TY  - CONF
AU  - Jovanović, Mirna
AU  - Podolski-Renić, Ana
AU  - Žalubovskis, Raivis
AU  - Pešić, Milica
PY  - 2020
UR  - https://stratagem-cost.eu/wp-content/uploads/2020/03/Abstract-book-Belgrade-2020.pdf
UR  - http://radar.ibiss.bg.ac.rs/handle/123456789/6497
AB  - Cancer cells have increased level of reactive oxygen species (ROS), due to metabolic changes following their growth and development; they have adapted to increase in ROS by different mechanism, in part by increasing activity of antioxidant systems. Main antioxidant systems in a living cell are thioredoxin and glutharedoxin systems. Thioredoxin system is mainly comprised of thioredoxin and thioredoxin reductase. It has been reported that cytosolic thioredoxin reductase, TrxR1, has increased activity in cancer cells. Inhibition of TrxR1 could have a detrimental effect on cancer cell survival, due to further increase of ROS. Development of new TrxR1 inhibitors gives possibilities in new therapeutic approaches in treating cancer,
as an accompanying treatment to conventional treatment strategies. STSM was realized in collaboration between home institution, Institute for Biological Research "Siniša Stanković" - National Institute of Republic of Serbia, University of Belgrade and host institution, Latvian Institute of Organic Synthesis (Riga, Latvia). Purpose of the STSM was to evaluate inhibitory properties of 6 potential inhibitors of thioredoxin reductase 1 on neuroblastoma cell line SHSY5Y. This particular cell line was chosen as it proved to be a good model for studying Trx system. Potential inhibitors were tested for inhibitory properties of TrxR on crude protein cell lysate of SHY5Y, rat TrxR1 enzyme and on insulin assay. Main result of this STSM is selection of the best candidate for further expansion series in studying Michael acceptors as inhibitors of TrxR1 and possible applications in anti-cancer therapy. The results obtained during STSM were published in a peer-reviewed journal [1]. This STSM is a perspective start to further investigation of importance of thioredoxin reductase 1 in cancer cell survival and inhibition of TrxR1 in cancer therapy. The candidate-inhibitors will in future be tested on cancer cell lines and multidrug resistant cancer cell models, with different antioxidant capacities.
PB  - COST Action CA17104
C3  - Abstract book: STRATAGEM CA17104: New diagnostic and therapeutic tools against multidrug-resistant tumours: First Working-Group Meeting WG1 - WG4; 2019 Jan 30-31; Turin, Italy
T1  - Presentation of STSM: Investigation of inhibitory properties of Michael acceptors on thioredoxin reductase 1 inhibition in vitro
SP  - 29
UR  - https://hdl.handle.net/21.15107/rcub_ibiss_6497
ER  - 

@conference{
author = "Jovanović, Mirna and Podolski-Renić, Ana and Žalubovskis, Raivis and Pešić, Milica",
year = "2020",
abstract = "Cancer cells have increased level of reactive oxygen species (ROS), due to metabolic changes following their growth and development; they have adapted to increase in ROS by different mechanism, in part by increasing activity of antioxidant systems. Main antioxidant systems in a living cell are thioredoxin and glutharedoxin systems. Thioredoxin system is mainly comprised of thioredoxin and thioredoxin reductase. It has been reported that cytosolic thioredoxin reductase, TrxR1, has increased activity in cancer cells. Inhibition of TrxR1 could have a detrimental effect on cancer cell survival, due to further increase of ROS. Development of new TrxR1 inhibitors gives possibilities in new therapeutic approaches in treating cancer,
as an accompanying treatment to conventional treatment strategies. STSM was realized in collaboration between home institution, Institute for Biological Research "Siniša Stanković" - National Institute of Republic of Serbia, University of Belgrade and host institution, Latvian Institute of Organic Synthesis (Riga, Latvia). Purpose of the STSM was to evaluate inhibitory properties of 6 potential inhibitors of thioredoxin reductase 1 on neuroblastoma cell line SHSY5Y. This particular cell line was chosen as it proved to be a good model for studying Trx system. Potential inhibitors were tested for inhibitory properties of TrxR on crude protein cell lysate of SHY5Y, rat TrxR1 enzyme and on insulin assay. Main result of this STSM is selection of the best candidate for further expansion series in studying Michael acceptors as inhibitors of TrxR1 and possible applications in anti-cancer therapy. The results obtained during STSM were published in a peer-reviewed journal [1]. This STSM is a perspective start to further investigation of importance of thioredoxin reductase 1 in cancer cell survival and inhibition of TrxR1 in cancer therapy. The candidate-inhibitors will in future be tested on cancer cell lines and multidrug resistant cancer cell models, with different antioxidant capacities.",
publisher = "COST Action CA17104",
journal = "Abstract book: STRATAGEM CA17104: New diagnostic and therapeutic tools against multidrug-resistant tumours: First Working-Group Meeting WG1 - WG4; 2019 Jan 30-31; Turin, Italy",
title = "Presentation of STSM: Investigation of inhibitory properties of Michael acceptors on thioredoxin reductase 1 inhibition in vitro",
pages = "29",
url = "https://hdl.handle.net/21.15107/rcub_ibiss_6497"
}

Jovanović, M., Podolski-Renić, A., Žalubovskis, R.,& Pešić, M.. (2020). Presentation of STSM: Investigation of inhibitory properties of Michael acceptors on thioredoxin reductase 1 inhibition in vitro. in Abstract book: STRATAGEM CA17104: New diagnostic and therapeutic tools against multidrug-resistant tumours: First Working-Group Meeting WG1 - WG4; 2019 Jan 30-31; Turin, Italy
COST Action CA17104., 29.
https://hdl.handle.net/21.15107/rcub_ibiss_6497

Jovanović M, Podolski-Renić A, Žalubovskis R, Pešić M. Presentation of STSM: Investigation of inhibitory properties of Michael acceptors on thioredoxin reductase 1 inhibition in vitro. in Abstract book: STRATAGEM CA17104: New diagnostic and therapeutic tools against multidrug-resistant tumours: First Working-Group Meeting WG1 - WG4; 2019 Jan 30-31; Turin, Italy. 2020;:29.
https://hdl.handle.net/21.15107/rcub_ibiss_6497 .

Jovanović, Mirna, Podolski-Renić, Ana, Žalubovskis, Raivis, Pešić, Milica, "Presentation of STSM: Investigation of inhibitory properties of Michael acceptors on thioredoxin reductase 1 inhibition in vitro" in Abstract book: STRATAGEM CA17104: New diagnostic and therapeutic tools against multidrug-resistant tumours: First Working-Group Meeting WG1 - WG4; 2019 Jan 30-31; Turin, Italy (2020):29,
https://hdl.handle.net/21.15107/rcub_ibiss_6497 .

TY  - JOUR
AU  - Jovanović, Mirna
AU  - Zhukovsky, Daniil
AU  - Podolski-Renić, Ana
AU  - Žalubovskis, Raivis
AU  - Dar'in, Dmitry
AU  - Sharoyko, Vladimir
AU  - Tennikova, Tatiana
AU  - Pešić, Milica
AU  - Krasavin, Mikhail
PY  - 2020
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/3614
AB  - A series of analogs of the earlier reported lead compound DVD-445 (thioredoxin reductase inhibitor with anticancer activity) has been synthesized via a modified Ugi reaction and investigated. Seven most potent compounds (with IC50 below 5.00 μM against recombinant rTrxR1 enzyme) were examined for their effect on cell growth and viability, oxidative stress induction and P-glycoprotein (P-gp) inhibition in human glioblastoma cells cell line U87 and its corresponding multidrug resistant (MDR) cell line U87-TxR. Several of these frontrunner compounds were shown to be superior over DVD-445. Besides providing promising candidates for anticancer therapy, our study further validates the small electrophilic Ugi Michael acceptor (UMA) chemotype as efficacious inhibitor of thioredoxin reductase.
T2  - European Journal of Medicinal Chemistry
T1  - Further exploration of DVD-445 as a lead thioredoxin reductase (TrxR) inhibitor for cancer therapy: Optimization of potency and evaluation of anticancer potential.
VL  - 191
DO  - 10.1016/j.ejmech.2020.112119
SP  - 112119
ER  - 

@article{
author = "Jovanović, Mirna and Zhukovsky, Daniil and Podolski-Renić, Ana and Žalubovskis, Raivis and Dar'in, Dmitry and Sharoyko, Vladimir and Tennikova, Tatiana and Pešić, Milica and Krasavin, Mikhail",
year = "2020",
abstract = "A series of analogs of the earlier reported lead compound DVD-445 (thioredoxin reductase inhibitor with anticancer activity) has been synthesized via a modified Ugi reaction and investigated. Seven most potent compounds (with IC50 below 5.00 μM against recombinant rTrxR1 enzyme) were examined for their effect on cell growth and viability, oxidative stress induction and P-glycoprotein (P-gp) inhibition in human glioblastoma cells cell line U87 and its corresponding multidrug resistant (MDR) cell line U87-TxR. Several of these frontrunner compounds were shown to be superior over DVD-445. Besides providing promising candidates for anticancer therapy, our study further validates the small electrophilic Ugi Michael acceptor (UMA) chemotype as efficacious inhibitor of thioredoxin reductase.",
journal = "European Journal of Medicinal Chemistry",
title = "Further exploration of DVD-445 as a lead thioredoxin reductase (TrxR) inhibitor for cancer therapy: Optimization of potency and evaluation of anticancer potential.",
volume = "191",
doi = "10.1016/j.ejmech.2020.112119",
pages = "112119"
}

Jovanović, M., Zhukovsky, D., Podolski-Renić, A., Žalubovskis, R., Dar'in, D., Sharoyko, V., Tennikova, T., Pešić, M.,& Krasavin, M.. (2020). Further exploration of DVD-445 as a lead thioredoxin reductase (TrxR) inhibitor for cancer therapy: Optimization of potency and evaluation of anticancer potential.. in European Journal of Medicinal Chemistry, 191, 112119.
https://doi.org/10.1016/j.ejmech.2020.112119

Jovanović M, Zhukovsky D, Podolski-Renić A, Žalubovskis R, Dar'in D, Sharoyko V, Tennikova T, Pešić M, Krasavin M. Further exploration of DVD-445 as a lead thioredoxin reductase (TrxR) inhibitor for cancer therapy: Optimization of potency and evaluation of anticancer potential.. in European Journal of Medicinal Chemistry. 2020;191:112119.
doi:10.1016/j.ejmech.2020.112119 .

Jovanović, Mirna, Zhukovsky, Daniil, Podolski-Renić, Ana, Žalubovskis, Raivis, Dar'in, Dmitry, Sharoyko, Vladimir, Tennikova, Tatiana, Pešić, Milica, Krasavin, Mikhail, "Further exploration of DVD-445 as a lead thioredoxin reductase (TrxR) inhibitor for cancer therapy: Optimization of potency and evaluation of anticancer potential." in European Journal of Medicinal Chemistry, 191 (2020):112119,
https://doi.org/10.1016/j.ejmech.2020.112119 . .

TY  - JOUR
AU  - Jovanović, Mirna
AU  - Zhukovsky, Daniil
AU  - Podolski-Renić, Ana
AU  - Domračeva, Ilona
AU  - Žalubovskis, Raivis
AU  - Senćanski, Milan
AU  - Glišić, Sanja
AU  - Sharoyko, Vladimir
AU  - Tennikova, Tatiana
AU  - Dar'in, Dmitry
AU  - Pešić, Milica
AU  - Krasavin, Mikhail
PY  - 2019
UR  - https://www.sciencedirect.com/science/article/pii/S0223523419307147?via%3Dihub
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/3488
AB  - A series of peptidomimetic compounds incorporating an electrophilic moiety was synthesized using the Ugi reaction. These compounds (termed the Ugi Michael acceptors or UMAs) were designed to target the selenocysteine catalytic residue of thioredoxin reductase 1 (TrxR1), a promising cancer target. The compounds were assessed for their potential to inhibit TrxR1 using human neuroblastoma (SH-SY5Y) cell lysate. Based on this initial screening, six compounds were selected for testing against recombinant rat TrxR1 and in the insulin assay to reveal low-micromolar to submicromolar potency of these inhibitors. The same frontrunner compounds were evaluated for their ability to exert antiproliferative activity and induce cell death and this activity was compared to the UMA effects on the levels of reactive oxygen and nitrogen species (RONS). Collectively, the UMA compounds class presented itself as a rich source of leads for TrxR1 inhibitor discovery for anticancer application. Compound 7 (DVD-445) was nominated a lead for further optimization.
T2  - European Journal of Medicinal Chemistry
T1  - Novel electrophilic amides amenable by the Ugi reaction perturb thioredoxin system via thioredoxin reductase 1 (TrxR1) inhibition: Identification of DVD-445 as a new lead compound for anticancer therapy.
VL  - 181
DO  - 10.1016/j.ejmech.2019.111580
SP  - 111580
ER  - 

@article{
author = "Jovanović, Mirna and Zhukovsky, Daniil and Podolski-Renić, Ana and Domračeva, Ilona and Žalubovskis, Raivis and Senćanski, Milan and Glišić, Sanja and Sharoyko, Vladimir and Tennikova, Tatiana and Dar'in, Dmitry and Pešić, Milica and Krasavin, Mikhail",
year = "2019",
abstract = "A series of peptidomimetic compounds incorporating an electrophilic moiety was synthesized using the Ugi reaction. These compounds (termed the Ugi Michael acceptors or UMAs) were designed to target the selenocysteine catalytic residue of thioredoxin reductase 1 (TrxR1), a promising cancer target. The compounds were assessed for their potential to inhibit TrxR1 using human neuroblastoma (SH-SY5Y) cell lysate. Based on this initial screening, six compounds were selected for testing against recombinant rat TrxR1 and in the insulin assay to reveal low-micromolar to submicromolar potency of these inhibitors. The same frontrunner compounds were evaluated for their ability to exert antiproliferative activity and induce cell death and this activity was compared to the UMA effects on the levels of reactive oxygen and nitrogen species (RONS). Collectively, the UMA compounds class presented itself as a rich source of leads for TrxR1 inhibitor discovery for anticancer application. Compound 7 (DVD-445) was nominated a lead for further optimization.",
journal = "European Journal of Medicinal Chemistry",
title = "Novel electrophilic amides amenable by the Ugi reaction perturb thioredoxin system via thioredoxin reductase 1 (TrxR1) inhibition: Identification of DVD-445 as a new lead compound for anticancer therapy.",
volume = "181",
doi = "10.1016/j.ejmech.2019.111580",
pages = "111580"
}

Jovanović, M., Zhukovsky, D., Podolski-Renić, A., Domračeva, I., Žalubovskis, R., Senćanski, M., Glišić, S., Sharoyko, V., Tennikova, T., Dar'in, D., Pešić, M.,& Krasavin, M.. (2019). Novel electrophilic amides amenable by the Ugi reaction perturb thioredoxin system via thioredoxin reductase 1 (TrxR1) inhibition: Identification of DVD-445 as a new lead compound for anticancer therapy.. in European Journal of Medicinal Chemistry, 181, 111580.
https://doi.org/10.1016/j.ejmech.2019.111580

Jovanović M, Zhukovsky D, Podolski-Renić A, Domračeva I, Žalubovskis R, Senćanski M, Glišić S, Sharoyko V, Tennikova T, Dar'in D, Pešić M, Krasavin M. Novel electrophilic amides amenable by the Ugi reaction perturb thioredoxin system via thioredoxin reductase 1 (TrxR1) inhibition: Identification of DVD-445 as a new lead compound for anticancer therapy.. in European Journal of Medicinal Chemistry. 2019;181:111580.
doi:10.1016/j.ejmech.2019.111580 .

Jovanović, Mirna, Zhukovsky, Daniil, Podolski-Renić, Ana, Domračeva, Ilona, Žalubovskis, Raivis, Senćanski, Milan, Glišić, Sanja, Sharoyko, Vladimir, Tennikova, Tatiana, Dar'in, Dmitry, Pešić, Milica, Krasavin, Mikhail, "Novel electrophilic amides amenable by the Ugi reaction perturb thioredoxin system via thioredoxin reductase 1 (TrxR1) inhibition: Identification of DVD-445 as a new lead compound for anticancer therapy." in European Journal of Medicinal Chemistry, 181 (2019):111580,
https://doi.org/10.1016/j.ejmech.2019.111580 . .

TY  - JOUR
AU  - Podolski-Renić, Ana
AU  - Dinić, Jelena
AU  - Stanković, Tijana
AU  - Jovanović, Mirna
AU  - Ramović, Amra
AU  - Pustenko, Aleksandrs
AU  - Žalubovskis, Raivis
AU  - Pešić, Milica
PY  - 2019
UR  - https://www.sciencedirect.com/science/article/pii/S0928098719302751?dgcid=coauthor
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/3441
AB  - New 6-triazolyl-substituted sulfocoumarins were described as potent inhibitors of the transmembrane human carbonic anhydrase isoforms, CAIX and CAXII. These membrane associated enzymes that maintain pH and CO2 homeostasis are involved in cancer progression, invasion, and resistance to therapy. Recently, it was shown that CAXII expression associates with the expression of P-glycoprotein in multidrug resistant cancer cells. CAXII regulates P-glycoprotein activity by maintaining high intracellular pHi. In this study, the activity of three new sulfocoumarins was evaluated in three sensitive and corresponding multidrug resistant cancer cell lines with increased P-glycoprotein expression (non-small cell lung carcinoma, colorectal carcinoma and glioblastoma). Compound 3 showed the highest potential for cancer cell growth inhibition in all tested cell lines. Flow cytometric analyses showed that compound 3 induced intracellular acidification, cell cycle arrest in G2/M phase and necrosis in non-small cell lung carcinoma cells. Compound 3 demonstrated irreversible, concentration- and time-dependent inhibition of P-glycoprotein activity in multidrug resistant non-small cell lung carcinoma cells. The suppression of P-glycoprotein activity was accompanied with increased P-glycoprotein expression suggesting a compensatory mechanism of multidrug resistant cancer cells. In addition, compound 3 was able to sensitize multidrug resistant non-small cell lung carcinoma cells to doxorubicin. Overall, results imply that compound 3 has multidrug resistance modulating effect through intracellular acidification and subsequent inhibition of P-glycoprotein activity.
T2  - European Journal of Pharmaceutical Sciences
T1  - Sulfocoumarins, specific carbonic anhydrase IX and XII inhibitors, interact with cancer multidrug resistant phenotype through pH regulation and reverse P-glycoprotein mediated resistance.
VL  - 138
DO  - 10.1016/j.ejps.2019.105012
SP  - 105012
ER  - 

@article{
author = "Podolski-Renić, Ana and Dinić, Jelena and Stanković, Tijana and Jovanović, Mirna and Ramović, Amra and Pustenko, Aleksandrs and Žalubovskis, Raivis and Pešić, Milica",
year = "2019",
abstract = "New 6-triazolyl-substituted sulfocoumarins were described as potent inhibitors of the transmembrane human carbonic anhydrase isoforms, CAIX and CAXII. These membrane associated enzymes that maintain pH and CO2 homeostasis are involved in cancer progression, invasion, and resistance to therapy. Recently, it was shown that CAXII expression associates with the expression of P-glycoprotein in multidrug resistant cancer cells. CAXII regulates P-glycoprotein activity by maintaining high intracellular pHi. In this study, the activity of three new sulfocoumarins was evaluated in three sensitive and corresponding multidrug resistant cancer cell lines with increased P-glycoprotein expression (non-small cell lung carcinoma, colorectal carcinoma and glioblastoma). Compound 3 showed the highest potential for cancer cell growth inhibition in all tested cell lines. Flow cytometric analyses showed that compound 3 induced intracellular acidification, cell cycle arrest in G2/M phase and necrosis in non-small cell lung carcinoma cells. Compound 3 demonstrated irreversible, concentration- and time-dependent inhibition of P-glycoprotein activity in multidrug resistant non-small cell lung carcinoma cells. The suppression of P-glycoprotein activity was accompanied with increased P-glycoprotein expression suggesting a compensatory mechanism of multidrug resistant cancer cells. In addition, compound 3 was able to sensitize multidrug resistant non-small cell lung carcinoma cells to doxorubicin. Overall, results imply that compound 3 has multidrug resistance modulating effect through intracellular acidification and subsequent inhibition of P-glycoprotein activity.",
journal = "European Journal of Pharmaceutical Sciences",
title = "Sulfocoumarins, specific carbonic anhydrase IX and XII inhibitors, interact with cancer multidrug resistant phenotype through pH regulation and reverse P-glycoprotein mediated resistance.",
volume = "138",
doi = "10.1016/j.ejps.2019.105012",
pages = "105012"
}

Podolski-Renić, A., Dinić, J., Stanković, T., Jovanović, M., Ramović, A., Pustenko, A., Žalubovskis, R.,& Pešić, M.. (2019). Sulfocoumarins, specific carbonic anhydrase IX and XII inhibitors, interact with cancer multidrug resistant phenotype through pH regulation and reverse P-glycoprotein mediated resistance.. in European Journal of Pharmaceutical Sciences, 138, 105012.
https://doi.org/10.1016/j.ejps.2019.105012

Podolski-Renić A, Dinić J, Stanković T, Jovanović M, Ramović A, Pustenko A, Žalubovskis R, Pešić M. Sulfocoumarins, specific carbonic anhydrase IX and XII inhibitors, interact with cancer multidrug resistant phenotype through pH regulation and reverse P-glycoprotein mediated resistance.. in European Journal of Pharmaceutical Sciences. 2019;138:105012.
doi:10.1016/j.ejps.2019.105012 .

Podolski-Renić, Ana, Dinić, Jelena, Stanković, Tijana, Jovanović, Mirna, Ramović, Amra, Pustenko, Aleksandrs, Žalubovskis, Raivis, Pešić, Milica, "Sulfocoumarins, specific carbonic anhydrase IX and XII inhibitors, interact with cancer multidrug resistant phenotype through pH regulation and reverse P-glycoprotein mediated resistance." in European Journal of Pharmaceutical Sciences, 138 (2019):105012,
https://doi.org/10.1016/j.ejps.2019.105012 . .

TY  - JOUR
AU  - Bakulina, Olga
AU  - Bannykh, Anton
AU  - Jovanović, Mirna
AU  - Domračeva, Ilona
AU  - Podolski-Renić, Ana
AU  - Žalubovskis, Raivis
AU  - Pešić, Milica
AU  - Dar'in, Dmitry
AU  - Krasavin, Mikhail
PY  - 2019
UR  - https://www.tandfonline.com/doi/full/10.1080/14756366.2019.1575372
UR  - http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=PMC6374954
UR  - https://radar.ibiss.bg.ac.rs/handle/123456789/3266
AB  - Human thioredoxin reductase 1 (TrxR1) is a selenocysteine-containing enzyme which plays a crucial role in regulating numerous redox signalling pathways within the cell. While its functioning is important in all cells, levels of TrxR1 expression are higher in cancer cells, possibly as an adaptation to much higher levels of reactive oxygen species and the need for more extensive DNA synthesis. This makes TrxR1 an attractive target for cancer therapy development. Inspired by the structure of disulphide compounds which have advanced through various stages of clinical development, we designed a series of dithiodiglycolic acid derivatives. These were prepared from respective thiol synthons using an iodine- or benzotriazolyl chloride-promoted oxidative disulphide bond formation. Inhibition of TrxR present in cell lysates from human neuroblastoma cells (SH-SY5Y) and rat liver cells indicated several compounds with a potential for TrxR inhibition. Some of these compounds were also tested for growth inhibition against two human cancer cell lines and normal human keratinocytes.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - Design, synthesis, and biological evaluation of novel derivatives of dithiodiglycolic acid prepared via oxidative coupling of thiols.
IS  - 1
VL  - 34
DO  - 10.1080/14756366.2019.1575372
SP  - 665
EP  - 671
ER  - 

@article{
author = "Bakulina, Olga and Bannykh, Anton and Jovanović, Mirna and Domračeva, Ilona and Podolski-Renić, Ana and Žalubovskis, Raivis and Pešić, Milica and Dar'in, Dmitry and Krasavin, Mikhail",
year = "2019",
abstract = "Human thioredoxin reductase 1 (TrxR1) is a selenocysteine-containing enzyme which plays a crucial role in regulating numerous redox signalling pathways within the cell. While its functioning is important in all cells, levels of TrxR1 expression are higher in cancer cells, possibly as an adaptation to much higher levels of reactive oxygen species and the need for more extensive DNA synthesis. This makes TrxR1 an attractive target for cancer therapy development. Inspired by the structure of disulphide compounds which have advanced through various stages of clinical development, we designed a series of dithiodiglycolic acid derivatives. These were prepared from respective thiol synthons using an iodine- or benzotriazolyl chloride-promoted oxidative disulphide bond formation. Inhibition of TrxR present in cell lysates from human neuroblastoma cells (SH-SY5Y) and rat liver cells indicated several compounds with a potential for TrxR inhibition. Some of these compounds were also tested for growth inhibition against two human cancer cell lines and normal human keratinocytes.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "Design, synthesis, and biological evaluation of novel derivatives of dithiodiglycolic acid prepared via oxidative coupling of thiols.",
number = "1",
volume = "34",
doi = "10.1080/14756366.2019.1575372",
pages = "665-671"
}

Bakulina, O., Bannykh, A., Jovanović, M., Domračeva, I., Podolski-Renić, A., Žalubovskis, R., Pešić, M., Dar'in, D.,& Krasavin, M.. (2019). Design, synthesis, and biological evaluation of novel derivatives of dithiodiglycolic acid prepared via oxidative coupling of thiols.. in Journal of Enzyme Inhibition and Medicinal Chemistry, 34(1), 665-671.
https://doi.org/10.1080/14756366.2019.1575372

Bakulina O, Bannykh A, Jovanović M, Domračeva I, Podolski-Renić A, Žalubovskis R, Pešić M, Dar'in D, Krasavin M. Design, synthesis, and biological evaluation of novel derivatives of dithiodiglycolic acid prepared via oxidative coupling of thiols.. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2019;34(1):665-671.
doi:10.1080/14756366.2019.1575372 .

Bakulina, Olga, Bannykh, Anton, Jovanović, Mirna, Domračeva, Ilona, Podolski-Renić, Ana, Žalubovskis, Raivis, Pešić, Milica, Dar'in, Dmitry, Krasavin, Mikhail, "Design, synthesis, and biological evaluation of novel derivatives of dithiodiglycolic acid prepared via oxidative coupling of thiols." in Journal of Enzyme Inhibition and Medicinal Chemistry, 34, no. 1 (2019):665-671,
https://doi.org/10.1080/14756366.2019.1575372 . .