(2)phen was able to inhibit the enzyme by interacting with its extracellular part as well. Toxic effects of the gold(III) complexes were evaluated in vitro by following lactate dehydrogenase activity in rat brain synaptosomes and incidence of micronuclei and cytokinesis-block proliferation index in cultivated human lymphocytes. All investigated complexes turned out to induce cytogenetic damage consisting of a significant decrease in cell proliferation and an increase in micronuclei in a dose-dependent manner. On the other hand, lactate dehydrogenase activity, an indicator of membrane integrity/viability, was not affected by Auoxo6 and Au(2)bipyC, while Au(2)phen slightly modified its activity.",
publisher = "Springer, New York",
journal = "Journal of Biological Inorganic Chemistry",
title = "The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach",
volume = "22",
number = "6",
pages = "819-832",
doi = "10.1007/s00775-017-1460-5"
}

Bondžić, A. M., Čolović, M. B., Janjić, G., Zarić, B., Petrović, S., Krstic, D. Z., Marzo, T., Messori, L.,& Vasić, V. M.. (2017). The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach. in Journal of Biological Inorganic Chemistry
Springer, New York., 22(6), 819-832.
https://doi.org/10.1007/s00775-017-1460-5

Bondžić AM, Čolović MB, Janjić G, Zarić B, Petrović S, Krstic DZ, Marzo T, Messori L, Vasić VM. The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach. in Journal of Biological Inorganic Chemistry. 2017;22(6):819-832.
doi:10.1007/s00775-017-1460-5 .

Bondžić, Aleksandra M., Čolović, Mirjana B., Janjić, Goran, Zarić, Božidarka, Petrović, Sandra, Krstic, Danijela Z., Marzo, Tiziano, Messori, Luigi, Vasić, Vesna M., "The influence of oxo-bridged binuclear gold(III) complexes on Na/K-ATPase activity: a joint experimental and theoretical approach" in Journal of Biological Inorganic Chemistry, 22, no. 6 (2017):819-832,
https://doi.org/10.1007/s00775-017-1460-5 . .

TY  - CHAP
AU  - Obradović, Milan
AU  - Stanimirović, Julijana
AU  - Panić, Anastasija
AU  - Zarić, Božidarka
AU  - Isenović, Esma R.
PY  - 2016
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3364
AB  - The Na+/K+-ATPase is a universally expressed
membrane protein responsible for maintaining
the low intracellular Na+ and high intracellular
K+ concentrations required for multitude of cellular functions. Besides, the Na+ /K+-ATPase helps maintaining resting potential, import of amino acids, glucose, and other nutrients into cells and regulates cellular volume. Increasing our understanding of the molecular mechanisms determining the regulation of
Na+/K+ -ATPase may help develop new strategies
for the treatment of f cardiovascular diseases
PB  - Springer Science and Business Media LLC
T2  - Encyclopedia of Signaling Molecules
T1  - Na+/K+-ATPase
SP  - 2038
EP  - 2043
DO  - 10.1007/978-1-4614-6438-9_101543-1
ER  - 

@inbook{
author = "Obradović, Milan and Stanimirović, Julijana and Panić, Anastasija and Zarić, Božidarka and Isenović, Esma R.",
year = "2016",
abstract = "The Na+/K+-ATPase is a universally expressed
membrane protein responsible for maintaining
the low intracellular Na+ and high intracellular
K+ concentrations required for multitude of cellular functions. Besides, the Na+ /K+-ATPase helps maintaining resting potential, import of amino acids, glucose, and other nutrients into cells and regulates cellular volume. Increasing our understanding of the molecular mechanisms determining the regulation of
Na+/K+ -ATPase may help develop new strategies
for the treatment of f cardiovascular diseases",
publisher = "Springer Science and Business Media LLC",
journal = "Encyclopedia of Signaling Molecules",
booktitle = "Na+/K+-ATPase",
pages = "2038-2043",
doi = "10.1007/978-1-4614-6438-9_101543-1"
}

Obradović, M., Stanimirović, J., Panić, A., Zarić, B.,& Isenović, E. R.. (2016). Na+/K+-ATPase. in Encyclopedia of Signaling Molecules
Springer Science and Business Media LLC., 2038-2043.
https://doi.org/10.1007/978-1-4614-6438-9_101543-1

Obradović M, Stanimirović J, Panić A, Zarić B, Isenović ER. Na+/K+-ATPase. in Encyclopedia of Signaling Molecules. 2016;:2038-2043.
doi:10.1007/978-1-4614-6438-9_101543-1 .

Obradović, Milan, Stanimirović, Julijana, Panić, Anastasija, Zarić, Božidarka, Isenović, Esma R., "Na+/K+-ATPase" in Encyclopedia of Signaling Molecules (2016):2038-2043,
https://doi.org/10.1007/978-1-4614-6438-9_101543-1 . .

TY  - JOUR
AU  - Zarić, Božidarka
AU  - Petrović, Srđan
AU  - Bjekic, Milan
AU  - Rajic, Ivana
AU  - Popović, Aleksandar R.
AU  - Đorđević, Dragana
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1475
AB  - Analysis of volatile organic compounds (VOCs) in human breath can provide information about the current physiological state of an individual, such as clinical conditions and exposure to exogenous pollutants. The blood-borne VOCs present in exhaled breath offer the possibility of exploring physiological and pathological processes in a noninvasive way. However, the field of exhaled breath analysis is still in its infancy. We undertook this study in order to define inter-individual variation and common compounds in breath VOCs of 48 young human volunteers. Alveolar breath samples were analyzed by automated thermal desorption, gas chromatography with flame ionization detector (FID) and electron capture detector (ECD) using SUPELCO standards with 66 compounds. Predominant compounds in the alveolar breath of analyzed subjects are ethylbenzene, 1-ethyl-4-methylbenzene, 1,2,4-trimethylbenzene and 1,3,5-trimethylbenzene (over 50% of the subjects). Isopropyl alcohol, propylene, acetone, ethanol were found as well. We detected substituted compounds in exhaled breath.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of Biological Sciences
T1  - Analysis of human exhaled breath in a population of young volunteers
VL  - 66
IS  - 4
SP  - 1529
EP  - 1538
DO  - 10.2298/ABS1404529Z
ER  - 

@article{
author = "Zarić, Božidarka and Petrović, Srđan and Bjekic, Milan and Rajic, Ivana and Popović, Aleksandar R. and Đorđević, Dragana",
year = "2014",
abstract = "Analysis of volatile organic compounds (VOCs) in human breath can provide information about the current physiological state of an individual, such as clinical conditions and exposure to exogenous pollutants. The blood-borne VOCs present in exhaled breath offer the possibility of exploring physiological and pathological processes in a noninvasive way. However, the field of exhaled breath analysis is still in its infancy. We undertook this study in order to define inter-individual variation and common compounds in breath VOCs of 48 young human volunteers. Alveolar breath samples were analyzed by automated thermal desorption, gas chromatography with flame ionization detector (FID) and electron capture detector (ECD) using SUPELCO standards with 66 compounds. Predominant compounds in the alveolar breath of analyzed subjects are ethylbenzene, 1-ethyl-4-methylbenzene, 1,2,4-trimethylbenzene and 1,3,5-trimethylbenzene (over 50% of the subjects). Isopropyl alcohol, propylene, acetone, ethanol were found as well. We detected substituted compounds in exhaled breath.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of Biological Sciences",
title = "Analysis of human exhaled breath in a population of young volunteers",
volume = "66",
number = "4",
pages = "1529-1538",
doi = "10.2298/ABS1404529Z"
}

Zarić, B., Petrović, S., Bjekic, M., Rajic, I., Popović, A. R.,& Đorđević, D.. (2014). Analysis of human exhaled breath in a population of young volunteers. in Archives of Biological Sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 66(4), 1529-1538.
https://doi.org/10.2298/ABS1404529Z

Zarić B, Petrović S, Bjekic M, Rajic I, Popović AR, Đorđević D. Analysis of human exhaled breath in a population of young volunteers. in Archives of Biological Sciences. 2014;66(4):1529-1538.
doi:10.2298/ABS1404529Z .

Zarić, Božidarka, Petrović, Srđan, Bjekic, Milan, Rajic, Ivana, Popović, Aleksandar R., Đorđević, Dragana, "Analysis of human exhaled breath in a population of young volunteers" in Archives of Biological Sciences, 66, no. 4 (2014):1529-1538,
https://doi.org/10.2298/ABS1404529Z . .

TY  - JOUR
AU  - Zarić, Božidarka
AU  - Bukorović, Milica
AU  - Stojanović, Srđan
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1210
AB  - The Sm and Sm-like (LSm) proteins are a widespread protein family with members in all kingdoms of life. Sm proteins form complexes engaging in various RNA-processing events. Sm proteins do form and act as oligomeric assemblies whose characteristic is their exceptional stability. This study compares strong and weak hydrogen bonds in the interior of monomers and at interfaces of Sm/LSm proteins in order to better understand the stability of oligomers. According to our results, the stability of oligomeric assemblies is achieved by CH center dot center dot center dot O, NH center dot center dot center dot O and CH center dot center dot center dot N interactions including, NH center dot center dot center dot N, OH center dot center dot center dot O, XH center dot center dot center dot pi interactions present in small percentages. Intrachain hydrogen bonds behave in respect to geometry, distances and angles, like interchain hydrogen bonds. It is also shown that amino acids Arg and Lys participate significantly as donors or acceptors in some of the strong or weak interactions at interfaces to a higher extent than in the monomers. There is a trend for most polar amino acids to cross into more solvent exposed position in interfaces, which is not the case for nonpolar or charged amino acids. There is no exclusive preference for particular secondary structure both for intrachains and for interfaces.
PB  - Inst Materials Physics, Bucharest
T2  - Digest Journal of Nanomaterials and Biostructures
T1  - Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction
VL  - 8
IS  - 2
SP  - 639
EP  - 654
UR  - https://hdl.handle.net/21.15107/rcub_cer_1210
ER  - 

@article{
author = "Zarić, Božidarka and Bukorović, Milica and Stojanović, Srđan",
year = "2013",
abstract = "The Sm and Sm-like (LSm) proteins are a widespread protein family with members in all kingdoms of life. Sm proteins form complexes engaging in various RNA-processing events. Sm proteins do form and act as oligomeric assemblies whose characteristic is their exceptional stability. This study compares strong and weak hydrogen bonds in the interior of monomers and at interfaces of Sm/LSm proteins in order to better understand the stability of oligomers. According to our results, the stability of oligomeric assemblies is achieved by CH center dot center dot center dot O, NH center dot center dot center dot O and CH center dot center dot center dot N interactions including, NH center dot center dot center dot N, OH center dot center dot center dot O, XH center dot center dot center dot pi interactions present in small percentages. Intrachain hydrogen bonds behave in respect to geometry, distances and angles, like interchain hydrogen bonds. It is also shown that amino acids Arg and Lys participate significantly as donors or acceptors in some of the strong or weak interactions at interfaces to a higher extent than in the monomers. There is a trend for most polar amino acids to cross into more solvent exposed position in interfaces, which is not the case for nonpolar or charged amino acids. There is no exclusive preference for particular secondary structure both for intrachains and for interfaces.",
publisher = "Inst Materials Physics, Bucharest",
journal = "Digest Journal of Nanomaterials and Biostructures",
title = "Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction",
volume = "8",
number = "2",
pages = "639-654",
url = "https://hdl.handle.net/21.15107/rcub_cer_1210"
}

Zarić, B., Bukorović, M.,& Stojanović, S.. (2013). Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction. in Digest Journal of Nanomaterials and Biostructures
Inst Materials Physics, Bucharest., 8(2), 639-654.
https://hdl.handle.net/21.15107/rcub_cer_1210

Zarić B, Bukorović M, Stojanović S. Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction. in Digest Journal of Nanomaterials and Biostructures. 2013;8(2):639-654.
https://hdl.handle.net/21.15107/rcub_cer_1210 .

Zarić, Božidarka, Bukorović, Milica, Stojanović, Srđan, "Strong and weak hydrogen bonds in sm/lsm oligomeric assemblies: a comparison of intra- and interchain interaction" in Digest Journal of Nanomaterials and Biostructures, 8, no. 2 (2013):639-654,
https://hdl.handle.net/21.15107/rcub_cer_1210 .

TY  - JOUR
AU  - Adžić, Miroslav
AU  - Nićiforović, Ana
AU  - Zarić, Božidarka
AU  - Nešković-Konstantinović, Zora
AU  - Spasić, Snežana
AU  - Jones, David
AU  - Radojčić, Marija
PY  - 2013
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3945
AB  - To compare the effects of ionising radiation on leukocytes from breast cancer patients and healthy subjects ex vivo, the level of NF-κB and the antioxidant enzymes manganese-containing superoxide dismutase (Mn-SOD), copper/zinc-containing superoxide dismutase (CuZn-SOD) and catalase (CAT) in combination with flow cytometric analysis of CD4+ lymphocytes was performed. The level of Mn-SOD protein was significantly increased in the breast cancer study group both before (P < 0.001) and after (P < 0.001) irradiation when compared with healthy subjects. Measurements in parallel indicated that the level of CAT protein was significantly higher in the breast cancer study group after irradiation (2 Gy [P < 0.001] and 9 Gy [P < 0.05]) when compared with healthy subjects. Although the initial number of lymphocytes in the blood of breast cancer patients was not different from healthy subjects, the percentage of apoptotic CD4+ cells was significantly (P < 0.001) lower both before and after irradiation indicating that cell culture conditions induced radioresistance of CD4+ cells in the blood of breast cancer patients. The data presented in this current study indicate that brief ex vivo culture of peripheral blood leukocytes potentiates oxidative stress imposed by a breast cancer tumour.
PB  - Taylor & Francis
T2  - Redox Report
T1  - Cell culture conditions potentiate differences in the response to ionising radiation of peripheral blood leukocytes isolated from breast cancer patients and healthy subjects
VL  - 13
IS  - 1
SP  - 17
EP  - 22
DO  - 10.1179/135100008X259088
ER  - 

@article{
author = "Adžić, Miroslav and Nićiforović, Ana and Zarić, Božidarka and Nešković-Konstantinović, Zora and Spasić, Snežana and Jones, David and Radojčić, Marija",
year = "2013",
abstract = "To compare the effects of ionising radiation on leukocytes from breast cancer patients and healthy subjects ex vivo, the level of NF-κB and the antioxidant enzymes manganese-containing superoxide dismutase (Mn-SOD), copper/zinc-containing superoxide dismutase (CuZn-SOD) and catalase (CAT) in combination with flow cytometric analysis of CD4+ lymphocytes was performed. The level of Mn-SOD protein was significantly increased in the breast cancer study group both before (P < 0.001) and after (P < 0.001) irradiation when compared with healthy subjects. Measurements in parallel indicated that the level of CAT protein was significantly higher in the breast cancer study group after irradiation (2 Gy [P < 0.001] and 9 Gy [P < 0.05]) when compared with healthy subjects. Although the initial number of lymphocytes in the blood of breast cancer patients was not different from healthy subjects, the percentage of apoptotic CD4+ cells was significantly (P < 0.001) lower both before and after irradiation indicating that cell culture conditions induced radioresistance of CD4+ cells in the blood of breast cancer patients. The data presented in this current study indicate that brief ex vivo culture of peripheral blood leukocytes potentiates oxidative stress imposed by a breast cancer tumour.",
publisher = "Taylor & Francis",
journal = "Redox Report",
title = "Cell culture conditions potentiate differences in the response to ionising radiation of peripheral blood leukocytes isolated from breast cancer patients and healthy subjects",
volume = "13",
number = "1",
pages = "17-22",
doi = "10.1179/135100008X259088"
}

Adžić, M., Nićiforović, A., Zarić, B., Nešković-Konstantinović, Z., Spasić, S., Jones, D.,& Radojčić, M.. (2013). Cell culture conditions potentiate differences in the response to ionising radiation of peripheral blood leukocytes isolated from breast cancer patients and healthy subjects. in Redox Report
Taylor & Francis., 13(1), 17-22.
https://doi.org/10.1179/135100008X259088

Adžić M, Nićiforović A, Zarić B, Nešković-Konstantinović Z, Spasić S, Jones D, Radojčić M. Cell culture conditions potentiate differences in the response to ionising radiation of peripheral blood leukocytes isolated from breast cancer patients and healthy subjects. in Redox Report. 2013;13(1):17-22.
doi:10.1179/135100008X259088 .

Adžić, Miroslav, Nićiforović, Ana, Zarić, Božidarka, Nešković-Konstantinović, Zora, Spasić, Snežana, Jones, David, Radojčić, Marija, "Cell culture conditions potentiate differences in the response to ionising radiation of peripheral blood leukocytes isolated from breast cancer patients and healthy subjects" in Redox Report, 13, no. 1 (2013):17-22,
https://doi.org/10.1179/135100008X259088 . .

TY  - JOUR
AU  - Stojanović, Srđan
AU  - Isenovic, Esma R.
AU  - Zarić, Božidarka
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1099
AB  - In this study we have described the non-canonical interactions between the porphyrin ring and the protein part of porphyrin-containing proteins to better understand their stabilizing role. The analysis reported in this study shows that the predominant type of non-canonical interactions at porphyrins are CH center dot center dot center dot O and CH center dot center dot center dot N interactions, with a small percentage of CH center dot center dot center dot pi and non-canonical interactions involving sulfur atoms. The majority of non-canonical interactions are formed from side-chains of charged and polar amino acids, whereas backbone groups are not frequently involved. The main-chain non-canonical interactions might be slightly more linear than the side-chain interactions, and they have somewhat shorter median distances. The analysis, performed in this study, shows that about 44% of the total interactions in the dataset are involved in the formation of multiple (furcated) non-canonical interactions. The high number of porphyrin-water interactions show importance of the inclusion of solvent in protein-ligand interaction studies. Furthermore, in the present study we have observed that stabilization centers are composed predominantly from nonpolar amino acid residues. Amino acids deployed in the environment of porphyrin rings are deposited in helices and coils. The results from this study might be used for structure-based porphyrin protein prediction and as scaffolds for future porphyrin-containing protein design.
PB  - Springer Wien, Wien
T2  - Amino Acids
T1  - Non-canonical interactions of porphyrins in porphyrin-containing proteins
VL  - 43
IS  - 4
SP  - 1535
EP  - 1546
DO  - 10.1007/s00726-012-1228-8
ER  - 

@article{
author = "Stojanović, Srđan and Isenovic, Esma R. and Zarić, Božidarka",
year = "2012",
abstract = "In this study we have described the non-canonical interactions between the porphyrin ring and the protein part of porphyrin-containing proteins to better understand their stabilizing role. The analysis reported in this study shows that the predominant type of non-canonical interactions at porphyrins are CH center dot center dot center dot O and CH center dot center dot center dot N interactions, with a small percentage of CH center dot center dot center dot pi and non-canonical interactions involving sulfur atoms. The majority of non-canonical interactions are formed from side-chains of charged and polar amino acids, whereas backbone groups are not frequently involved. The main-chain non-canonical interactions might be slightly more linear than the side-chain interactions, and they have somewhat shorter median distances. The analysis, performed in this study, shows that about 44% of the total interactions in the dataset are involved in the formation of multiple (furcated) non-canonical interactions. The high number of porphyrin-water interactions show importance of the inclusion of solvent in protein-ligand interaction studies. Furthermore, in the present study we have observed that stabilization centers are composed predominantly from nonpolar amino acid residues. Amino acids deployed in the environment of porphyrin rings are deposited in helices and coils. The results from this study might be used for structure-based porphyrin protein prediction and as scaffolds for future porphyrin-containing protein design.",
publisher = "Springer Wien, Wien",
journal = "Amino Acids",
title = "Non-canonical interactions of porphyrins in porphyrin-containing proteins",
volume = "43",
number = "4",
pages = "1535-1546",
doi = "10.1007/s00726-012-1228-8"
}

Stojanović, S., Isenovic, E. R.,& Zarić, B.. (2012). Non-canonical interactions of porphyrins in porphyrin-containing proteins. in Amino Acids
Springer Wien, Wien., 43(4), 1535-1546.
https://doi.org/10.1007/s00726-012-1228-8

Stojanović S, Isenovic ER, Zarić B. Non-canonical interactions of porphyrins in porphyrin-containing proteins. in Amino Acids. 2012;43(4):1535-1546.
doi:10.1007/s00726-012-1228-8 .

Stojanović, Srđan, Isenovic, Esma R., Zarić, Božidarka, "Non-canonical interactions of porphyrins in porphyrin-containing proteins" in Amino Acids, 43, no. 4 (2012):1535-1546,
https://doi.org/10.1007/s00726-012-1228-8 . .

TY  - CHAP
AU  - Sudar, Emina
AU  - Soskić, Sanja
AU  - Zarić, Božidarka
AU  - Rašić-Milutinović, Zorica
AU  - Smiljanić, Katarina
AU  - Radak, Đorđe
AU  - Mikhailidis, Dimitri
AU  - Rizzo, Manfredi
AU  - Isenović, Esma
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4379
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4380
AB  - Cardiovascular disease (CVD) is common cause of death in humans and its major underlying pathology is atherosclerosis. Atherosclerosis is a chronic inflammatory disease that predisposes to coronary artery disease (CAD), stroke and peripheral arterial disease, responsible for most of the cardiovascular morbidity and mortality. This inflammatory process, triggered by the presence of lipids in the vascular wall, and encompasses a complex interaction among inflammatory cells, vascular elements, and lipoproteins through the expression of several adhesion molecules and cytokines. Obesity is a risk factor for CVD but this association is not fully understood. Altered levels of obesity related peptides such as ghrelin may play an important role in this pathophysiology. Recent evidence indicates that ghrelin features several cardiovascular activities, including increased myocardial contractility, vasodilatation and protection from myocardial infarction. Recent data demonstrate that ghrelin can influence important key events in atherogenesis and thus they may play a role in atherosclerosis. In this review we present the latest data from recent animal and clinical studies which focus on a novel approach to ghrelin as a potential therapeutic agent in the treatment of a complex disease like atherosclerosis. Thus, ghrelin may become a new therapeutic target for the treatment of CVD. Further studies are necessary to investigate the potential mechanisms involved in the effects of ghrelin on the cardiovascular system.
PB  - New York : Nova Science Publishers Inc.
T2  - Ghrelin: Production, Action Mechanisms and Physiological Effects
T1  - Ghrelin, obesity and atherosclerosis
SP  - 111
EP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3920
ER  - 

@inbook{
author = "Sudar, Emina and Soskić, Sanja and Zarić, Božidarka and Rašić-Milutinović, Zorica and Smiljanić, Katarina and Radak, Đorđe and Mikhailidis, Dimitri and Rizzo, Manfredi and Isenović, Esma",
year = "2012",
abstract = "Cardiovascular disease (CVD) is common cause of death in humans and its major underlying pathology is atherosclerosis. Atherosclerosis is a chronic inflammatory disease that predisposes to coronary artery disease (CAD), stroke and peripheral arterial disease, responsible for most of the cardiovascular morbidity and mortality. This inflammatory process, triggered by the presence of lipids in the vascular wall, and encompasses a complex interaction among inflammatory cells, vascular elements, and lipoproteins through the expression of several adhesion molecules and cytokines. Obesity is a risk factor for CVD but this association is not fully understood. Altered levels of obesity related peptides such as ghrelin may play an important role in this pathophysiology. Recent evidence indicates that ghrelin features several cardiovascular activities, including increased myocardial contractility, vasodilatation and protection from myocardial infarction. Recent data demonstrate that ghrelin can influence important key events in atherogenesis and thus they may play a role in atherosclerosis. In this review we present the latest data from recent animal and clinical studies which focus on a novel approach to ghrelin as a potential therapeutic agent in the treatment of a complex disease like atherosclerosis. Thus, ghrelin may become a new therapeutic target for the treatment of CVD. Further studies are necessary to investigate the potential mechanisms involved in the effects of ghrelin on the cardiovascular system.",
publisher = "New York : Nova Science Publishers Inc.",
journal = "Ghrelin: Production, Action Mechanisms and Physiological Effects",
booktitle = "Ghrelin, obesity and atherosclerosis",
pages = "111-126",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3920"
}

Sudar, E., Soskić, S., Zarić, B., Rašić-Milutinović, Z., Smiljanić, K., Radak, Đ., Mikhailidis, D., Rizzo, M.,& Isenović, E.. (2012). Ghrelin, obesity and atherosclerosis. in Ghrelin: Production, Action Mechanisms and Physiological Effects
New York : Nova Science Publishers Inc.., 111-126.
https://hdl.handle.net/21.15107/rcub_cherry_3920

Sudar E, Soskić S, Zarić B, Rašić-Milutinović Z, Smiljanić K, Radak Đ, Mikhailidis D, Rizzo M, Isenović E. Ghrelin, obesity and atherosclerosis. in Ghrelin: Production, Action Mechanisms and Physiological Effects. 2012;:111-126.
https://hdl.handle.net/21.15107/rcub_cherry_3920 .

Sudar, Emina, Soskić, Sanja, Zarić, Božidarka, Rašić-Milutinović, Zorica, Smiljanić, Katarina, Radak, Đorđe, Mikhailidis, Dimitri, Rizzo, Manfredi, Isenović, Esma, "Ghrelin, obesity and atherosclerosis" in Ghrelin: Production, Action Mechanisms and Physiological Effects (2012):111-126,
https://hdl.handle.net/21.15107/rcub_cherry_3920 .

TY  - CHAP
AU  - Sudar, Emina
AU  - Soskić, Sanja
AU  - Zarić, Božidarka
AU  - Rašić-Milutinović, Zorica
AU  - Smiljanić, Katarina
AU  - Radak, Đorđe
AU  - Mikhailidis, Dimitri
AU  - Rizzo, Manfredi
AU  - Isenović, Esma
PY  - 2012
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/4379
AB  - Cardiovascular disease (CVD) is common cause of death in humans and its major underlying pathology is atherosclerosis. Atherosclerosis is a chronic inflammatory disease that predisposes to coronary artery disease (CAD), stroke and peripheral arterial disease, responsible for most of the cardiovascular morbidity and mortality. This inflammatory process, triggered by the presence of lipids in the vascular wall, and encompasses a complex interaction among inflammatory cells, vascular elements, and lipoproteins through the expression of several adhesion molecules and cytokines. Obesity is a risk factor for CVD but this association is not fully understood. Altered levels of obesity related peptides such as ghrelin may play an important role in this pathophysiology. Recent evidence indicates that ghrelin features several cardiovascular activities, including increased myocardial contractility, vasodilatation and protection from myocardial infarction. Recent data demonstrate that ghrelin can influence important key events in atherogenesis and thus they may play a role in atherosclerosis. In this review we present the latest data from recent animal and clinical studies which focus on a novel approach to ghrelin as a potential therapeutic agent in the treatment of a complex disease like atherosclerosis. Thus, ghrelin may become a new therapeutic target for the treatment of CVD. Further studies are necessary to investigate the potential mechanisms involved in the effects of ghrelin on the cardiovascular system.
PB  - New York : Nova Science Publishers Inc.
T2  - Ghrelin: Production, Action Mechanisms and Physiological Effects
T1  - Ghrelin, obesity and atherosclerosis
SP  - 111
EP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3920
ER  - 

@inbook{
author = "Sudar, Emina and Soskić, Sanja and Zarić, Božidarka and Rašić-Milutinović, Zorica and Smiljanić, Katarina and Radak, Đorđe and Mikhailidis, Dimitri and Rizzo, Manfredi and Isenović, Esma",
year = "2012",
abstract = "Cardiovascular disease (CVD) is common cause of death in humans and its major underlying pathology is atherosclerosis. Atherosclerosis is a chronic inflammatory disease that predisposes to coronary artery disease (CAD), stroke and peripheral arterial disease, responsible for most of the cardiovascular morbidity and mortality. This inflammatory process, triggered by the presence of lipids in the vascular wall, and encompasses a complex interaction among inflammatory cells, vascular elements, and lipoproteins through the expression of several adhesion molecules and cytokines. Obesity is a risk factor for CVD but this association is not fully understood. Altered levels of obesity related peptides such as ghrelin may play an important role in this pathophysiology. Recent evidence indicates that ghrelin features several cardiovascular activities, including increased myocardial contractility, vasodilatation and protection from myocardial infarction. Recent data demonstrate that ghrelin can influence important key events in atherogenesis and thus they may play a role in atherosclerosis. In this review we present the latest data from recent animal and clinical studies which focus on a novel approach to ghrelin as a potential therapeutic agent in the treatment of a complex disease like atherosclerosis. Thus, ghrelin may become a new therapeutic target for the treatment of CVD. Further studies are necessary to investigate the potential mechanisms involved in the effects of ghrelin on the cardiovascular system.",
publisher = "New York : Nova Science Publishers Inc.",
journal = "Ghrelin: Production, Action Mechanisms and Physiological Effects",
booktitle = "Ghrelin, obesity and atherosclerosis",
pages = "111-126",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3920"
}

Sudar, E., Soskić, S., Zarić, B., Rašić-Milutinović, Z., Smiljanić, K., Radak, Đ., Mikhailidis, D., Rizzo, M.,& Isenović, E.. (2012). Ghrelin, obesity and atherosclerosis. in Ghrelin: Production, Action Mechanisms and Physiological Effects
New York : Nova Science Publishers Inc.., 111-126.
https://hdl.handle.net/21.15107/rcub_cherry_3920

Sudar E, Soskić S, Zarić B, Rašić-Milutinović Z, Smiljanić K, Radak Đ, Mikhailidis D, Rizzo M, Isenović E. Ghrelin, obesity and atherosclerosis. in Ghrelin: Production, Action Mechanisms and Physiological Effects. 2012;:111-126.
https://hdl.handle.net/21.15107/rcub_cherry_3920 .

Sudar, Emina, Soskić, Sanja, Zarić, Božidarka, Rašić-Milutinović, Zorica, Smiljanić, Katarina, Radak, Đorđe, Mikhailidis, Dimitri, Rizzo, Manfredi, Isenović, Esma, "Ghrelin, obesity and atherosclerosis" in Ghrelin: Production, Action Mechanisms and Physiological Effects (2012):111-126,
https://hdl.handle.net/21.15107/rcub_cherry_3920 .

TY  - JOUR
AU  - Soskic, Sanja S.
AU  - Dobutovic, Branislava D.
AU  - Sudar, Emina M.
AU  - Obradovic, Milan M.
AU  - Nikolic, Dragana M.
AU  - Zarić, Božidarka
AU  - Stojanović, Srđan
AU  - Stokic, Edita J.
AU  - Mikhailidis, Dimitri P.
AU  - Isenovic, Esma R.
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/762
AB  - The peroxisome proliferator-activated receptors (PPARs) represent the family of 3 nuclear receptor isoforms-PPAR alpha, -gamma, and -delta/beta, which are encoded by different genes. As lipid sensors, they are primarily involved in regulation of lipid metabolism and subsequently in inflammation and atherosclerosis. Atherosclerosis considers accumulation of the cells and extracellular matrix in the vessel wall leading to the formation of atherosclerotic plaque, atherothrombosis, and other vascular complications. Besides existence of natural ligands for PPARs, their more potent synthetic ligands are fibrates and thiazolidindiones. Future investigations should now focus on the mechanisms of PPARs activation, which might present new approaches involved in the antiatherosclerotic effects revealed in this review. In addition, in this review we are presenting latest data from recent performed clinical studies which have focus on novel approach to PPARs agonists as potential therapeutic agents in the treatment of complex disease such as atherosclerosis.
PB  - Sage Publications Inc, Thousand Oaks
T2  - Angiology
T1  - Peroxisome Proliferator-Activated Receptors and Atherosclerosis
VL  - 62
IS  - 7
SP  - 523
EP  - 534
DO  - 10.1177/0003319711401012
ER  - 

@article{
author = "Soskic, Sanja S. and Dobutovic, Branislava D. and Sudar, Emina M. and Obradovic, Milan M. and Nikolic, Dragana M. and Zarić, Božidarka and Stojanović, Srđan and Stokic, Edita J. and Mikhailidis, Dimitri P. and Isenovic, Esma R.",
year = "2011",
abstract = "The peroxisome proliferator-activated receptors (PPARs) represent the family of 3 nuclear receptor isoforms-PPAR alpha, -gamma, and -delta/beta, which are encoded by different genes. As lipid sensors, they are primarily involved in regulation of lipid metabolism and subsequently in inflammation and atherosclerosis. Atherosclerosis considers accumulation of the cells and extracellular matrix in the vessel wall leading to the formation of atherosclerotic plaque, atherothrombosis, and other vascular complications. Besides existence of natural ligands for PPARs, their more potent synthetic ligands are fibrates and thiazolidindiones. Future investigations should now focus on the mechanisms of PPARs activation, which might present new approaches involved in the antiatherosclerotic effects revealed in this review. In addition, in this review we are presenting latest data from recent performed clinical studies which have focus on novel approach to PPARs agonists as potential therapeutic agents in the treatment of complex disease such as atherosclerosis.",
publisher = "Sage Publications Inc, Thousand Oaks",
journal = "Angiology",
title = "Peroxisome Proliferator-Activated Receptors and Atherosclerosis",
volume = "62",
number = "7",
pages = "523-534",
doi = "10.1177/0003319711401012"
}

Soskic, S. S., Dobutovic, B. D., Sudar, E. M., Obradovic, M. M., Nikolic, D. M., Zarić, B., Stojanović, S., Stokic, E. J., Mikhailidis, D. P.,& Isenovic, E. R.. (2011). Peroxisome Proliferator-Activated Receptors and Atherosclerosis. in Angiology
Sage Publications Inc, Thousand Oaks., 62(7), 523-534.
https://doi.org/10.1177/0003319711401012

Soskic SS, Dobutovic BD, Sudar EM, Obradovic MM, Nikolic DM, Zarić B, Stojanović S, Stokic EJ, Mikhailidis DP, Isenovic ER. Peroxisome Proliferator-Activated Receptors and Atherosclerosis. in Angiology. 2011;62(7):523-534.
doi:10.1177/0003319711401012 .

Soskic, Sanja S., Dobutovic, Branislava D., Sudar, Emina M., Obradovic, Milan M., Nikolic, Dragana M., Zarić, Božidarka, Stojanović, Srđan, Stokic, Edita J., Mikhailidis, Dimitri P., Isenovic, Esma R., "Peroxisome Proliferator-Activated Receptors and Atherosclerosis" in Angiology, 62, no. 7 (2011):523-534,
https://doi.org/10.1177/0003319711401012 . .

TY  - JOUR
AU  - Stojanović, Srđan
AU  - Isenovic, Esma R.
AU  - Zarić, Božidarka
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/785
AB  - The distinguishing property of Sm/LSm protein assemblies is their high stability. In order to better understand the nature of Sm/LSm protein oligomers in this study we have analyzed the contribution of non-canonical interactions to the stability of assemblies. The predominant types of non-canonical interactions at Sm/LSm protein interfaces are CH center dot center dot center dot O, and CH center dot center dot center dot N interactions represented at interfaces. Our results show low percentages of XH-pi and non-canonical interactions involving sulfur atoms, while the backbone groups were less frequently involved. The data show a high percentage of non-canonical interactions in interfaces formed by charged residues with Lys and Arg, these being the major charged donors. The main chain non-canonical interactions might be slightly more linear than the side chain interactions, and they have somewhat shorter median distances. Comparing the stabilizing amino acid residues with amino acids which build non-canonical interactions at interfaces shows that certain amino acids like Phe, Pro, His and Tyr are involved with a high percentage. The high conservation score of amino acids that are involved in non-canonical interactions in protein interfaces is an additional strong argument for their importance in the stabilization of Sm/LSm protein assemblies.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Molecular Informatics
T1  - Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies
VL  - 30
IS  - 5
SP  - 430
EP  - 442
DO  - 10.1002/minf.201000176
ER  - 

@article{
author = "Stojanović, Srđan and Isenovic, Esma R. and Zarić, Božidarka",
year = "2011",
abstract = "The distinguishing property of Sm/LSm protein assemblies is their high stability. In order to better understand the nature of Sm/LSm protein oligomers in this study we have analyzed the contribution of non-canonical interactions to the stability of assemblies. The predominant types of non-canonical interactions at Sm/LSm protein interfaces are CH center dot center dot center dot O, and CH center dot center dot center dot N interactions represented at interfaces. Our results show low percentages of XH-pi and non-canonical interactions involving sulfur atoms, while the backbone groups were less frequently involved. The data show a high percentage of non-canonical interactions in interfaces formed by charged residues with Lys and Arg, these being the major charged donors. The main chain non-canonical interactions might be slightly more linear than the side chain interactions, and they have somewhat shorter median distances. Comparing the stabilizing amino acid residues with amino acids which build non-canonical interactions at interfaces shows that certain amino acids like Phe, Pro, His and Tyr are involved with a high percentage. The high conservation score of amino acids that are involved in non-canonical interactions in protein interfaces is an additional strong argument for their importance in the stabilization of Sm/LSm protein assemblies.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Molecular Informatics",
title = "Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies",
volume = "30",
number = "5",
pages = "430-442",
doi = "10.1002/minf.201000176"
}

Stojanović, S., Isenovic, E. R.,& Zarić, B.. (2011). Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies. in Molecular Informatics
Wiley-V C H Verlag Gmbh, Weinheim., 30(5), 430-442.
https://doi.org/10.1002/minf.201000176

Stojanović S, Isenovic ER, Zarić B. Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies. in Molecular Informatics. 2011;30(5):430-442.
doi:10.1002/minf.201000176 .

Stojanović, Srđan, Isenovic, Esma R., Zarić, Božidarka, "Contribution of Non-Canonical Interactions to the Stability of Sm/LSm Oligomeric Assemblies" in Molecular Informatics, 30, no. 5 (2011):430-442,
https://doi.org/10.1002/minf.201000176 . .

TY  - JOUR
AU  - Zarić, Božidarka
AU  - Jovanović, Vesna B.
AU  - Stojanović, Srđan
PY  - 2011
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/924
AB  - The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Theoretical Biology
T1  - Non-covalent interactions across subunit interfaces in Sm proteins
VL  - 271
IS  - 1
SP  - 18
EP  - 26
DO  - 10.1016/j.jtbi.2010.11.025
ER  - 

@article{
author = "Zarić, Božidarka and Jovanović, Vesna B. and Stojanović, Srđan",
year = "2011",
abstract = "The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Theoretical Biology",
title = "Non-covalent interactions across subunit interfaces in Sm proteins",
volume = "271",
number = "1",
pages = "18-26",
doi = "10.1016/j.jtbi.2010.11.025"
}

Zarić, B., Jovanović, V. B.,& Stojanović, S.. (2011). Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology
Academic Press Ltd- Elsevier Science Ltd, London., 271(1), 18-26.
https://doi.org/10.1016/j.jtbi.2010.11.025

Zarić B, Jovanović VB, Stojanović S. Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology. 2011;271(1):18-26.
doi:10.1016/j.jtbi.2010.11.025 .

Zarić, Božidarka, Jovanović, Vesna B., Stojanović, Srđan, "Non-covalent interactions across subunit interfaces in Sm proteins" in Journal of Theoretical Biology, 271, no. 1 (2011):18-26,
https://doi.org/10.1016/j.jtbi.2010.11.025 . .

TY  - JOUR
AU  - Stojanović, Srđan
AU  - Zarić, Božidarka
AU  - Zarić, Snežana D.
PY  - 2010
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/680
AB  - The distinguishing property of Sm protein associations is very high stability. In order to understand this property, we analyzed the interfaces and compared the properties of Sm protein interfaces with those of a test set, the Binding Interface Database (BID). The comparison revealed that the main differences between the interfaces of Sm proteins and those of the BID set are the content of charged residues, the coordination numbers of the residues, knowledge-based pair potentials, and the conservation scores of hot spots. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surfaces, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Hot spots are residues that make up a small fraction of the interfaces, but they contribute most of the binding energy. These residues are critical to protein-protein interactions. Analyses of knowledge-based pair potentials of hot spot and non-hot spot residues in Sm proteins show that they are significantly different; their mean values are 31.5 and 11.3, respectively. In the BID set, this difference is smaller; in this case, the mean values for hot spot and non-hot spot residues are 20.7 and 12.4, respectively. Hence, the pair potentials of hot spots differ significantly for the Sm and BID data sets. In the interfaces of Sm proteins, the amino acids are tightly packed, and the coordination numbers are larger in Sm proteins than in the BID set for both hot spots and non-hot spots. At the same time, the coordination numbers are higher for hot spots; the average coordination number of the hot spot residues in Sm proteins is 7.7, while it is 6.1 for the non-hot spot residues. The difference in the calculated average conservation score for hot spots and non-hot spots in Sm proteins is significantly larger than it is in the BID set. In Sm proteins, the average conservation score for the hot spots is 7.4. Hot spots are surrounded by residues that are moderately conserved (5.9). The average conservation score for the other interface residues is 5.6. The conservation scores in the BID set do not show a significant distinction between hot and non-hot spots: the mean values for hot and non-hot spot residues are 5.5 and 5.2, respectively. These data show that structurally conserved residues and hot spots are significantly correlated in Sm proteins.
PB  - Springer, New York
T2  - Journal of Molecular Modeling
T1  - Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins
VL  - 16
IS  - 11
SP  - 1743
EP  - 1751
DO  - 10.1007/s00894-010-0787-4
ER  - 

@article{
author = "Stojanović, Srđan and Zarić, Božidarka and Zarić, Snežana D.",
year = "2010",
abstract = "The distinguishing property of Sm protein associations is very high stability. In order to understand this property, we analyzed the interfaces and compared the properties of Sm protein interfaces with those of a test set, the Binding Interface Database (BID). The comparison revealed that the main differences between the interfaces of Sm proteins and those of the BID set are the content of charged residues, the coordination numbers of the residues, knowledge-based pair potentials, and the conservation scores of hot spots. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surfaces, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Hot spots are residues that make up a small fraction of the interfaces, but they contribute most of the binding energy. These residues are critical to protein-protein interactions. Analyses of knowledge-based pair potentials of hot spot and non-hot spot residues in Sm proteins show that they are significantly different; their mean values are 31.5 and 11.3, respectively. In the BID set, this difference is smaller; in this case, the mean values for hot spot and non-hot spot residues are 20.7 and 12.4, respectively. Hence, the pair potentials of hot spots differ significantly for the Sm and BID data sets. In the interfaces of Sm proteins, the amino acids are tightly packed, and the coordination numbers are larger in Sm proteins than in the BID set for both hot spots and non-hot spots. At the same time, the coordination numbers are higher for hot spots; the average coordination number of the hot spot residues in Sm proteins is 7.7, while it is 6.1 for the non-hot spot residues. The difference in the calculated average conservation score for hot spots and non-hot spots in Sm proteins is significantly larger than it is in the BID set. In Sm proteins, the average conservation score for the hot spots is 7.4. Hot spots are surrounded by residues that are moderately conserved (5.9). The average conservation score for the other interface residues is 5.6. The conservation scores in the BID set do not show a significant distinction between hot and non-hot spots: the mean values for hot and non-hot spot residues are 5.5 and 5.2, respectively. These data show that structurally conserved residues and hot spots are significantly correlated in Sm proteins.",
publisher = "Springer, New York",
journal = "Journal of Molecular Modeling",
title = "Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins",
volume = "16",
number = "11",
pages = "1743-1751",
doi = "10.1007/s00894-010-0787-4"
}

Stojanović, S., Zarić, B.,& Zarić, S. D.. (2010). Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins. in Journal of Molecular Modeling
Springer, New York., 16(11), 1743-1751.
https://doi.org/10.1007/s00894-010-0787-4

Stojanović S, Zarić B, Zarić SD. Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins. in Journal of Molecular Modeling. 2010;16(11):1743-1751.
doi:10.1007/s00894-010-0787-4 .

Stojanović, Srđan, Zarić, Božidarka, Zarić, Snežana D., "Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins" in Journal of Molecular Modeling, 16, no. 11 (2010):1743-1751,
https://doi.org/10.1007/s00894-010-0787-4 . .

TY  - CONF
AU  - Stojanović, Srđan
AU  - Zarić, Božidarka
AU  - Zarić, Snežana
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/6531
AB  - This study aims to characterize the interface hot spot
residues of subunits in Sm proteins. We performed an analysis of the X ray structure of 15 Sm
motif containing proteins from the Protein Data Bank (PDB) and summarize physicochemical
properties in an effort to understand the origin of their stabilizing contributions to protein–
protein associations.Our results show that low relCompASA is critical for a residue to be a hot spot. Though
many of the hot spot residues have similar relCompASA values with nonhot spot residues,
they have different mean values (hot spots: 5.1%, non-hot spots: 29.1%). The P-value for
relCompASA is less than 0.05, which indicate that hot spots located near the center of the
interface are a general property of the interfaces, and largely protected from bulk solvent
(corresponding to low relCompASA). RelDASA indicates the change in the solvent
accessibility of a residue, and correlate significantly with relCompASA. Additionally,
knowledge-based pair potentials of residues is statistically significant to discriminate hot
spots and non-hot spots (P-value = 5.7×10−6). These results indicate that hot spots are mostly
buried, tightly packed and form a network of favorable interactions with other residues.
Structurally conserved residues and hot spots correlate significantly, and demonstrate
that hot spots play an important role in the stability of oligomers.
PB  - Belgrade, Serbia : Faculty of Chemistry, University of Belgrade
PB  - Germany : Alexander von Humboldt Foundation
C3  - Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia
T1  - Identification of Hot spots in Sm protein interfaces
SP  - 75
EP  - 75
UR  - https://hdl.handle.net/21.15107/rcub_cer_6531
ER  - 

@conference{
author = "Stojanović, Srđan and Zarić, Božidarka and Zarić, Snežana",
year = "2009",
abstract = "This study aims to characterize the interface hot spot
residues of subunits in Sm proteins. We performed an analysis of the X ray structure of 15 Sm
motif containing proteins from the Protein Data Bank (PDB) and summarize physicochemical
properties in an effort to understand the origin of their stabilizing contributions to protein–
protein associations.Our results show that low relCompASA is critical for a residue to be a hot spot. Though
many of the hot spot residues have similar relCompASA values with nonhot spot residues,
they have different mean values (hot spots: 5.1%, non-hot spots: 29.1%). The P-value for
relCompASA is less than 0.05, which indicate that hot spots located near the center of the
interface are a general property of the interfaces, and largely protected from bulk solvent
(corresponding to low relCompASA). RelDASA indicates the change in the solvent
accessibility of a residue, and correlate significantly with relCompASA. Additionally,
knowledge-based pair potentials of residues is statistically significant to discriminate hot
spots and non-hot spots (P-value = 5.7×10−6). These results indicate that hot spots are mostly
buried, tightly packed and form a network of favorable interactions with other residues.
Structurally conserved residues and hot spots correlate significantly, and demonstrate
that hot spots play an important role in the stability of oligomers.",
publisher = "Belgrade, Serbia : Faculty of Chemistry, University of Belgrade, Germany : Alexander von Humboldt Foundation",
journal = "Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia",
title = "Identification of Hot spots in Sm protein interfaces",
pages = "75-75",
url = "https://hdl.handle.net/21.15107/rcub_cer_6531"
}

Stojanović, S., Zarić, B.,& Zarić, S.. (2009). Identification of Hot spots in Sm protein interfaces. in Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia
Belgrade, Serbia : Faculty of Chemistry, University of Belgrade., 75-75.
https://hdl.handle.net/21.15107/rcub_cer_6531

Stojanović S, Zarić B, Zarić S. Identification of Hot spots in Sm protein interfaces. in Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia. 2009;:75-75.
https://hdl.handle.net/21.15107/rcub_cer_6531 .

Stojanović, Srđan, Zarić, Božidarka, Zarić, Snežana, "Identification of Hot spots in Sm protein interfaces" in Book of abstracts - Second Humboldt conference on noncovalent interactions, October 22-25, 2009, Vršac, Serbia (2009):75-75,
https://hdl.handle.net/21.15107/rcub_cer_6531 .