TY  - JOUR
AU  - Matošević, Ana
AU  - Opsenica, Dejan
AU  - Spasić, Marta
AU  - Maraković, Nikola
AU  - Zandona, Antonio
AU  - Žunec, Suzana
AU  - Bartolić, Marija
AU  - Kovarik, Zrinka
AU  - Bosak, Anita
PY  - 2023
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/7159
AB  - The most successful therapeutic strategy in the treatment of Alzheimer's disease (AD) is directed toward increasing levels of the neurotransmitter acetylcholine (ACh) by inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), the enzymes responsible for its hydrolysis. In this paper, we extended our study on 4-aminoquinolines as human cholinesterase inhibitors on twenty-six new 4-aminoquinolines containing an n-octylamino spacer on C(4) and different substituents on the terminal amino group. We evaluated the potency of new derivatives to act as multi-targeted ligands by determining their inhibition potency towards human AChE and BChE, ability to chelate biometals Fe, Cu and Zn, ability to inhibit the action of β-secretase 1 (BACE1) and their antioxidant capacity. All of the tested derivatives were very potent inhibitors of human AChE and BChE with inhibition constants (Ki) ranging from 0.0023 to 1.6 μM. Most of the compounds were estimated to be able to cross the blood-brain barrier (BBB) by passive transport and were nontoxic to human neuronal, kidney and liver cells in concentrations in which they inhibit cholinesterases. Generally, newly synthesised compounds were weak reductants compared to standard antioxidants, but all possessed a certain amount of antioxidant activity compared to tacrine. Of the eleven most potent cholinesterase inhibitors, eight compounds also inhibited BACE1 activity at 10–18%. Based on our overall results, compounds 8 with 3-fluorobenzyl, 11 with 3-chlorobenzyl and 17 with 3-metoxy benzyl substituents on the terminal amino group stood out as the most promising for the treatment of AD; they strongly inhibited AChE and BChE, were non-toxic on HepG2, HEK293 and SH-SY5Y cells, had the potential to cross the BBB and possessed the ability to chelate biometals and/or inhibit the activity of BACE1 within a range close to the therapeutically desired degree of inhibition.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Evaluation of 4-aminoquinoline derivatives with an n-octylamino spacer as potential multi-targeting ligands for the treatment of Alzheimer's disease
VL  - 382
SP  - 110620
DO  - 10.1016/j.cbi.2023.110620
ER  - 

@article{
author = "Matošević, Ana and Opsenica, Dejan and Spasić, Marta and Maraković, Nikola and Zandona, Antonio and Žunec, Suzana and Bartolić, Marija and Kovarik, Zrinka and Bosak, Anita",
year = "2023",
abstract = "The most successful therapeutic strategy in the treatment of Alzheimer's disease (AD) is directed toward increasing levels of the neurotransmitter acetylcholine (ACh) by inhibition of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), the enzymes responsible for its hydrolysis. In this paper, we extended our study on 4-aminoquinolines as human cholinesterase inhibitors on twenty-six new 4-aminoquinolines containing an n-octylamino spacer on C(4) and different substituents on the terminal amino group. We evaluated the potency of new derivatives to act as multi-targeted ligands by determining their inhibition potency towards human AChE and BChE, ability to chelate biometals Fe, Cu and Zn, ability to inhibit the action of β-secretase 1 (BACE1) and their antioxidant capacity. All of the tested derivatives were very potent inhibitors of human AChE and BChE with inhibition constants (Ki) ranging from 0.0023 to 1.6 μM. Most of the compounds were estimated to be able to cross the blood-brain barrier (BBB) by passive transport and were nontoxic to human neuronal, kidney and liver cells in concentrations in which they inhibit cholinesterases. Generally, newly synthesised compounds were weak reductants compared to standard antioxidants, but all possessed a certain amount of antioxidant activity compared to tacrine. Of the eleven most potent cholinesterase inhibitors, eight compounds also inhibited BACE1 activity at 10–18%. Based on our overall results, compounds 8 with 3-fluorobenzyl, 11 with 3-chlorobenzyl and 17 with 3-metoxy benzyl substituents on the terminal amino group stood out as the most promising for the treatment of AD; they strongly inhibited AChE and BChE, were non-toxic on HepG2, HEK293 and SH-SY5Y cells, had the potential to cross the BBB and possessed the ability to chelate biometals and/or inhibit the activity of BACE1 within a range close to the therapeutically desired degree of inhibition.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Evaluation of 4-aminoquinoline derivatives with an n-octylamino spacer as potential multi-targeting ligands for the treatment of Alzheimer's disease",
volume = "382",
pages = "110620",
doi = "10.1016/j.cbi.2023.110620"
}

Matošević, A., Opsenica, D., Spasić, M., Maraković, N., Zandona, A., Žunec, S., Bartolić, M., Kovarik, Z.,& Bosak, A.. (2023). Evaluation of 4-aminoquinoline derivatives with an n-octylamino spacer as potential multi-targeting ligands for the treatment of Alzheimer's disease. in Chemico-Biological Interactions
Elsevier., 382, 110620.
https://doi.org/10.1016/j.cbi.2023.110620

Matošević A, Opsenica D, Spasić M, Maraković N, Zandona A, Žunec S, Bartolić M, Kovarik Z, Bosak A. Evaluation of 4-aminoquinoline derivatives with an n-octylamino spacer as potential multi-targeting ligands for the treatment of Alzheimer's disease. in Chemico-Biological Interactions. 2023;382:110620.
doi:10.1016/j.cbi.2023.110620 .

Matošević, Ana, Opsenica, Dejan, Spasić, Marta, Maraković, Nikola, Zandona, Antonio, Žunec, Suzana, Bartolić, Marija, Kovarik, Zrinka, Bosak, Anita, "Evaluation of 4-aminoquinoline derivatives with an n-octylamino spacer as potential multi-targeting ligands for the treatment of Alzheimer's disease" in Chemico-Biological Interactions, 382 (2023):110620,
https://doi.org/10.1016/j.cbi.2023.110620 . .

TY  - JOUR
AU  - Komatović, Katarina
AU  - Matošević, Ana
AU  - Terzić-Jovanović, Nataša
AU  - Žunec, Suzana
AU  - Šegan, Sandra
AU  - Zlatović, Mario
AU  - Maraković, Nikola
AU  - Bosak, Anita
AU  - Opsenica, Dejan
PY  - 2022
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/5232
AB  - Considering that acetylcholinesterase (AChE) inhibition is the most important mode of action expected of a potential drug used for the treatment of symptoms of Alzheimer’s disease (AD), our previous pilot study of 4-aminoquinolines as potential human cholinesterase inhibitors was extended to twenty-two new structurally distinct 4-aminoquinolines bearing an adamantane moiety. Inhibition studies revealed that all of the compounds were very potent inhibitors of AChE and butyrylcholinesterase (BChE), with inhibition constants (Ki) ranging between 0.075 and 25 µM. The tested compounds exhibited a modest selectivity between the two cholinesterases; the most selective for BChE was compound 14, which displayed a 10 times higher preference, while compound 19 was a 5.8 times more potent inhibitor of AChE. Most of the compounds were estimated to be able to cross the blood–brain barrier (BBB) by passive transport. Evaluation of druglikeness singled out fourteen compounds with possible oral route of administration. The tested compounds displayed modest but generally higher antioxidant activity than the structurally similar AD drug tacrine. Compound 19 showed the highest reducing power, comparable to those of standard antioxidants. Considering their simple structure, high inhibition of AChE and BChE, and ability to cross the BBB, 4-aminoquinoline-based adamantanes show promise as structural scaffolds for further design of novel central nervous system drugs. Among them, two compounds stand out: compound 5 as the most potent inhibitor of both cholinesterases with a Ki constant in low nano molar range and the potential to cross the BBB, and compound 8, which met all our requirements, including high cholinesterase inhibition, good oral bioavailability, and antioxidative effect. The QSAR model revealed that AChE and BChE inhibition was mainly influenced by the ring and topological descriptors MCD, Nnum, RP, and RSIpw3, which defined the shape, conformational flexibility, and surface properties of the molecules
PB  - MDPI
T2  - Pharmaceutics
T1  - 4-Aminoquinoline-Based Adamantanes as Potential Anticholinesterase Agents in Symptomatic Treatment of Alzheimer’s Disease
VL  - 14
IS  - 6
SP  - 1305
DO  - 10.3390/pharmaceutics14061305
ER  - 

@article{
author = "Komatović, Katarina and Matošević, Ana and Terzić-Jovanović, Nataša and Žunec, Suzana and Šegan, Sandra and Zlatović, Mario and Maraković, Nikola and Bosak, Anita and Opsenica, Dejan",
year = "2022",
abstract = "Considering that acetylcholinesterase (AChE) inhibition is the most important mode of action expected of a potential drug used for the treatment of symptoms of Alzheimer’s disease (AD), our previous pilot study of 4-aminoquinolines as potential human cholinesterase inhibitors was extended to twenty-two new structurally distinct 4-aminoquinolines bearing an adamantane moiety. Inhibition studies revealed that all of the compounds were very potent inhibitors of AChE and butyrylcholinesterase (BChE), with inhibition constants (Ki) ranging between 0.075 and 25 µM. The tested compounds exhibited a modest selectivity between the two cholinesterases; the most selective for BChE was compound 14, which displayed a 10 times higher preference, while compound 19 was a 5.8 times more potent inhibitor of AChE. Most of the compounds were estimated to be able to cross the blood–brain barrier (BBB) by passive transport. Evaluation of druglikeness singled out fourteen compounds with possible oral route of administration. The tested compounds displayed modest but generally higher antioxidant activity than the structurally similar AD drug tacrine. Compound 19 showed the highest reducing power, comparable to those of standard antioxidants. Considering their simple structure, high inhibition of AChE and BChE, and ability to cross the BBB, 4-aminoquinoline-based adamantanes show promise as structural scaffolds for further design of novel central nervous system drugs. Among them, two compounds stand out: compound 5 as the most potent inhibitor of both cholinesterases with a Ki constant in low nano molar range and the potential to cross the BBB, and compound 8, which met all our requirements, including high cholinesterase inhibition, good oral bioavailability, and antioxidative effect. The QSAR model revealed that AChE and BChE inhibition was mainly influenced by the ring and topological descriptors MCD, Nnum, RP, and RSIpw3, which defined the shape, conformational flexibility, and surface properties of the molecules",
publisher = "MDPI",
journal = "Pharmaceutics",
title = "4-Aminoquinoline-Based Adamantanes as Potential Anticholinesterase Agents in Symptomatic Treatment of Alzheimer’s Disease",
volume = "14",
number = "6",
pages = "1305",
doi = "10.3390/pharmaceutics14061305"
}

Komatović, K., Matošević, A., Terzić-Jovanović, N., Žunec, S., Šegan, S., Zlatović, M., Maraković, N., Bosak, A.,& Opsenica, D.. (2022). 4-Aminoquinoline-Based Adamantanes as Potential Anticholinesterase Agents in Symptomatic Treatment of Alzheimer’s Disease. in Pharmaceutics
MDPI., 14(6), 1305.
https://doi.org/10.3390/pharmaceutics14061305

Komatović K, Matošević A, Terzić-Jovanović N, Žunec S, Šegan S, Zlatović M, Maraković N, Bosak A, Opsenica D. 4-Aminoquinoline-Based Adamantanes as Potential Anticholinesterase Agents in Symptomatic Treatment of Alzheimer’s Disease. in Pharmaceutics. 2022;14(6):1305.
doi:10.3390/pharmaceutics14061305 .

Komatović, Katarina, Matošević, Ana, Terzić-Jovanović, Nataša, Žunec, Suzana, Šegan, Sandra, Zlatović, Mario, Maraković, Nikola, Bosak, Anita, Opsenica, Dejan, "4-Aminoquinoline-Based Adamantanes as Potential Anticholinesterase Agents in Symptomatic Treatment of Alzheimer’s Disease" in Pharmaceutics, 14, no. 6 (2022):1305,
https://doi.org/10.3390/pharmaceutics14061305 . .

TY  - JOUR
AU  - Bosak, Anita
AU  - Opsenica, Dejan
AU  - Šinko, Goran
AU  - Zlatar, Matija
AU  - Kovarik, Zrinka
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2886
AB  - Eight derivatives of 4-aminoquinolines differing in the substituents attached to the C(4)-amino group and C(7)were synthesised and tested as inhibitors of human acetylcholinesterase (AChE)and butyrylcholinesterase (BChE). Both enzymes were inhibited by all of the compounds with inhibition constants (K i )ranging from 0.50 to 50 μM exhibiting slight selectivity toward AChE over BChE. The most potent inhibitors of AChE were compounds with an n-octylamino chain or adamantyl group. The shortening of the chain length resulted in a decrease in AChE inhibition by 5–20 times. Docking studies revealed that the quinoline group within the AChE active site was positioned in the choline binding site, while the C(4)-amino group substituents, depending on their lipophilicity, could establish hydrogen bonds or π-interactions with residues of the peripheral anionic site. The most potent inhibitors of BChE were compounds with the most voluminous substituent on C(4)-amino group (adamantyl)or those with a stronger electron withdrawing substituent on C(7)(trifluormethyl group). Based on AChE inhibition, compounds with an n-octylamino chain or adamantyl substituent were shown to possess the capacity for further development as potential drugs for treatment of neurodegenerative diseases. © 2019 Elsevier B.V.
PB  - Elsevier Ireland Ltd
T2  - Chemico-Biological Interactions
T1  - Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase
VL  - 308
SP  - 101
EP  - 109
DO  - 10.1016/j.cbi.2019.05.024
ER  - 

@article{
author = "Bosak, Anita and Opsenica, Dejan and Šinko, Goran and Zlatar, Matija and Kovarik, Zrinka",
year = "2019",
abstract = "Eight derivatives of 4-aminoquinolines differing in the substituents attached to the C(4)-amino group and C(7)were synthesised and tested as inhibitors of human acetylcholinesterase (AChE)and butyrylcholinesterase (BChE). Both enzymes were inhibited by all of the compounds with inhibition constants (K i )ranging from 0.50 to 50 μM exhibiting slight selectivity toward AChE over BChE. The most potent inhibitors of AChE were compounds with an n-octylamino chain or adamantyl group. The shortening of the chain length resulted in a decrease in AChE inhibition by 5–20 times. Docking studies revealed that the quinoline group within the AChE active site was positioned in the choline binding site, while the C(4)-amino group substituents, depending on their lipophilicity, could establish hydrogen bonds or π-interactions with residues of the peripheral anionic site. The most potent inhibitors of BChE were compounds with the most voluminous substituent on C(4)-amino group (adamantyl)or those with a stronger electron withdrawing substituent on C(7)(trifluormethyl group). Based on AChE inhibition, compounds with an n-octylamino chain or adamantyl substituent were shown to possess the capacity for further development as potential drugs for treatment of neurodegenerative diseases. © 2019 Elsevier B.V.",
publisher = "Elsevier Ireland Ltd",
journal = "Chemico-Biological Interactions",
title = "Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase",
volume = "308",
pages = "101-109",
doi = "10.1016/j.cbi.2019.05.024"
}

Bosak, A., Opsenica, D., Šinko, G., Zlatar, M.,& Kovarik, Z.. (2019). Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase. in Chemico-Biological Interactions
Elsevier Ireland Ltd., 308, 101-109.
https://doi.org/10.1016/j.cbi.2019.05.024

Bosak A, Opsenica D, Šinko G, Zlatar M, Kovarik Z. Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase. in Chemico-Biological Interactions. 2019;308:101-109.
doi:10.1016/j.cbi.2019.05.024 .

Bosak, Anita, Opsenica, Dejan, Šinko, Goran, Zlatar, Matija, Kovarik, Zrinka, "Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase" in Chemico-Biological Interactions, 308 (2019):101-109,
https://doi.org/10.1016/j.cbi.2019.05.024 . .

TY  - JOUR
AU  - Bosak, Anita
AU  - Opsenica, Dejan
AU  - Šinko, Goran
AU  - Zlatar, Matija
AU  - Kovarik, Zrinka
PY  - 2019
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2905
AB  - Eight derivatives of 4-aminoquinolines differing in the substituents attached to the C(4)-amino group and C(7)were synthesised and tested as inhibitors of human acetylcholinesterase (AChE)and butyrylcholinesterase (BChE). Both enzymes were inhibited by all of the compounds with inhibition constants (K i )ranging from 0.50 to 50 μM exhibiting slight selectivity toward AChE over BChE. The most potent inhibitors of AChE were compounds with an n-octylamino chain or adamantyl group. The shortening of the chain length resulted in a decrease in AChE inhibition by 5–20 times. Docking studies revealed that the quinoline group within the AChE active site was positioned in the choline binding site, while the C(4)-amino group substituents, depending on their lipophilicity, could establish hydrogen bonds or π-interactions with residues of the peripheral anionic site. The most potent inhibitors of BChE were compounds with the most voluminous substituent on C(4)-amino group (adamantyl)or those with a stronger electron withdrawing substituent on C(7)(trifluormethyl group). Based on AChE inhibition, compounds with an n-octylamino chain or adamantyl substituent were shown to possess the capacity for further development as potential drugs for treatment of neurodegenerative diseases. © 2019 Elsevier B.V.
PB  - Elsevier Ireland Ltd
T2  - Chemico-Biological Interactions
T1  - Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase
VL  - 308
SP  - 101
EP  - 109
DO  - 10.1016/j.cbi.2019.05.024
ER  - 

@article{
author = "Bosak, Anita and Opsenica, Dejan and Šinko, Goran and Zlatar, Matija and Kovarik, Zrinka",
year = "2019",
abstract = "Eight derivatives of 4-aminoquinolines differing in the substituents attached to the C(4)-amino group and C(7)were synthesised and tested as inhibitors of human acetylcholinesterase (AChE)and butyrylcholinesterase (BChE). Both enzymes were inhibited by all of the compounds with inhibition constants (K i )ranging from 0.50 to 50 μM exhibiting slight selectivity toward AChE over BChE. The most potent inhibitors of AChE were compounds with an n-octylamino chain or adamantyl group. The shortening of the chain length resulted in a decrease in AChE inhibition by 5–20 times. Docking studies revealed that the quinoline group within the AChE active site was positioned in the choline binding site, while the C(4)-amino group substituents, depending on their lipophilicity, could establish hydrogen bonds or π-interactions with residues of the peripheral anionic site. The most potent inhibitors of BChE were compounds with the most voluminous substituent on C(4)-amino group (adamantyl)or those with a stronger electron withdrawing substituent on C(7)(trifluormethyl group). Based on AChE inhibition, compounds with an n-octylamino chain or adamantyl substituent were shown to possess the capacity for further development as potential drugs for treatment of neurodegenerative diseases. © 2019 Elsevier B.V.",
publisher = "Elsevier Ireland Ltd",
journal = "Chemico-Biological Interactions",
title = "Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase",
volume = "308",
pages = "101-109",
doi = "10.1016/j.cbi.2019.05.024"
}

Bosak, A., Opsenica, D., Šinko, G., Zlatar, M.,& Kovarik, Z.. (2019). Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase. in Chemico-Biological Interactions
Elsevier Ireland Ltd., 308, 101-109.
https://doi.org/10.1016/j.cbi.2019.05.024

Bosak A, Opsenica D, Šinko G, Zlatar M, Kovarik Z. Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase. in Chemico-Biological Interactions. 2019;308:101-109.
doi:10.1016/j.cbi.2019.05.024 .

Bosak, Anita, Opsenica, Dejan, Šinko, Goran, Zlatar, Matija, Kovarik, Zrinka, "Structural aspects of 4-aminoquinolines as reversible inhibitors of human acetylcholinesterase and butyrylcholinesterase" in Chemico-Biological Interactions, 308 (2019):101-109,
https://doi.org/10.1016/j.cbi.2019.05.024 . .

TY  - CONF
AU  - Bosak, Anita
AU  - Opsenica, Dejan
AU  - Šinko, Goran
AU  - Zlatar, Matija
AU  - Kovarik, Zrinka
PY  - 2018
UR  - https://mmsl.cz/artkey/mms-201888-0083.php
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/3216
AB  - We synthesised eight derivatives of 4-aminoquinolines differing in the substituents attached to the C(4)-amino group and C(7) carbon of 4-aminoquinoline, and tested their potency to inhibit human AChE and BChE. All of the compounds reversibly inhibited both enzymes with dissociation inhibition (Ki) constants from 0.50 to 50 µM exhibiting selectivity. In other words, for all compounds, AChE exhibited higher affinity than BChE. The most potent inhibitors of AChE were compounds with an octyl chain or adamantane, regardless of the group in position C(7). The shortening of the chain length caused the AChE inhibition decrease by 5-20 times. Docking studies made it clear that the high AChE affinity resulted from simultaneous interactions of the quinoline group with aromatic residues of both the catalytic active site and the peripheral site. In conclusion, the inhibition potency and selectivity classify several novel compounds as leads for further modification and optimization towards the development of new inhibitors of AChE and potential drugs for treatment of neurodegenerative diseases.
PB  - Faculty of Military Health Sciences, Czech Republic
C3  - Military Medical Science Letters
T1  - 4-Aminoqionolines as reversible inhibitors of human cholinesterase activity
VL  - 87
IS  - Suppl. 1
SP  - 83
EP  - 83
UR  - https://hdl.handle.net/21.15107/rcub_cer_3216
ER  - 

@conference{
author = "Bosak, Anita and Opsenica, Dejan and Šinko, Goran and Zlatar, Matija and Kovarik, Zrinka",
year = "2018",
abstract = "We synthesised eight derivatives of 4-aminoquinolines differing in the substituents attached to the C(4)-amino group and C(7) carbon of 4-aminoquinoline, and tested their potency to inhibit human AChE and BChE. All of the compounds reversibly inhibited both enzymes with dissociation inhibition (Ki) constants from 0.50 to 50 µM exhibiting selectivity. In other words, for all compounds, AChE exhibited higher affinity than BChE. The most potent inhibitors of AChE were compounds with an octyl chain or adamantane, regardless of the group in position C(7). The shortening of the chain length caused the AChE inhibition decrease by 5-20 times. Docking studies made it clear that the high AChE affinity resulted from simultaneous interactions of the quinoline group with aromatic residues of both the catalytic active site and the peripheral site. In conclusion, the inhibition potency and selectivity classify several novel compounds as leads for further modification and optimization towards the development of new inhibitors of AChE and potential drugs for treatment of neurodegenerative diseases.",
publisher = "Faculty of Military Health Sciences, Czech Republic",
journal = "Military Medical Science Letters",
title = "4-Aminoqionolines as reversible inhibitors of human cholinesterase activity",
volume = "87",
number = "Suppl. 1",
pages = "83-83",
url = "https://hdl.handle.net/21.15107/rcub_cer_3216"
}

Bosak, A., Opsenica, D., Šinko, G., Zlatar, M.,& Kovarik, Z.. (2018). 4-Aminoqionolines as reversible inhibitors of human cholinesterase activity. in Military Medical Science Letters
Faculty of Military Health Sciences, Czech Republic., 87(Suppl. 1), 83-83.
https://hdl.handle.net/21.15107/rcub_cer_3216

Bosak A, Opsenica D, Šinko G, Zlatar M, Kovarik Z. 4-Aminoqionolines as reversible inhibitors of human cholinesterase activity. in Military Medical Science Letters. 2018;87(Suppl. 1):83-83.
https://hdl.handle.net/21.15107/rcub_cer_3216 .

Bosak, Anita, Opsenica, Dejan, Šinko, Goran, Zlatar, Matija, Kovarik, Zrinka, "4-Aminoqionolines as reversible inhibitors of human cholinesterase activity" in Military Medical Science Letters, 87, no. Suppl. 1 (2018):83-83,
https://hdl.handle.net/21.15107/rcub_cer_3216 .