TY  - JOUR
AU  - Atanasković, Marija
AU  - Morić, Ivana
AU  - Rokić, Miloš
AU  - Đokić, Anđela
AU  - Pantović, Jelena
AU  - Despotović, Dragana
AU  - Šenerović, Lidija
PY  - 2024
UR  - https://www.sciencedirect.com/science/article/pii/S221242922301194X
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2331
AB  - SalmonellaEnteritidis is the most commonly reported pathogen for foodborne illness outbreaks in both underdeveloped and developed regions. S. Enteritidis biofilms, which form on various food contact surfaces, are resistant to conventional physical and chemical cleaning and disinfection procedures routinely used in food processing. The aim of this study was to identify novel, industrially applicable enzymes that are active against S. Enteritidis biofilms. We describe the properties and anti-biofilm activity of heterologously expressed β-glucosidase B derived from the environmental strain Microbacterium sp. BG28 (BglB-BG28) collected from gills of bream fish. The enzyme inhibited adhesion and the early stages of biofilm formation in clinical isolates of S. Enteritidis. At a concentration of 200 μg/mL, BglB-BG28 effectively reduced biofilm formation, by decreasing biofilm biomass by 50% and metabolic activity within biofilms by 80%. The enzyme reduced the formation of air-liquid biofilms on various surfaces, including plastic, glass and metal, as observed by fluorescence microscopy. BglB-BG28 inhibited biofilm formation in Escherichia coli, another important food pathogen that also forms cellulose-rich biofilms. Using o-NPG as substrate, the enzyme showed activity at temperatures up to 50 °C and in a pH range between 4 and 8, high tolerance to sodium chloride and glucose, and compatibility with nonionic detergents. Importantly, no toxicity was observed in the model system Caenorhabditis elegans even at an enzyme concentration of 1 mg/mL. These results suggest that the β-glucosidase BglB-BG28 is a promising candidate for the development of a new enzyme-based disinfection protocol that can be used in food processing facilities.
PB  - Elsevier
T2  - Food Bioscience
T2  - Food BioscienceFood Bioscience
T1  - Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28
SP  - 103543
VL  - 57
DO  - 10.1016/j.fbio.2023.103543
ER  - 

@article{
author = "Atanasković, Marija and Morić, Ivana and Rokić, Miloš and Đokić, Anđela and Pantović, Jelena and Despotović, Dragana and Šenerović, Lidija",
year = "2024",
abstract = "SalmonellaEnteritidis is the most commonly reported pathogen for foodborne illness outbreaks in both underdeveloped and developed regions. S. Enteritidis biofilms, which form on various food contact surfaces, are resistant to conventional physical and chemical cleaning and disinfection procedures routinely used in food processing. The aim of this study was to identify novel, industrially applicable enzymes that are active against S. Enteritidis biofilms. We describe the properties and anti-biofilm activity of heterologously expressed β-glucosidase B derived from the environmental strain Microbacterium sp. BG28 (BglB-BG28) collected from gills of bream fish. The enzyme inhibited adhesion and the early stages of biofilm formation in clinical isolates of S. Enteritidis. At a concentration of 200 μg/mL, BglB-BG28 effectively reduced biofilm formation, by decreasing biofilm biomass by 50% and metabolic activity within biofilms by 80%. The enzyme reduced the formation of air-liquid biofilms on various surfaces, including plastic, glass and metal, as observed by fluorescence microscopy. BglB-BG28 inhibited biofilm formation in Escherichia coli, another important food pathogen that also forms cellulose-rich biofilms. Using o-NPG as substrate, the enzyme showed activity at temperatures up to 50 °C and in a pH range between 4 and 8, high tolerance to sodium chloride and glucose, and compatibility with nonionic detergents. Importantly, no toxicity was observed in the model system Caenorhabditis elegans even at an enzyme concentration of 1 mg/mL. These results suggest that the β-glucosidase BglB-BG28 is a promising candidate for the development of a new enzyme-based disinfection protocol that can be used in food processing facilities.",
publisher = "Elsevier",
journal = "Food Bioscience, Food BioscienceFood Bioscience",
title = "Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28",
pages = "103543",
volume = "57",
doi = "10.1016/j.fbio.2023.103543"
}

Atanasković, M., Morić, I., Rokić, M., Đokić, A., Pantović, J., Despotović, D.,& Šenerović, L.. (2024). Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28. in Food Bioscience
Elsevier., 57, 103543.
https://doi.org/10.1016/j.fbio.2023.103543

Atanasković M, Morić I, Rokić M, Đokić A, Pantović J, Despotović D, Šenerović L. Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28. in Food Bioscience. 2024;57:103543.
doi:10.1016/j.fbio.2023.103543 .

Atanasković, Marija, Morić, Ivana, Rokić, Miloš, Đokić, Anđela, Pantović, Jelena, Despotović, Dragana, Šenerović, Lidija, "Inhibition of Salmonella Enteritidis adhesion and biofilm formation by β-glucosidase B from Microbacterium sp. BG28" in Food Bioscience, 57 (2024):103543,
https://doi.org/10.1016/j.fbio.2023.103543 . .

TY  - CONF
AU  - Atanasković, Marija
AU  - Morić, Ivana
AU  - Rokić, Miloš
AU  - Šenerović, Lidija
PY  - 2023
UR  - https://belbi.bg.ac.rs/
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/2031
AB  - Biofilms are ubiquitous in nature, and the food industry is vulnerable to the risks posed by
biofilm formation. Not only do they interfere with the food production process, but they also
pose a public health threat. However, complete elimination of biofilms on food and food
contact surfaces cannot be achieved by conventional methods (cleaning and disinfection)
alone. New biofilm control strategies must be developed to prevent its formation and/or
persistence. Novel approaches may be based on enzymes that depolymerize components
of the biofilm matrix, making bacterial cells accessible to antimicrobial agents.
Environmental microorganisms are an inexhaustible source of new enzymes. In
Salmonella Enteritidis and Escherichia coli, known foodborne pathogens, cellulose is an
important component of the biofilm matrix, so our isolates from untapped environments
were tested for cellulolytic activity. Of the more than 70 isolates examined, isolate BG28
was selected as the most promising. Its genome was sequenced, annotated, and it was
identified as Gram-positive Microbacterium sp. Genome mining revealed the presence of
four complete genes for different β-glucosidases, one of three enzyme types of cellulase
complexes. To select the best candidate for heterologous expression DeepTMHMM,
ProtParam, and SoluProt were used to predict the presence/absence of signal peptide
and transmembrane domains, instability index, aliphatic index, hydrophilicity, and soluble
expression in E. coli. Based on the prediction results, the gene annotated as β-glucosidase
B was selected for recombinant expression. In addition, I-TASSER was used to model the
tertiary structure of the selected enzyme.
The β-glucosidase B was recombinantly expressed, purified, and tested for its anti-biofilm
activity. It was active and showed a 50% inhibitory effect on S. Enteritidis and E. coli biofilm
formation at a concentration of 100 μg/ml. To further evaluate this in silico approach in
the preselection of candidate enzymes for recombinant expression and purification, we
will use it to identify other enzymes of the cellulase complex.
PB  - Belgrade : Institute of molecular genetics and genetic engineering
C3  - 4th Belgrade Bioinformatics Conference
T1  - In silico pre-selection of β-glucosidase gene for heterologous recombinant expression
EP  - 86
SP  - 86
VL  - 4
UR  - https://hdl.handle.net/21.15107/rcub_imagine_2031
ER  - 

@conference{
author = "Atanasković, Marija and Morić, Ivana and Rokić, Miloš and Šenerović, Lidija",
year = "2023",
abstract = "Biofilms are ubiquitous in nature, and the food industry is vulnerable to the risks posed by
biofilm formation. Not only do they interfere with the food production process, but they also
pose a public health threat. However, complete elimination of biofilms on food and food
contact surfaces cannot be achieved by conventional methods (cleaning and disinfection)
alone. New biofilm control strategies must be developed to prevent its formation and/or
persistence. Novel approaches may be based on enzymes that depolymerize components
of the biofilm matrix, making bacterial cells accessible to antimicrobial agents.
Environmental microorganisms are an inexhaustible source of new enzymes. In
Salmonella Enteritidis and Escherichia coli, known foodborne pathogens, cellulose is an
important component of the biofilm matrix, so our isolates from untapped environments
were tested for cellulolytic activity. Of the more than 70 isolates examined, isolate BG28
was selected as the most promising. Its genome was sequenced, annotated, and it was
identified as Gram-positive Microbacterium sp. Genome mining revealed the presence of
four complete genes for different β-glucosidases, one of three enzyme types of cellulase
complexes. To select the best candidate for heterologous expression DeepTMHMM,
ProtParam, and SoluProt were used to predict the presence/absence of signal peptide
and transmembrane domains, instability index, aliphatic index, hydrophilicity, and soluble
expression in E. coli. Based on the prediction results, the gene annotated as β-glucosidase
B was selected for recombinant expression. In addition, I-TASSER was used to model the
tertiary structure of the selected enzyme.
The β-glucosidase B was recombinantly expressed, purified, and tested for its anti-biofilm
activity. It was active and showed a 50% inhibitory effect on S. Enteritidis and E. coli biofilm
formation at a concentration of 100 μg/ml. To further evaluate this in silico approach in
the preselection of candidate enzymes for recombinant expression and purification, we
will use it to identify other enzymes of the cellulase complex.",
publisher = "Belgrade : Institute of molecular genetics and genetic engineering",
journal = "4th Belgrade Bioinformatics Conference",
title = "In silico pre-selection of β-glucosidase gene for heterologous recombinant expression",
pages = "86-86",
volume = "4",
url = "https://hdl.handle.net/21.15107/rcub_imagine_2031"
}

Atanasković, M., Morić, I., Rokić, M.,& Šenerović, L.. (2023). In silico pre-selection of β-glucosidase gene for heterologous recombinant expression. in 4th Belgrade Bioinformatics Conference
Belgrade : Institute of molecular genetics and genetic engineering., 4, 86-86.
https://hdl.handle.net/21.15107/rcub_imagine_2031

Atanasković M, Morić I, Rokić M, Šenerović L. In silico pre-selection of β-glucosidase gene for heterologous recombinant expression. in 4th Belgrade Bioinformatics Conference. 2023;4:86-86.
https://hdl.handle.net/21.15107/rcub_imagine_2031 .

Atanasković, Marija, Morić, Ivana, Rokić, Miloš, Šenerović, Lidija, "In silico pre-selection of β-glucosidase gene for heterologous recombinant expression" in 4th Belgrade Bioinformatics Conference, 4 (2023):86-86,
https://hdl.handle.net/21.15107/rcub_imagine_2031 .

TY  - JOUR
AU  - Rokić, Miloš
AU  - Castro, Patricio
AU  - Leiva-Salcedo, Elias
AU  - Tomić, Melanija
AU  - Stojilković, Stanko S.
AU  - Coddou, Claudio
PY  - 2018
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/1109
AB  - P2X2 receptors (P2X2R) exhibit a slow desensitization during the initial ATP application and a progressive, calcium-dependent increase in rates of desensitization during repetitive stimulation. This pattern is observed in whole-cell recordings from cells expressing recombinant and native P2X2R. However, desensitization is not observed in perforated-patched cells and in two-electrode voltage clamped oocytes. Addition of ATP, but not ATP gamma S or GTP, in the pipette solution also abolishes progressive desensitization, whereas intracellular injection of apyrase facilitates receptor desensitization. Experiments with injection of alkaline phosphatase or addition of staurosporine and ATP in the intracellular solution suggest a role for a phosphorylation-dephosphorylation in receptor desensitization. Mutation of residues that are potential phosphorylation sites identified a critical role of the S363 residue in the intracellular ATP action. These findings indicate that intracellular calcium and ATP have opposing effects on P2X2R gating: calcium allosterically facilitates receptor desensitization and ATP covalently prevents the action of calcium. Single cell measurements further revealed that intracellular calcium stays elevated after washout in P2X2R-expressing cells and the blockade of mitochondrial sodium/calcium exchanger lowers calcium concentrations during washout periods to basal levels, suggesting a role of mitochondria in this process. Therefore, the metabolic state of the cell can influence P2X2R gating.
PB  - MDPI, Basel
T2  - International Journal of Molecular Sciences
T1  - Opposing Roles of Calcium and Intracellular ATP on Gating of the Purinergic P2X2 Receptor Channel
IS  - 4
VL  - 19
DO  - 10.3390/ijms19041161
ER  - 

@article{
author = "Rokić, Miloš and Castro, Patricio and Leiva-Salcedo, Elias and Tomić, Melanija and Stojilković, Stanko S. and Coddou, Claudio",
year = "2018",
abstract = "P2X2 receptors (P2X2R) exhibit a slow desensitization during the initial ATP application and a progressive, calcium-dependent increase in rates of desensitization during repetitive stimulation. This pattern is observed in whole-cell recordings from cells expressing recombinant and native P2X2R. However, desensitization is not observed in perforated-patched cells and in two-electrode voltage clamped oocytes. Addition of ATP, but not ATP gamma S or GTP, in the pipette solution also abolishes progressive desensitization, whereas intracellular injection of apyrase facilitates receptor desensitization. Experiments with injection of alkaline phosphatase or addition of staurosporine and ATP in the intracellular solution suggest a role for a phosphorylation-dephosphorylation in receptor desensitization. Mutation of residues that are potential phosphorylation sites identified a critical role of the S363 residue in the intracellular ATP action. These findings indicate that intracellular calcium and ATP have opposing effects on P2X2R gating: calcium allosterically facilitates receptor desensitization and ATP covalently prevents the action of calcium. Single cell measurements further revealed that intracellular calcium stays elevated after washout in P2X2R-expressing cells and the blockade of mitochondrial sodium/calcium exchanger lowers calcium concentrations during washout periods to basal levels, suggesting a role of mitochondria in this process. Therefore, the metabolic state of the cell can influence P2X2R gating.",
publisher = "MDPI, Basel",
journal = "International Journal of Molecular Sciences",
title = "Opposing Roles of Calcium and Intracellular ATP on Gating of the Purinergic P2X2 Receptor Channel",
number = "4",
volume = "19",
doi = "10.3390/ijms19041161"
}

Rokić, M., Castro, P., Leiva-Salcedo, E., Tomić, M., Stojilković, S. S.,& Coddou, C.. (2018). Opposing Roles of Calcium and Intracellular ATP on Gating of the Purinergic P2X2 Receptor Channel. in International Journal of Molecular Sciences
MDPI, Basel., 19(4).
https://doi.org/10.3390/ijms19041161

Rokić M, Castro P, Leiva-Salcedo E, Tomić M, Stojilković SS, Coddou C. Opposing Roles of Calcium and Intracellular ATP on Gating of the Purinergic P2X2 Receptor Channel. in International Journal of Molecular Sciences. 2018;19(4).
doi:10.3390/ijms19041161 .

Rokić, Miloš, Castro, Patricio, Leiva-Salcedo, Elias, Tomić, Melanija, Stojilković, Stanko S., Coddou, Claudio, "Opposing Roles of Calcium and Intracellular ATP on Gating of the Purinergic P2X2 Receptor Channel" in International Journal of Molecular Sciences, 19, no. 4 (2018),
https://doi.org/10.3390/ijms19041161 . .

TY  - JOUR
AU  - Tvrdonova, Vendula
AU  - Rokić, Miloš
AU  - Stojilković, Stanko S.
AU  - Zemkova, Hana
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/738
AB  - Crystallization of the zebrafish P2X4 receptor in both open and closed states revealed conformational differences in the ectodomain structures, including the dorsal fin and left flipper domains. Here, we focused on the role of these domains in receptor activation, responsiveness to orthosteric ATP analogue agonists, and desensitization. Alanine scanning mutagenesis of the R203-L214 (dorsal fin) and the D280-N293 (left flipper) sequences of the rat P2X4 receptor showed that ATP potency/efficacy was reduced in 15 out of 26 alanine mutants. The R203A, N204A, and N293A mutants were essentially non-functional, but receptor function was restored by ivermectin, an allosteric modulator. The I205A, T210A, L214A, P290A, G291A, and Y292A mutants exhibited significant changes in the responsiveness to orthosteric analog agonists 2-(methylthio) adenosine 5'-triphosphate, adenosine 5'-(gamma-thio) triphosphate, 2'(3'-O-(4-benzoylbenzoyl) adenosine 5'-triphosphate, and alpha,beta-methyleneadenosine 5'-triphosphate. In contrast, the responsiveness of L206A, N208A, D280A, T281A, R282A, and H286A mutants to analog agonists was comparable to that of the wild type receptor. Among these mutants, D280A, T281A, R282A, H286A, G291A, and Y292A also exhibited increased time-constant of the desensitizing current response. These experiments, together with homology modeling, indicate that residues located in the upper part of the dorsal fin and left flipper domains, relative to distance from the channel pore, contribute to the organization of the ATP binding pocket and to the initiation of signal transmission towards residues in the lower part of both domains. The R203 and N204 residues, deeply buried in the protein, may integrate the output signal from these two domains towards the gate. In addition, the left flipper residues predominantly account for the control of transition of channels from an open to a desensitized state.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Identification of Functionally Important Residues of the Rat P2X4 Receptor by Alanine Scanning Mutagenesis of the Dorsal Fin and Left Flipper Domains
IS  - 11
VL  - 9
DO  - 10.1371/journal.pone.0112902
ER  - 

@article{
author = "Tvrdonova, Vendula and Rokić, Miloš and Stojilković, Stanko S. and Zemkova, Hana",
year = "2014",
abstract = "Crystallization of the zebrafish P2X4 receptor in both open and closed states revealed conformational differences in the ectodomain structures, including the dorsal fin and left flipper domains. Here, we focused on the role of these domains in receptor activation, responsiveness to orthosteric ATP analogue agonists, and desensitization. Alanine scanning mutagenesis of the R203-L214 (dorsal fin) and the D280-N293 (left flipper) sequences of the rat P2X4 receptor showed that ATP potency/efficacy was reduced in 15 out of 26 alanine mutants. The R203A, N204A, and N293A mutants were essentially non-functional, but receptor function was restored by ivermectin, an allosteric modulator. The I205A, T210A, L214A, P290A, G291A, and Y292A mutants exhibited significant changes in the responsiveness to orthosteric analog agonists 2-(methylthio) adenosine 5'-triphosphate, adenosine 5'-(gamma-thio) triphosphate, 2'(3'-O-(4-benzoylbenzoyl) adenosine 5'-triphosphate, and alpha,beta-methyleneadenosine 5'-triphosphate. In contrast, the responsiveness of L206A, N208A, D280A, T281A, R282A, and H286A mutants to analog agonists was comparable to that of the wild type receptor. Among these mutants, D280A, T281A, R282A, H286A, G291A, and Y292A also exhibited increased time-constant of the desensitizing current response. These experiments, together with homology modeling, indicate that residues located in the upper part of the dorsal fin and left flipper domains, relative to distance from the channel pore, contribute to the organization of the ATP binding pocket and to the initiation of signal transmission towards residues in the lower part of both domains. The R203 and N204 residues, deeply buried in the protein, may integrate the output signal from these two domains towards the gate. In addition, the left flipper residues predominantly account for the control of transition of channels from an open to a desensitized state.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Identification of Functionally Important Residues of the Rat P2X4 Receptor by Alanine Scanning Mutagenesis of the Dorsal Fin and Left Flipper Domains",
number = "11",
volume = "9",
doi = "10.1371/journal.pone.0112902"
}

Tvrdonova, V., Rokić, M., Stojilković, S. S.,& Zemkova, H.. (2014). Identification of Functionally Important Residues of the Rat P2X4 Receptor by Alanine Scanning Mutagenesis of the Dorsal Fin and Left Flipper Domains. in PLoS One
Public Library Science, San Francisco., 9(11).
https://doi.org/10.1371/journal.pone.0112902

Tvrdonova V, Rokić M, Stojilković SS, Zemkova H. Identification of Functionally Important Residues of the Rat P2X4 Receptor by Alanine Scanning Mutagenesis of the Dorsal Fin and Left Flipper Domains. in PLoS One. 2014;9(11).
doi:10.1371/journal.pone.0112902 .

Tvrdonova, Vendula, Rokić, Miloš, Stojilković, Stanko S., Zemkova, Hana, "Identification of Functionally Important Residues of the Rat P2X4 Receptor by Alanine Scanning Mutagenesis of the Dorsal Fin and Left Flipper Domains" in PLoS One, 9, no. 11 (2014),
https://doi.org/10.1371/journal.pone.0112902 . .

TY  - JOUR
AU  - Stojilković, Stanko S.
AU  - Leiva-Salcedo, Elias
AU  - Rokić, Miloš
AU  - Coddou, Claudio
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/741
AB  - Significance: The family of purinergic P2X receptors (P2XRs) is a part of ligand-gated superfamily of channels activated by extracellular adenosine-5'-triphosphate. P2XRs are present in virtually all mammalian tissues as well as in tissues of other vertebrate and nonvertebrate species and mediate a large variety of functions, including fast transmission at central synapses, contraction of smooth muscle cells, platelet aggregation, and macrophage activation to proliferation and cell death. Recent Advances: The recent solving of crystal structure of the zebrafish P2X4.1R is a major advance in the understanding of structural correlates of channel activation and regulation. Combined with growing information obtained in the post-structure era and the reinterpretation of previous work within the context of the tridimensional structure, these data provide a better understanding of how the channel operates at the molecular levels. Critical Issues: This review focuses on the relationship between redox signaling and P2XR function. We also discuss other allosteric modulation of P2XR gating in the physiological/pathophysiological context. This includes the summary of extracellular actions of trace metals, which can be released to the synaptic cleft, pH decrease that happens during ischemia and inflammation, and calcium, an extracellular and intracellular messenger. Future Directions: Our evolving understanding of activation and regulation of P2XRs is helpful in clarifying the mechanism by which these channels trigger and modulate cellular functions. Further research is required to identify the signaling pathways contributing to the regulation of the receptor activity and to develop novel and receptor-specific allosteric modulators, which could be used in vivo with therapeutic potential.
PB  - Mary Ann Liebert, Inc, New Rochelle
T2  - Antioxidants & Redox Signaling
T1  - Regulation of ATP-Gated P2X Channels: From Redox Signaling to Interactions with Other Proteins
EP  - 970
IS  - 6
SP  - 953
VL  - 21
DO  - 10.1089/ars.2013.5549
ER  - 

@article{
author = "Stojilković, Stanko S. and Leiva-Salcedo, Elias and Rokić, Miloš and Coddou, Claudio",
year = "2014",
abstract = "Significance: The family of purinergic P2X receptors (P2XRs) is a part of ligand-gated superfamily of channels activated by extracellular adenosine-5'-triphosphate. P2XRs are present in virtually all mammalian tissues as well as in tissues of other vertebrate and nonvertebrate species and mediate a large variety of functions, including fast transmission at central synapses, contraction of smooth muscle cells, platelet aggregation, and macrophage activation to proliferation and cell death. Recent Advances: The recent solving of crystal structure of the zebrafish P2X4.1R is a major advance in the understanding of structural correlates of channel activation and regulation. Combined with growing information obtained in the post-structure era and the reinterpretation of previous work within the context of the tridimensional structure, these data provide a better understanding of how the channel operates at the molecular levels. Critical Issues: This review focuses on the relationship between redox signaling and P2XR function. We also discuss other allosteric modulation of P2XR gating in the physiological/pathophysiological context. This includes the summary of extracellular actions of trace metals, which can be released to the synaptic cleft, pH decrease that happens during ischemia and inflammation, and calcium, an extracellular and intracellular messenger. Future Directions: Our evolving understanding of activation and regulation of P2XRs is helpful in clarifying the mechanism by which these channels trigger and modulate cellular functions. Further research is required to identify the signaling pathways contributing to the regulation of the receptor activity and to develop novel and receptor-specific allosteric modulators, which could be used in vivo with therapeutic potential.",
publisher = "Mary Ann Liebert, Inc, New Rochelle",
journal = "Antioxidants & Redox Signaling",
title = "Regulation of ATP-Gated P2X Channels: From Redox Signaling to Interactions with Other Proteins",
pages = "970-953",
number = "6",
volume = "21",
doi = "10.1089/ars.2013.5549"
}

Stojilković, S. S., Leiva-Salcedo, E., Rokić, M.,& Coddou, C.. (2014). Regulation of ATP-Gated P2X Channels: From Redox Signaling to Interactions with Other Proteins. in Antioxidants & Redox Signaling
Mary Ann Liebert, Inc, New Rochelle., 21(6), 953-970.
https://doi.org/10.1089/ars.2013.5549

Stojilković SS, Leiva-Salcedo E, Rokić M, Coddou C. Regulation of ATP-Gated P2X Channels: From Redox Signaling to Interactions with Other Proteins. in Antioxidants & Redox Signaling. 2014;21(6):953-970.
doi:10.1089/ars.2013.5549 .

Stojilković, Stanko S., Leiva-Salcedo, Elias, Rokić, Miloš, Coddou, Claudio, "Regulation of ATP-Gated P2X Channels: From Redox Signaling to Interactions with Other Proteins" in Antioxidants & Redox Signaling, 21, no. 6 (2014):953-970,
https://doi.org/10.1089/ars.2013.5549 . .

TY  - JOUR
AU  - Rokić, Miloš
AU  - Stojilković, Stanko S.
AU  - Zemkova, Hana
PY  - 2014
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/764
AB  - P2X receptors are ATP-gated cation channels consisting of three subunits that are mutually intertwined and form an upper, central, and extracellular vestibule with three lateral portals and the channel pore. Here we used cysteine and alanine scanning mutagenesis of the rat P2X4R receptor V47 V61 and K326 N338 sequences to study structural and functional properties of extracellular vestibule during gating. Cysteine mutants were used to test the accessibility of these residue side chains to cadmium during closedopen-desensitized transitions, whereas alanine mutants served as controls. This study revealed the accessibility of residues E51, T57, S59, V61, K326, and M336 to cadmium in channels undergoing a transition from a closed-to-open state and the accessibility of residues V47, G53, D331, 1332, 1333, T335, 1337, and N338 in channels undergoing a transition from an open-to-desensitized state; residues E56 and K329 were accessible during both transitions. The effect of cadmium on channel gating was stimulatory in all reactive V47 V61 mutants and inhibitory in the majority of reactive K326 N338 mutants. The rat P2X4 receptor homology model suggests that residues affected by cadmium in the closed-to-open transition were located within the lumen of the extracellular vestibule and toward the central vestibule; however, the residues affected by cadmium in the open-to-desensitized state were located at the bottom of the vestibule near the pore. Analysis of the model assumed that there is ion access to extracellular and central vestibules through lateral ports when the channel is closed, with residues above the first transmembrane domain being predominantly responsible for ion uptake. Upon receptor activation, there is passage of ions toward the residues located on the upper region of the second transmembrane domain, followed by permeation through the gate region.
PB  - Frontiers Research Foundation, Lausanne
T2  - Frontiers in Cellular Neuroscience
T1  - Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating
VL  - 8
DO  - 10.3389/fncel.2014.00003
ER  - 

@article{
author = "Rokić, Miloš and Stojilković, Stanko S. and Zemkova, Hana",
year = "2014",
abstract = "P2X receptors are ATP-gated cation channels consisting of three subunits that are mutually intertwined and form an upper, central, and extracellular vestibule with three lateral portals and the channel pore. Here we used cysteine and alanine scanning mutagenesis of the rat P2X4R receptor V47 V61 and K326 N338 sequences to study structural and functional properties of extracellular vestibule during gating. Cysteine mutants were used to test the accessibility of these residue side chains to cadmium during closedopen-desensitized transitions, whereas alanine mutants served as controls. This study revealed the accessibility of residues E51, T57, S59, V61, K326, and M336 to cadmium in channels undergoing a transition from a closed-to-open state and the accessibility of residues V47, G53, D331, 1332, 1333, T335, 1337, and N338 in channels undergoing a transition from an open-to-desensitized state; residues E56 and K329 were accessible during both transitions. The effect of cadmium on channel gating was stimulatory in all reactive V47 V61 mutants and inhibitory in the majority of reactive K326 N338 mutants. The rat P2X4 receptor homology model suggests that residues affected by cadmium in the closed-to-open transition were located within the lumen of the extracellular vestibule and toward the central vestibule; however, the residues affected by cadmium in the open-to-desensitized state were located at the bottom of the vestibule near the pore. Analysis of the model assumed that there is ion access to extracellular and central vestibules through lateral ports when the channel is closed, with residues above the first transmembrane domain being predominantly responsible for ion uptake. Upon receptor activation, there is passage of ions toward the residues located on the upper region of the second transmembrane domain, followed by permeation through the gate region.",
publisher = "Frontiers Research Foundation, Lausanne",
journal = "Frontiers in Cellular Neuroscience",
title = "Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating",
volume = "8",
doi = "10.3389/fncel.2014.00003"
}

Rokić, M., Stojilković, S. S.,& Zemkova, H.. (2014). Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating. in Frontiers in Cellular Neuroscience
Frontiers Research Foundation, Lausanne., 8.
https://doi.org/10.3389/fncel.2014.00003

Rokić M, Stojilković SS, Zemkova H. Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating. in Frontiers in Cellular Neuroscience. 2014;8.
doi:10.3389/fncel.2014.00003 .

Rokić, Miloš, Stojilković, Stanko S., Zemkova, Hana, "Structural and functional properties of the rat P2X4 purinoreceptor extracellular vestibule during gating" in Frontiers in Cellular Neuroscience, 8 (2014),
https://doi.org/10.3389/fncel.2014.00003 . .

TY  - JOUR
AU  - Rokić, Miloš
AU  - Stojilković, Stanko S.
PY  - 2013
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/700
AB  - The occupancy of the orthosteric ligand binding sites of P2X receptor (P2XR) channels causes the rapid opening of a small cation-permeable pore, followed by a gradual dilation that renders the pore permeable to large organic cations. Electrophysiologically, this phenomenon was shown using whole-cell current recording on P2X2R-, P2X2/X5R-, P2X4R- and P2X7R-expressing cells that were bathed in N-methyl-D-glucamine (NMDG(+))-containing buffers in the presence and/or absence of small monovalent and divalent cations. The pore dilation of P2X4R and P2X7R caused a secondary current growth, whereas that of P2X2R showed a sustained kinetic coupling of dilation and desensitization, leading to receptor channel closure. The pore size of the P2X7R open and dilated states was estimated to be approximately 0.85 nm and greater than 1 nm, respectively. The P2XR pore dilation was also observed in intact cells by measurement of fluorescent dye uptake/release, application of polyethylene glycols of different sizes, and atomic force microscopy. However, pore dilation was not observed at the single channel level. Structural data describing the dilated state are not available, and the relevance of orthosteric and allosteric ligand interactions to pore dilation was not studied.
PB  - Frontiers Media Sa, Lausanne
T2  - Frontiers in Cellular Neuroscience
T1  - Two open states of P2X receptor channels
VL  - 7
DO  - 10.3389/fncel.2013.00215
ER  - 

@article{
author = "Rokić, Miloš and Stojilković, Stanko S.",
year = "2013",
abstract = "The occupancy of the orthosteric ligand binding sites of P2X receptor (P2XR) channels causes the rapid opening of a small cation-permeable pore, followed by a gradual dilation that renders the pore permeable to large organic cations. Electrophysiologically, this phenomenon was shown using whole-cell current recording on P2X2R-, P2X2/X5R-, P2X4R- and P2X7R-expressing cells that were bathed in N-methyl-D-glucamine (NMDG(+))-containing buffers in the presence and/or absence of small monovalent and divalent cations. The pore dilation of P2X4R and P2X7R caused a secondary current growth, whereas that of P2X2R showed a sustained kinetic coupling of dilation and desensitization, leading to receptor channel closure. The pore size of the P2X7R open and dilated states was estimated to be approximately 0.85 nm and greater than 1 nm, respectively. The P2XR pore dilation was also observed in intact cells by measurement of fluorescent dye uptake/release, application of polyethylene glycols of different sizes, and atomic force microscopy. However, pore dilation was not observed at the single channel level. Structural data describing the dilated state are not available, and the relevance of orthosteric and allosteric ligand interactions to pore dilation was not studied.",
publisher = "Frontiers Media Sa, Lausanne",
journal = "Frontiers in Cellular Neuroscience",
title = "Two open states of P2X receptor channels",
volume = "7",
doi = "10.3389/fncel.2013.00215"
}

Rokić, M.,& Stojilković, S. S.. (2013). Two open states of P2X receptor channels. in Frontiers in Cellular Neuroscience
Frontiers Media Sa, Lausanne., 7.
https://doi.org/10.3389/fncel.2013.00215

Rokić M, Stojilković SS. Two open states of P2X receptor channels. in Frontiers in Cellular Neuroscience. 2013;7.
doi:10.3389/fncel.2013.00215 .

Rokić, Miloš, Stojilković, Stanko S., "Two open states of P2X receptor channels" in Frontiers in Cellular Neuroscience, 7 (2013),
https://doi.org/10.3389/fncel.2013.00215 . .

TY  - JOUR
AU  - Rokić, Miloš
AU  - Stojilković, Stanko S.
AU  - Vavra, Vojtech
AU  - Kuzyk, Pavlo
AU  - Tvrdonova, Vendula
AU  - Zemkova, Hana
PY  - 2013
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/625
AB  - The binding of ATP to trimeric P2X receptors (P2XR) causes an enlargement of the receptor extracellular vestibule, leading to opening of the cation-selective transmembrane pore, but specific roles of vestibule amino acid residues in receptor activation have not been evaluated systematically. In this study, alanine or cysteine scanning mutagenesis of V47-V61 and F324-N338 sequences of rat P2X4R revealed that V49, Y54, Q55, F324, and G325 mutants were poorly responsive to ATP and trafficking was only affected by the V49 mutation. The Y54F and Y54W mutations, but not the Y54L mutation, rescued receptor function, suggesting that an aromatic residue is important at this position. Furthermore, the Y54A and Y54C receptor function was partially rescued by ivermectin, a positive allosteric modulator of P2X4R, suggesting a rightward shift in the potency of ATP to activate P2X4R. The Q55T, Q55N, Q55E, and Q55K mutations resulted in non-responsive receptors and only the Q55E mutant was ivermectin-sensitive. The F324L, F324Y, and F324W mutations also rescued receptor function partially or completely, ivermectin action on channel gating was preserved in all mutants, and changes in ATP responsiveness correlated with the hydrophobicity and side chain volume of the substituent. The G325P mutant had a normal response to ATP, suggesting that G325 is a flexible hinge. A topological analysis revealed that the G325 and F324 residues disrupt a beta-sheet upon ATP binding. These results indicate multiple roles of the extracellular vestibule amino acid residues in the P2X4R function: the V49 residue is important for receptor trafficking to plasma membrane, the Y54 and Q55 residues play a critical role in channel gating and the F324 and G325 residues are critical for vestibule widening.
PB  - Public Library Science, San Francisco
T2  - PLoS One
T1  - Multiple Roles of the Extracellular Vestibule Amino Acid Residues in the Function of the Rat P2X4 Receptor
IS  - 3
VL  - 8
DO  - 10.1371/journal.pone.0059411
ER  - 

@article{
author = "Rokić, Miloš and Stojilković, Stanko S. and Vavra, Vojtech and Kuzyk, Pavlo and Tvrdonova, Vendula and Zemkova, Hana",
year = "2013",
abstract = "The binding of ATP to trimeric P2X receptors (P2XR) causes an enlargement of the receptor extracellular vestibule, leading to opening of the cation-selective transmembrane pore, but specific roles of vestibule amino acid residues in receptor activation have not been evaluated systematically. In this study, alanine or cysteine scanning mutagenesis of V47-V61 and F324-N338 sequences of rat P2X4R revealed that V49, Y54, Q55, F324, and G325 mutants were poorly responsive to ATP and trafficking was only affected by the V49 mutation. The Y54F and Y54W mutations, but not the Y54L mutation, rescued receptor function, suggesting that an aromatic residue is important at this position. Furthermore, the Y54A and Y54C receptor function was partially rescued by ivermectin, a positive allosteric modulator of P2X4R, suggesting a rightward shift in the potency of ATP to activate P2X4R. The Q55T, Q55N, Q55E, and Q55K mutations resulted in non-responsive receptors and only the Q55E mutant was ivermectin-sensitive. The F324L, F324Y, and F324W mutations also rescued receptor function partially or completely, ivermectin action on channel gating was preserved in all mutants, and changes in ATP responsiveness correlated with the hydrophobicity and side chain volume of the substituent. The G325P mutant had a normal response to ATP, suggesting that G325 is a flexible hinge. A topological analysis revealed that the G325 and F324 residues disrupt a beta-sheet upon ATP binding. These results indicate multiple roles of the extracellular vestibule amino acid residues in the P2X4R function: the V49 residue is important for receptor trafficking to plasma membrane, the Y54 and Q55 residues play a critical role in channel gating and the F324 and G325 residues are critical for vestibule widening.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One",
title = "Multiple Roles of the Extracellular Vestibule Amino Acid Residues in the Function of the Rat P2X4 Receptor",
number = "3",
volume = "8",
doi = "10.1371/journal.pone.0059411"
}

Rokić, M., Stojilković, S. S., Vavra, V., Kuzyk, P., Tvrdonova, V.,& Zemkova, H.. (2013). Multiple Roles of the Extracellular Vestibule Amino Acid Residues in the Function of the Rat P2X4 Receptor. in PLoS One
Public Library Science, San Francisco., 8(3).
https://doi.org/10.1371/journal.pone.0059411

Rokić M, Stojilković SS, Vavra V, Kuzyk P, Tvrdonova V, Zemkova H. Multiple Roles of the Extracellular Vestibule Amino Acid Residues in the Function of the Rat P2X4 Receptor. in PLoS One. 2013;8(3).
doi:10.1371/journal.pone.0059411 .

Rokić, Miloš, Stojilković, Stanko S., Vavra, Vojtech, Kuzyk, Pavlo, Tvrdonova, Vendula, Zemkova, Hana, "Multiple Roles of the Extracellular Vestibule Amino Acid Residues in the Function of the Rat P2X4 Receptor" in PLoS One, 8, no. 3 (2013),
https://doi.org/10.1371/journal.pone.0059411 . .

TY  - CONF
AU  - Tvrdonova, V.
AU  - Rokić, Miloš
AU  - Zemkova, H.
PY  - 2013
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/631
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal
T1  - Influence of residues in low-conserved regions near the ATP-binding site of P2X4 receptor on channel gating
EP  - 191
SP  - 191
VL  - 280
UR  - https://hdl.handle.net/21.15107/rcub_imagine_631
ER  - 

@conference{
author = "Tvrdonova, V. and Rokić, Miloš and Zemkova, H.",
year = "2013",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal",
title = "Influence of residues in low-conserved regions near the ATP-binding site of P2X4 receptor on channel gating",
pages = "191-191",
volume = "280",
url = "https://hdl.handle.net/21.15107/rcub_imagine_631"
}

Tvrdonova, V., Rokić, M.,& Zemkova, H.. (2013). Influence of residues in low-conserved regions near the ATP-binding site of P2X4 receptor on channel gating. in FEBS Journal
Wiley-Blackwell, Hoboken., 280, 191-191.
https://hdl.handle.net/21.15107/rcub_imagine_631

Tvrdonova V, Rokić M, Zemkova H. Influence of residues in low-conserved regions near the ATP-binding site of P2X4 receptor on channel gating. in FEBS Journal. 2013;280:191-191.
https://hdl.handle.net/21.15107/rcub_imagine_631 .

Tvrdonova, V., Rokić, Miloš, Zemkova, H., "Influence of residues in low-conserved regions near the ATP-binding site of P2X4 receptor on channel gating" in FEBS Journal, 280 (2013):191-191,
https://hdl.handle.net/21.15107/rcub_imagine_631 .

TY  - CONF
AU  - Tvrdonova, V.
AU  - Rokić, Miloš
AU  - Kuzyk, P.
AU  - Stojilković, S. S.
AU  - Zemkova, H.
PY  - 2011
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/537
PB  - Springer Wien, Wien
C3  - Amino Acids
T1  - Role of low-conserved areas of extracellular vestibule in function of purinergic P2X4 receptor
EP  - S46
SP  - S46
VL  - 41
UR  - https://hdl.handle.net/21.15107/rcub_imagine_537
ER  - 

@conference{
author = "Tvrdonova, V. and Rokić, Miloš and Kuzyk, P. and Stojilković, S. S. and Zemkova, H.",
year = "2011",
publisher = "Springer Wien, Wien",
journal = "Amino Acids",
title = "Role of low-conserved areas of extracellular vestibule in function of purinergic P2X4 receptor",
pages = "S46-S46",
volume = "41",
url = "https://hdl.handle.net/21.15107/rcub_imagine_537"
}

Tvrdonova, V., Rokić, M., Kuzyk, P., Stojilković, S. S.,& Zemkova, H.. (2011). Role of low-conserved areas of extracellular vestibule in function of purinergic P2X4 receptor. in Amino Acids
Springer Wien, Wien., 41, S46-S46.
https://hdl.handle.net/21.15107/rcub_imagine_537

Tvrdonova V, Rokić M, Kuzyk P, Stojilković SS, Zemkova H. Role of low-conserved areas of extracellular vestibule in function of purinergic P2X4 receptor. in Amino Acids. 2011;41:S46-S46.
https://hdl.handle.net/21.15107/rcub_imagine_537 .

Tvrdonova, V., Rokić, Miloš, Kuzyk, P., Stojilković, S. S., Zemkova, H., "Role of low-conserved areas of extracellular vestibule in function of purinergic P2X4 receptor" in Amino Acids, 41 (2011):S46-S46,
https://hdl.handle.net/21.15107/rcub_imagine_537 .

TY  - JOUR
AU  - Rokić, Miloš
AU  - Tvrdonova, V.
AU  - Vavra, V.
AU  - Jindrichova, M.
AU  - Obsil, T.
AU  - Stojilković, S. S.
AU  - Zemkova, H.
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/403
AB  - Mammalian P2X receptors contain 10 conserved cysteine residues in their ectodomains, which form five disulfide bonds (SS1-5). Here, we analyzed the relevance of these disulfide pairs in rat P2X4 receptor function by replacing one or both cysteines with alanine or threonine, expressing receptors in HEK293 cells and studying their responsiveness to ATP in the absence and presence of ivermectin, an allostenic modulator of these channels. Response to ATP was not altered when both cysteines forming the SS3 bond (C132-C159) were replaced with threonines. Replacement of SS1 (C116-C165), SS2 (C126-C149) and SS4 (C217-C227), but not SS5 (C261-C270), cysteine pairs with threonines resulted in decreased sensitivity to ATP and faster deactivation times. The maximum current amplitude was reduced in SS2, SS4 and SS5 double mutants and could be partially rescued by ivermectin in SS2 and SS5 double mutants. This response pattern was also observed in numerous single residue mutants, but receptor function was not affected when the 217 cysteine was replaced with threonine or arginine or when the 261 cysteine was replaced with alanine. These results suggest that the SS1, SS2 and SS4 bonds contribute substantially to the structure of the ligand binding pocket, while the SS5 bond located towards the transmembrane domain contributes to receptor gating.
PB  - Acad Sciences Czech Republic, Inst Physiology, Prague 4
T2  - Physiological Research
T1  - Roles of Conserved Ectodomain Cysteines of the Rat P2X4 Purinoreceptor in Agonist Binding and Channel Gating
EP  - 935
IS  - 6
SP  - 927
VL  - 59
DO  - 10.33549/physiolres.931979
ER  - 

@article{
author = "Rokić, Miloš and Tvrdonova, V. and Vavra, V. and Jindrichova, M. and Obsil, T. and Stojilković, S. S. and Zemkova, H.",
year = "2010",
abstract = "Mammalian P2X receptors contain 10 conserved cysteine residues in their ectodomains, which form five disulfide bonds (SS1-5). Here, we analyzed the relevance of these disulfide pairs in rat P2X4 receptor function by replacing one or both cysteines with alanine or threonine, expressing receptors in HEK293 cells and studying their responsiveness to ATP in the absence and presence of ivermectin, an allostenic modulator of these channels. Response to ATP was not altered when both cysteines forming the SS3 bond (C132-C159) were replaced with threonines. Replacement of SS1 (C116-C165), SS2 (C126-C149) and SS4 (C217-C227), but not SS5 (C261-C270), cysteine pairs with threonines resulted in decreased sensitivity to ATP and faster deactivation times. The maximum current amplitude was reduced in SS2, SS4 and SS5 double mutants and could be partially rescued by ivermectin in SS2 and SS5 double mutants. This response pattern was also observed in numerous single residue mutants, but receptor function was not affected when the 217 cysteine was replaced with threonine or arginine or when the 261 cysteine was replaced with alanine. These results suggest that the SS1, SS2 and SS4 bonds contribute substantially to the structure of the ligand binding pocket, while the SS5 bond located towards the transmembrane domain contributes to receptor gating.",
publisher = "Acad Sciences Czech Republic, Inst Physiology, Prague 4",
journal = "Physiological Research",
title = "Roles of Conserved Ectodomain Cysteines of the Rat P2X4 Purinoreceptor in Agonist Binding and Channel Gating",
pages = "935-927",
number = "6",
volume = "59",
doi = "10.33549/physiolres.931979"
}

Rokić, M., Tvrdonova, V., Vavra, V., Jindrichova, M., Obsil, T., Stojilković, S. S.,& Zemkova, H.. (2010). Roles of Conserved Ectodomain Cysteines of the Rat P2X4 Purinoreceptor in Agonist Binding and Channel Gating. in Physiological Research
Acad Sciences Czech Republic, Inst Physiology, Prague 4., 59(6), 927-935.
https://doi.org/10.33549/physiolres.931979

Rokić M, Tvrdonova V, Vavra V, Jindrichova M, Obsil T, Stojilković SS, Zemkova H. Roles of Conserved Ectodomain Cysteines of the Rat P2X4 Purinoreceptor in Agonist Binding and Channel Gating. in Physiological Research. 2010;59(6):927-935.
doi:10.33549/physiolres.931979 .

Rokić, Miloš, Tvrdonova, V., Vavra, V., Jindrichova, M., Obsil, T., Stojilković, S. S., Zemkova, H., "Roles of Conserved Ectodomain Cysteines of the Rat P2X4 Purinoreceptor in Agonist Binding and Channel Gating" in Physiological Research, 59, no. 6 (2010):927-935,
https://doi.org/10.33549/physiolres.931979 . .

TY  - JOUR
AU  - Nikolić, Ljiljana
AU  - Rokić, Miloš
AU  - Todorović, Nataša V.
AU  - Kartelija, Gordana S.
AU  - Nedeljković, Miodrag S.
AU  - Zakrzewska, Joanna S.
PY  - 2010
UR  - https://imagine.imgge.bg.ac.rs/handle/123456789/459
AB  - The effect of extremely low frequency magnetic fields (50 Hz, 0.5 mT) - ELF-MF, on phosphate metabolism has been studied in the isolated ganglions of the garden snail Helix pomatia, after 7 and 16 days of snail exposure to ELF-MF. The influence of ELF-MF on the level of phosphate compounds and intracellular pH was monitored by P-31 NMR spectroscopy. Furthermore, the activity of enzymes involved in phosphate turnover, total ATPases, Na+/K+-ATPase and acid phosphatase has been measured. The exposure of snails to the ELF-MF for the period of 7 days shifted intracellular pH toward more alkaline conditions, and increased the activity of investigated enzymes. Prolonged exposure to the ELF-MF for the period of 16 days caused a decrease of PCr and ATP levels and decreased enzyme activity, compared to the 7-day treatment group. Our results can be explained in terms of: 1. increase in phosphate turnover by exposure to the ELF-MF for the period of 7 days, and 2. adaptation of phosphate metabolism in the nervous system of snails to prolonged ELF-MF exposure.
PB  - Soc Biolgia Chile, Santiago
T2  - Biological Research
T1  - Effect of alternating the magnetic field on phosphate metabolism in the nervous system of Helix pomatia
EP  - 250
IS  - 2
SP  - 243
VL  - 43
DO  - 10.4067/S0716-97602010000200012
ER  - 

@article{
author = "Nikolić, Ljiljana and Rokić, Miloš and Todorović, Nataša V. and Kartelija, Gordana S. and Nedeljković, Miodrag S. and Zakrzewska, Joanna S.",
year = "2010",
abstract = "The effect of extremely low frequency magnetic fields (50 Hz, 0.5 mT) - ELF-MF, on phosphate metabolism has been studied in the isolated ganglions of the garden snail Helix pomatia, after 7 and 16 days of snail exposure to ELF-MF. The influence of ELF-MF on the level of phosphate compounds and intracellular pH was monitored by P-31 NMR spectroscopy. Furthermore, the activity of enzymes involved in phosphate turnover, total ATPases, Na+/K+-ATPase and acid phosphatase has been measured. The exposure of snails to the ELF-MF for the period of 7 days shifted intracellular pH toward more alkaline conditions, and increased the activity of investigated enzymes. Prolonged exposure to the ELF-MF for the period of 16 days caused a decrease of PCr and ATP levels and decreased enzyme activity, compared to the 7-day treatment group. Our results can be explained in terms of: 1. increase in phosphate turnover by exposure to the ELF-MF for the period of 7 days, and 2. adaptation of phosphate metabolism in the nervous system of snails to prolonged ELF-MF exposure.",
publisher = "Soc Biolgia Chile, Santiago",
journal = "Biological Research",
title = "Effect of alternating the magnetic field on phosphate metabolism in the nervous system of Helix pomatia",
pages = "250-243",
number = "2",
volume = "43",
doi = "10.4067/S0716-97602010000200012"
}

Nikolić, L., Rokić, M., Todorović, N. V., Kartelija, G. S., Nedeljković, M. S.,& Zakrzewska, J. S.. (2010). Effect of alternating the magnetic field on phosphate metabolism in the nervous system of Helix pomatia. in Biological Research
Soc Biolgia Chile, Santiago., 43(2), 243-250.
https://doi.org/10.4067/S0716-97602010000200012

Nikolić L, Rokić M, Todorović NV, Kartelija GS, Nedeljković MS, Zakrzewska JS. Effect of alternating the magnetic field on phosphate metabolism in the nervous system of Helix pomatia. in Biological Research. 2010;43(2):243-250.
doi:10.4067/S0716-97602010000200012 .

Nikolić, Ljiljana, Rokić, Miloš, Todorović, Nataša V., Kartelija, Gordana S., Nedeljković, Miodrag S., Zakrzewska, Joanna S., "Effect of alternating the magnetic field on phosphate metabolism in the nervous system of Helix pomatia" in Biological Research, 43, no. 2 (2010):243-250,
https://doi.org/10.4067/S0716-97602010000200012 . .