TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Smiljanić, Katarina
AU  - Takić, Marija
AU  - Sarac, Ivana
AU  - Petovic-Oggiano, Gordana
AU  - Nikolić, Milan
AU  - Jovanović, Vesna B.
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6429
AB  - The binding of ubiquitous serum ligands (free fatty acids) to human serum albumin (HSA)
or its glycation can affect thiol group reactivity, thus influencing its antioxidant activity. The effects
of stearic acid (SA) and glucose binding on HSA structural changes and thiol group content and
reactivity were monitored by fluoroscopy and the Ellman method during a 14-day incubation in
molar ratios to HSA that mimic pathophysiological conditions. Upon incubation with 5 mM glucose,
HSA glycation was the same as HSA without it, in three different HSA:SA molar ratios (HSA:SA-
1:1-2-4). The protective effect of SA on the antioxidant property of HSA under different glucose
regimes (5-10-20 mM) was significantly affected by molar ratios of HSA:SA. Thiol reactivity was fully
restored with 5–20 mM glucose at a 1:1 HSA:SA ratio, while the highest thiol content recovery was in
pathological glucose regimes at a 1:1 HSA:SA ratio. The SA affinity for HSA increased significantly
(1.5- and 1.3-fold, p < 0.01) with 5 and 10 mM glucose compared to the control. These results deepen
the knowledge about the possible regulation of the antioxidant role of HSA in diabetes and other
pathophysiological conditions and enable the design of future HSA-drug studies which, in turn, is
important for clinicians when designing information-based treatments.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding
VL  - 5
SP  - 2335
DO  - 10.3390/ijms25042335
ER  - 

@article{
author = "Uzelac, Tamara N. and Smiljanić, Katarina and Takić, Marija and Sarac, Ivana and Petovic-Oggiano, Gordana and Nikolić, Milan and Jovanović, Vesna B.",
year = "2024",
abstract = "The binding of ubiquitous serum ligands (free fatty acids) to human serum albumin (HSA)
or its glycation can affect thiol group reactivity, thus influencing its antioxidant activity. The effects
of stearic acid (SA) and glucose binding on HSA structural changes and thiol group content and
reactivity were monitored by fluoroscopy and the Ellman method during a 14-day incubation in
molar ratios to HSA that mimic pathophysiological conditions. Upon incubation with 5 mM glucose,
HSA glycation was the same as HSA without it, in three different HSA:SA molar ratios (HSA:SA-
1:1-2-4). The protective effect of SA on the antioxidant property of HSA under different glucose
regimes (5-10-20 mM) was significantly affected by molar ratios of HSA:SA. Thiol reactivity was fully
restored with 5–20 mM glucose at a 1:1 HSA:SA ratio, while the highest thiol content recovery was in
pathological glucose regimes at a 1:1 HSA:SA ratio. The SA affinity for HSA increased significantly
(1.5- and 1.3-fold, p < 0.01) with 5 and 10 mM glucose compared to the control. These results deepen
the knowledge about the possible regulation of the antioxidant role of HSA in diabetes and other
pathophysiological conditions and enable the design of future HSA-drug studies which, in turn, is
important for clinicians when designing information-based treatments.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding",
volume = "5",
pages = "2335",
doi = "10.3390/ijms25042335"
}

Uzelac, T. N., Smiljanić, K., Takić, M., Sarac, I., Petovic-Oggiano, G., Nikolić, M.,& Jovanović, V. B.. (2024). The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding. in International Journal of Molecular Sciences
MDPI., 5, 2335.
https://doi.org/10.3390/ijms25042335

Uzelac TN, Smiljanić K, Takić M, Sarac I, Petovic-Oggiano G, Nikolić M, Jovanović VB. The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding. in International Journal of Molecular Sciences. 2024;5:2335.
doi:10.3390/ijms25042335 .

Uzelac, Tamara N., Smiljanić, Katarina, Takić, Marija, Sarac, Ivana, Petovic-Oggiano, Gordana, Nikolić, Milan, Jovanović, Vesna B., "The Thiol Group Reactivity and the Antioxidant Property of Human Serum Albumin Are Controlled by the Joint Action of Fatty Acids and Glucose Binding" in International Journal of Molecular Sciences, 5 (2024):2335,
https://doi.org/10.3390/ijms25042335 . .

TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3333
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
SP  - 1
EP  - 7
DO  - 10.1016/j.cbi.2019.108787
ER  - 

@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
pages = "1-7",
doi = "10.1016/j.cbi.2019.108787"
}

Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions, 311, 1-7.
https://doi.org/10.1016/j.cbi.2019.108787

Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311:1-7.
doi:10.1016/j.cbi.2019.108787 .

Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311 (2019):1-7,
https://doi.org/10.1016/j.cbi.2019.108787 . .

TY  - DATA
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3335
T2  - Chemico-Biological Interactions
T1  - Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3335
ER  - 

@misc{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
journal = "Chemico-Biological Interactions",
title = "Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3335"
}

Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787. in Chemico-Biological Interactions.
https://hdl.handle.net/21.15107/rcub_cherry_3335

Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787. in Chemico-Biological Interactions. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_3335 .

Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Supplementary data for the article: Uzelac, T. N.; Nikolić-Kokić, A. L.; Spasić, S. D.; Mačvanin, M. T.; Nikolić, M. R.; Mandić, L. M.; Jovanović, V. B. Opposite Clozapine and Ziprasidone Effects on the Reactivity of Plasma Albumin SH-Group Are the Consequence of Their Different Binding Properties Dependent on Protein Fatty Acids Content. Chemico-Biological Interactions 2019, 311. https://doi.org/10.1016/j.cbi.2019.108787" in Chemico-Biological Interactions (2019),
https://hdl.handle.net/21.15107/rcub_cherry_3335 .

TY  - JOUR
AU  - Uzelac, Tamara N.
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Mačvanin, Mirjana T.
AU  - Nikolić, Milan
AU  - Mandić, Ljuba M.
AU  - Jovanović, Vesna B.
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3865
AB  - Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.
PB  - Elsevier
T2  - Chemico-Biological Interactions
T1  - Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content
VL  - 311
IS  - 108787
DO  - 10.1016/j.cbi.2019.108787
ER  - 

@article{
author = "Uzelac, Tamara N. and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Mačvanin, Mirjana T. and Nikolić, Milan and Mandić, Ljuba M. and Jovanović, Vesna B.",
year = "2019",
abstract = "Antipsychotic drugs interfere with the antioxidant defense system provoking complex and often toxicological effects. Here we examined differences in plasma albumin reduced free thiol (SH) group content and its reactivity as a consequence of clozapine (CLZ) and ziprasidone (ZIP) binding. Chronic administration of CLZ reduced, whereas treatment with ZIP increased albumin-SH content in rats. Regardless of the ratio of stearic acid (SA) bound to protein, in vitro binding of ZIP to human serum albumin (HSA) increased both the SH group level and reactivity. In contrast, the effect of CLZ on HSA-SH reactivity was dependent on HSA to SA molar ratio. CLZ binding was accompanied by an increase in HSA-SH reactivity in samples with normal, but a reduction of its reactivity level with higher SA/HSA ratio, compared to drug-free samples. We demonstrate by steady-state fluorescence quenching studies that an increase in SA binding to HSA is associated with a significant reduction of binding constant for both antipsychotics. In addition, this is the first report of quantitative characterization of ZIP binding to HSA. Our findings suggest that albumin-SH content and reactivity is modulated by ZIP towards an increased antioxidant defense capacity in circulation, as opposed to CLZ, which can contribute to the safer, more effective treatment of schizophrenia.",
publisher = "Elsevier",
journal = "Chemico-Biological Interactions",
title = "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content",
volume = "311",
number = "108787",
doi = "10.1016/j.cbi.2019.108787"
}

Uzelac, T. N., Nikolić-Kokić, A., Spasić, S., Mačvanin, M. T., Nikolić, M., Mandić, L. M.,& Jovanović, V. B.. (2019). Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions
Elsevier., 311(108787).
https://doi.org/10.1016/j.cbi.2019.108787

Uzelac TN, Nikolić-Kokić A, Spasić S, Mačvanin MT, Nikolić M, Mandić LM, Jovanović VB. Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content. in Chemico-Biological Interactions. 2019;311(108787).
doi:10.1016/j.cbi.2019.108787 .

Uzelac, Tamara N., Nikolić-Kokić, Aleksandra, Spasić, Snežana, Mačvanin, Mirjana T., Nikolić, Milan, Mandić, Ljuba M., Jovanović, Vesna B., "Opposite clozapine and ziprasidone effects on the reactivity of plasma albumin SH-group are the consequence of their different binding properties dependent on protein fatty acids content" in Chemico-Biological Interactions, 311, no. 108787 (2019),
https://doi.org/10.1016/j.cbi.2019.108787 . .

TY  - JOUR
AU  - Takić, Marija M.
AU  - Jovanović, Vesna B.
AU  - Pavićević, Ivan D.
AU  - Uzelac, Tamara N.
AU  - Aćimović, Jelena M.
AU  - Ristić-Medić, Danijela
AU  - Mandić, Ljuba M.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2054
AB  - The interaction of polyphenolic molecules with human serum albumin (HSA) could lead to changes in the reactivity of the HSA Cys34 thiol group (HSA-SH). The influences of enterolactone (EL) and enterodiol (ED) binding on HSA-SH reactivity in fatty acid (FA)-free HSA, and in HSA with bound stearic acid (S) in S/HSA molar ratios of 1 : 1 and 4 : 1, were investigated by the determination of the pseudo first order rate constants (k') for the thiol reaction with 5,5'-dithiobis-(2-nitrobenzoic acid). The binding affinities and binding sites of EL and ED were also determined, using fluorescence measurements of the intrinsic fluorescence of Trp214 and diazepam (binding site marker). EL and ED binding to HSA increased the reactivity of HSA-SH in all assayed HSA-enterolignan complexes by 9.1-33.1%. The strongest effects were obtained for FA-free HSA-enterolignan complexes. S modulated/reduced the effect of EL on HSA-SH reactivity, while its influence on the effect of ED was negligible. The binding of enterolignans to HSA was investigated: the binding constants were the highest for FA-free HSA (EL: 11.64 x 10(4) M-1 and ED: 5.59 x 10(4) M-1 at 37 degrees C) and the lowest for S/HSA 4 : 1-enterolignan complexes (EL: 2.43 x 10(4) M-1 and ED: 1.92 x 10(4) M-1). When the S/HSA ratio was increased, the binding affinities and number of binding sites for EL and ED were decreased. At the same time, a high correlation between binding constants and increased Cys34 reactivity was found (r = 0.974). Competitive experiments using diazepam indicated that the binding of ED and of EL was located in the hydrophobic pocket of site II in HSA. Overall, it is evident that stearic acid could modulate the enterolignan effects on HSA-SH reactivity as well as their binding to HSA. This finding could be important for pharmacokinetics and the expression of enterolignan antioxidant effects in vivo after an intake of lignan rich food.
PB  - Royal Soc Chemistry, Cambridge
T2  - Food and Function
T1  - Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity
VL  - 7
IS  - 2
SP  - 1217
EP  - 1226
DO  - 10.1039/c5fo01346a
ER  - 

@article{
author = "Takić, Marija M. and Jovanović, Vesna B. and Pavićević, Ivan D. and Uzelac, Tamara N. and Aćimović, Jelena M. and Ristić-Medić, Danijela and Mandić, Ljuba M.",
year = "2016",
abstract = "The interaction of polyphenolic molecules with human serum albumin (HSA) could lead to changes in the reactivity of the HSA Cys34 thiol group (HSA-SH). The influences of enterolactone (EL) and enterodiol (ED) binding on HSA-SH reactivity in fatty acid (FA)-free HSA, and in HSA with bound stearic acid (S) in S/HSA molar ratios of 1 : 1 and 4 : 1, were investigated by the determination of the pseudo first order rate constants (k') for the thiol reaction with 5,5'-dithiobis-(2-nitrobenzoic acid). The binding affinities and binding sites of EL and ED were also determined, using fluorescence measurements of the intrinsic fluorescence of Trp214 and diazepam (binding site marker). EL and ED binding to HSA increased the reactivity of HSA-SH in all assayed HSA-enterolignan complexes by 9.1-33.1%. The strongest effects were obtained for FA-free HSA-enterolignan complexes. S modulated/reduced the effect of EL on HSA-SH reactivity, while its influence on the effect of ED was negligible. The binding of enterolignans to HSA was investigated: the binding constants were the highest for FA-free HSA (EL: 11.64 x 10(4) M-1 and ED: 5.59 x 10(4) M-1 at 37 degrees C) and the lowest for S/HSA 4 : 1-enterolignan complexes (EL: 2.43 x 10(4) M-1 and ED: 1.92 x 10(4) M-1). When the S/HSA ratio was increased, the binding affinities and number of binding sites for EL and ED were decreased. At the same time, a high correlation between binding constants and increased Cys34 reactivity was found (r = 0.974). Competitive experiments using diazepam indicated that the binding of ED and of EL was located in the hydrophobic pocket of site II in HSA. Overall, it is evident that stearic acid could modulate the enterolignan effects on HSA-SH reactivity as well as their binding to HSA. This finding could be important for pharmacokinetics and the expression of enterolignan antioxidant effects in vivo after an intake of lignan rich food.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Food and Function",
title = "Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity",
volume = "7",
number = "2",
pages = "1217-1226",
doi = "10.1039/c5fo01346a"
}

Takić, M. M., Jovanović, V. B., Pavićević, I. D., Uzelac, T. N., Aćimović, J. M., Ristić-Medić, D.,& Mandić, L. M.. (2016). Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity. in Food and Function
Royal Soc Chemistry, Cambridge., 7(2), 1217-1226.
https://doi.org/10.1039/c5fo01346a

Takić MM, Jovanović VB, Pavićević ID, Uzelac TN, Aćimović JM, Ristić-Medić D, Mandić LM. Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity. in Food and Function. 2016;7(2):1217-1226.
doi:10.1039/c5fo01346a .

Takić, Marija M., Jovanović, Vesna B., Pavićević, Ivan D., Uzelac, Tamara N., Aćimović, Jelena M., Ristić-Medić, Danijela, Mandić, Ljuba M., "Binding of enterolactone and enterodiol to human serum albumin: increase of cysteine-34 thiol group reactivity" in Food and Function, 7, no. 2 (2016):1217-1226,
https://doi.org/10.1039/c5fo01346a . .