TY  - JOUR
AU  - Wedmann, Rudolf
AU  - Onderka, Constantin
AU  - Wei, Shengwei
AU  - Szijarto, Istvan Andras
AU  - Miljković, Jan Lj
AU  - Mitrović, Aleksandra D.
AU  - Lange, Mike
AU  - Savitsky, Sergey
AU  - Yadav, Pramod Kumar
AU  - Torregrossa, Roberta
AU  - Harrer, Ellen G.
AU  - Harrer, Thomas
AU  - Ishii, Isao
AU  - Gollasch, Maik
AU  - Wood, Mark E.
AU  - Galardon, Erwan
AU  - Xian, Ming
AU  - Whiteman, Matthew
AU  - Banerjee, Ruma
AU  - Filipović, Miloš R.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1925
AB  - Hydrogen sulfide (H2S) has emerged as a signalling molecule capable of regulating several important physiological functions such as blood pressure, neurotransmission and inflammation. The mechanisms behind these effects are still largely elusive and oxidative posttranslational modification of cysteine residues (protein persulfidation or S-sulfhydration) has been proposed as the main pathway for H2S-induced biological and pharmacological effects. As a signalling mechanism, persulfidation has to be controlled. Using an improved tag-switch assay for persulfide detection we show here that protein persulfide levels are controlled by the thioredoxin system. Recombinant thioredoxin showed an almost 10-fold higher reactivity towards cysteine persulfide than towards cystine and readily cleaved protein persulfides as well. This reaction resulted in H2S release suggesting that thioredoxin could be an important regulator of H2S levels from persulfide pools. Inhibition of the thioredoxin system caused an increase in intracellular persulfides, highlighting thioredoxin as a major protein depersulfidase that controls H2S signalling. Finally, using plasma from HIV-1 patients that have higher circulatory levels of thioredoxin, we could prove depersulfidase role in vivo.
PB  - Royal Soc Chemistry, Cambridge
T2  - Chemical Science
T1  - Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation
VL  - 7
IS  - 5
SP  - 3414
EP  - 3426
DO  - 10.1039/c5sc04818d
ER  - 

@article{
author = "Wedmann, Rudolf and Onderka, Constantin and Wei, Shengwei and Szijarto, Istvan Andras and Miljković, Jan Lj and Mitrović, Aleksandra D. and Lange, Mike and Savitsky, Sergey and Yadav, Pramod Kumar and Torregrossa, Roberta and Harrer, Ellen G. and Harrer, Thomas and Ishii, Isao and Gollasch, Maik and Wood, Mark E. and Galardon, Erwan and Xian, Ming and Whiteman, Matthew and Banerjee, Ruma and Filipović, Miloš R.",
year = "2016",
abstract = "Hydrogen sulfide (H2S) has emerged as a signalling molecule capable of regulating several important physiological functions such as blood pressure, neurotransmission and inflammation. The mechanisms behind these effects are still largely elusive and oxidative posttranslational modification of cysteine residues (protein persulfidation or S-sulfhydration) has been proposed as the main pathway for H2S-induced biological and pharmacological effects. As a signalling mechanism, persulfidation has to be controlled. Using an improved tag-switch assay for persulfide detection we show here that protein persulfide levels are controlled by the thioredoxin system. Recombinant thioredoxin showed an almost 10-fold higher reactivity towards cysteine persulfide than towards cystine and readily cleaved protein persulfides as well. This reaction resulted in H2S release suggesting that thioredoxin could be an important regulator of H2S levels from persulfide pools. Inhibition of the thioredoxin system caused an increase in intracellular persulfides, highlighting thioredoxin as a major protein depersulfidase that controls H2S signalling. Finally, using plasma from HIV-1 patients that have higher circulatory levels of thioredoxin, we could prove depersulfidase role in vivo.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Chemical Science",
title = "Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation",
volume = "7",
number = "5",
pages = "3414-3426",
doi = "10.1039/c5sc04818d"
}

Wedmann, R., Onderka, C., Wei, S., Szijarto, I. A., Miljković, J. L., Mitrović, A. D., Lange, M., Savitsky, S., Yadav, P. K., Torregrossa, R., Harrer, E. G., Harrer, T., Ishii, I., Gollasch, M., Wood, M. E., Galardon, E., Xian, M., Whiteman, M., Banerjee, R.,& Filipović, M. R.. (2016). Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation. in Chemical Science
Royal Soc Chemistry, Cambridge., 7(5), 3414-3426.
https://doi.org/10.1039/c5sc04818d

Wedmann R, Onderka C, Wei S, Szijarto IA, Miljković JL, Mitrović AD, Lange M, Savitsky S, Yadav PK, Torregrossa R, Harrer EG, Harrer T, Ishii I, Gollasch M, Wood ME, Galardon E, Xian M, Whiteman M, Banerjee R, Filipović MR. Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation. in Chemical Science. 2016;7(5):3414-3426.
doi:10.1039/c5sc04818d .

Wedmann, Rudolf, Onderka, Constantin, Wei, Shengwei, Szijarto, Istvan Andras, Miljković, Jan Lj, Mitrović, Aleksandra D., Lange, Mike, Savitsky, Sergey, Yadav, Pramod Kumar, Torregrossa, Roberta, Harrer, Ellen G., Harrer, Thomas, Ishii, Isao, Gollasch, Maik, Wood, Mark E., Galardon, Erwan, Xian, Ming, Whiteman, Matthew, Banerjee, Ruma, Filipović, Miloš R., "Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation" in Chemical Science, 7, no. 5 (2016):3414-3426,
https://doi.org/10.1039/c5sc04818d . .

TY  - DATA
AU  - Wedmann, Rudolf
AU  - Onderka, Constantin
AU  - Wei, Shengwei
AU  - Szijarto, Istvan Andras
AU  - Miljković, Jan Lj
AU  - Mitrović, Aleksandra D.
AU  - Lange, Mike
AU  - Savitsky, Sergey
AU  - Yadav, Pramod Kumar
AU  - Torregrossa, Roberta
AU  - Harrer, Ellen G.
AU  - Harrer, Thomas
AU  - Ishii, Isao
AU  - Gollasch, Maik
AU  - Wood, Mark E.
AU  - Galardon, Erwan
AU  - Xian, Ming
AU  - Whiteman, Matthew
AU  - Banerjee, Ruma
AU  - Filipović, Miloš R.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3543
PB  - Royal Soc Chemistry, Cambridge
T2  - Chemical Science
T1  - Supplementary material for the article: Wedmann, R.; Onderka, C.; Wei, S.; Szijártó, I. A.; Miljkovic, J. L.; Mitrovic, A.; Lange, M.; Savitsky, S.; Yadav, P. K.; Torregrossa, R.; et al. Improved Tag-Switch Method Reveals That Thioredoxin Acts as Depersulfidase and Controls the Intracellular Levels of Protein Persulfidation. Chemical Science 2016, 7 (5), 3414–3426. https://doi.org/10.1039/c5sc04818d
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3543
ER  - 

@misc{
author = "Wedmann, Rudolf and Onderka, Constantin and Wei, Shengwei and Szijarto, Istvan Andras and Miljković, Jan Lj and Mitrović, Aleksandra D. and Lange, Mike and Savitsky, Sergey and Yadav, Pramod Kumar and Torregrossa, Roberta and Harrer, Ellen G. and Harrer, Thomas and Ishii, Isao and Gollasch, Maik and Wood, Mark E. and Galardon, Erwan and Xian, Ming and Whiteman, Matthew and Banerjee, Ruma and Filipović, Miloš R.",
year = "2016",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Chemical Science",
title = "Supplementary material for the article: Wedmann, R.; Onderka, C.; Wei, S.; Szijártó, I. A.; Miljkovic, J. L.; Mitrovic, A.; Lange, M.; Savitsky, S.; Yadav, P. K.; Torregrossa, R.; et al. Improved Tag-Switch Method Reveals That Thioredoxin Acts as Depersulfidase and Controls the Intracellular Levels of Protein Persulfidation. Chemical Science 2016, 7 (5), 3414–3426. https://doi.org/10.1039/c5sc04818d",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3543"
}

Wedmann, R., Onderka, C., Wei, S., Szijarto, I. A., Miljković, J. L., Mitrović, A. D., Lange, M., Savitsky, S., Yadav, P. K., Torregrossa, R., Harrer, E. G., Harrer, T., Ishii, I., Gollasch, M., Wood, M. E., Galardon, E., Xian, M., Whiteman, M., Banerjee, R.,& Filipović, M. R.. (2016). Supplementary material for the article: Wedmann, R.; Onderka, C.; Wei, S.; Szijártó, I. A.; Miljkovic, J. L.; Mitrovic, A.; Lange, M.; Savitsky, S.; Yadav, P. K.; Torregrossa, R.; et al. Improved Tag-Switch Method Reveals That Thioredoxin Acts as Depersulfidase and Controls the Intracellular Levels of Protein Persulfidation. Chemical Science 2016, 7 (5), 3414–3426. https://doi.org/10.1039/c5sc04818d. in Chemical Science
Royal Soc Chemistry, Cambridge..
https://hdl.handle.net/21.15107/rcub_cherry_3543

Wedmann R, Onderka C, Wei S, Szijarto IA, Miljković JL, Mitrović AD, Lange M, Savitsky S, Yadav PK, Torregrossa R, Harrer EG, Harrer T, Ishii I, Gollasch M, Wood ME, Galardon E, Xian M, Whiteman M, Banerjee R, Filipović MR. Supplementary material for the article: Wedmann, R.; Onderka, C.; Wei, S.; Szijártó, I. A.; Miljkovic, J. L.; Mitrovic, A.; Lange, M.; Savitsky, S.; Yadav, P. K.; Torregrossa, R.; et al. Improved Tag-Switch Method Reveals That Thioredoxin Acts as Depersulfidase and Controls the Intracellular Levels of Protein Persulfidation. Chemical Science 2016, 7 (5), 3414–3426. https://doi.org/10.1039/c5sc04818d. in Chemical Science. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3543 .

Wedmann, Rudolf, Onderka, Constantin, Wei, Shengwei, Szijarto, Istvan Andras, Miljković, Jan Lj, Mitrović, Aleksandra D., Lange, Mike, Savitsky, Sergey, Yadav, Pramod Kumar, Torregrossa, Roberta, Harrer, Ellen G., Harrer, Thomas, Ishii, Isao, Gollasch, Maik, Wood, Mark E., Galardon, Erwan, Xian, Ming, Whiteman, Matthew, Banerjee, Ruma, Filipović, Miloš R., "Supplementary material for the article: Wedmann, R.; Onderka, C.; Wei, S.; Szijártó, I. A.; Miljkovic, J. L.; Mitrovic, A.; Lange, M.; Savitsky, S.; Yadav, P. K.; Torregrossa, R.; et al. Improved Tag-Switch Method Reveals That Thioredoxin Acts as Depersulfidase and Controls the Intracellular Levels of Protein Persulfidation. Chemical Science 2016, 7 (5), 3414–3426. https://doi.org/10.1039/c5sc04818d" in Chemical Science (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3543 .

TY  - JOUR
AU  - Snijder, Pauline M.
AU  - Baratashvili, Madina
AU  - Grzeschik, Nicola A.
AU  - Leuvenink, Henri G. D.
AU  - Kuijpers, Lucas
AU  - Huitema, Sippie
AU  - Schaap, Onno
AU  - Giepmans, Ben N. G.
AU  - Kuipers, Jeroen
AU  - Miljković, Jan Lj
AU  - Mitrović, Aleksandra D.
AU  - Bos, Eelke M.
AU  - Szabo, Csaba
AU  - Kampinga, Harm H.
AU  - Dijkers, Pascale F.
AU  - den Dunnen, Wilfred F. A.
AU  - Filipović, Miloš R.
AU  - van Goor, Harry
AU  - Sibon, Ody C. M.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2255
AB  - Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder caused by a CAG repeat expansion in the ataxin-3 (ATXN3) gene resulting in toxic protein aggregation. Inflammation and oxidative stress are considered secondary factors contributing to the progression of this neurodegenerative disease. There is no cure that halts or reverses the progressive neurodegeneration of SCA3. Here we show that overexpression of cystathionine.-lyase, a central enzyme in cysteine metabolism, is protective in a Drosophila model for SCA3. SCA3 flies show eye degeneration, increased oxidative stress, insoluble protein aggregates, reduced levels of protein persulfidation and increased activation of the innate immune response. Overexpression of Drosophila cystathionine.-lyase restores protein persulfidation, decreases oxidative stress, dampens the immune response and improves SCA3-associated tissue degeneration. Levels of insoluble protein aggregates are not altered; therefore, the data implicate a modifying role of cystathionine.-lyase in ameliorating the downstream consequence of protein aggregation leading to protection against SCA3-induced tissue degeneration. The cystathionine.-lyase expression is decreased in affected brain tissue of SCA3 patients, suggesting that enhancers of cystathionine.-lyase expression or activity are attractive candidates for future therapies.
PB  - Feinstein Inst Med Res, Manhasset
T2  - Molecular Medicine
T1  - Overexpression of Cystathionine gamma-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3
VL  - 21
SP  - 758
EP  - 768
DO  - 10.2119/molmed.2015.00221
ER  - 

@article{
author = "Snijder, Pauline M. and Baratashvili, Madina and Grzeschik, Nicola A. and Leuvenink, Henri G. D. and Kuijpers, Lucas and Huitema, Sippie and Schaap, Onno and Giepmans, Ben N. G. and Kuipers, Jeroen and Miljković, Jan Lj and Mitrović, Aleksandra D. and Bos, Eelke M. and Szabo, Csaba and Kampinga, Harm H. and Dijkers, Pascale F. and den Dunnen, Wilfred F. A. and Filipović, Miloš R. and van Goor, Harry and Sibon, Ody C. M.",
year = "2015",
abstract = "Spinocerebellar ataxia type 3 (SCA3) is a polyglutamine (polyQ) disorder caused by a CAG repeat expansion in the ataxin-3 (ATXN3) gene resulting in toxic protein aggregation. Inflammation and oxidative stress are considered secondary factors contributing to the progression of this neurodegenerative disease. There is no cure that halts or reverses the progressive neurodegeneration of SCA3. Here we show that overexpression of cystathionine.-lyase, a central enzyme in cysteine metabolism, is protective in a Drosophila model for SCA3. SCA3 flies show eye degeneration, increased oxidative stress, insoluble protein aggregates, reduced levels of protein persulfidation and increased activation of the innate immune response. Overexpression of Drosophila cystathionine.-lyase restores protein persulfidation, decreases oxidative stress, dampens the immune response and improves SCA3-associated tissue degeneration. Levels of insoluble protein aggregates are not altered; therefore, the data implicate a modifying role of cystathionine.-lyase in ameliorating the downstream consequence of protein aggregation leading to protection against SCA3-induced tissue degeneration. The cystathionine.-lyase expression is decreased in affected brain tissue of SCA3 patients, suggesting that enhancers of cystathionine.-lyase expression or activity are attractive candidates for future therapies.",
publisher = "Feinstein Inst Med Res, Manhasset",
journal = "Molecular Medicine",
title = "Overexpression of Cystathionine gamma-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3",
volume = "21",
pages = "758-768",
doi = "10.2119/molmed.2015.00221"
}

Snijder, P. M., Baratashvili, M., Grzeschik, N. A., Leuvenink, H. G. D., Kuijpers, L., Huitema, S., Schaap, O., Giepmans, B. N. G., Kuipers, J., Miljković, J. L., Mitrović, A. D., Bos, E. M., Szabo, C., Kampinga, H. H., Dijkers, P. F., den Dunnen, W. F. A., Filipović, M. R., van Goor, H.,& Sibon, O. C. M.. (2015). Overexpression of Cystathionine gamma-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3. in Molecular Medicine
Feinstein Inst Med Res, Manhasset., 21, 758-768.
https://doi.org/10.2119/molmed.2015.00221

Snijder PM, Baratashvili M, Grzeschik NA, Leuvenink HGD, Kuijpers L, Huitema S, Schaap O, Giepmans BNG, Kuipers J, Miljković JL, Mitrović AD, Bos EM, Szabo C, Kampinga HH, Dijkers PF, den Dunnen WFA, Filipović MR, van Goor H, Sibon OCM. Overexpression of Cystathionine gamma-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3. in Molecular Medicine. 2015;21:758-768.
doi:10.2119/molmed.2015.00221 .

Snijder, Pauline M., Baratashvili, Madina, Grzeschik, Nicola A., Leuvenink, Henri G. D., Kuijpers, Lucas, Huitema, Sippie, Schaap, Onno, Giepmans, Ben N. G., Kuipers, Jeroen, Miljković, Jan Lj, Mitrović, Aleksandra D., Bos, Eelke M., Szabo, Csaba, Kampinga, Harm H., Dijkers, Pascale F., den Dunnen, Wilfred F. A., Filipović, Miloš R., van Goor, Harry, Sibon, Ody C. M., "Overexpression of Cystathionine gamma-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3" in Molecular Medicine, 21 (2015):758-768,
https://doi.org/10.2119/molmed.2015.00221 . .

TY  - DATA
AU  - Snijder, Pauline M.
AU  - Baratashvili, Madina
AU  - Grzeschik, Nicola A.
AU  - Leuvenink, Henri G. D.
AU  - Kuijpers, Lucas
AU  - Huitema, Sippie
AU  - Schaap, Onno
AU  - Giepmans, Ben N. G.
AU  - Kuipers, Jeroen
AU  - Miljković, Jan Lj
AU  - Mitrović, Aleksandra D.
AU  - Bos, Eelke M.
AU  - Szabo, Csaba
AU  - Kampinga, Harm H.
AU  - Dijkers, Pascale F.
AU  - den Dunnen, Wilfred F. A.
AU  - Filipović, Miloš R.
AU  - van Goor, Harry
AU  - Sibon, Ody C. M.
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3402
PB  - Feinstein Inst Med Res, Manhasset
T2  - Molecular Medicine
T1  - Supplementary data for article: Snijder, P. M.; Baratashvili, M.; Grzeschik, N. A.; Leuvenink, H. G. D.; Kuijpers, L.; Huitema, S.; Schaap, O.; Giepmans, B. N. G.; Kuipers, J.; Miljkovic, J. L.; et al. Overexpression of Cystathionine γ-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3. Molecular Medicine 2015, 21, 758–768. https://doi.org/10.2119/molmed.2015.00221
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3402
ER  - 

@misc{
author = "Snijder, Pauline M. and Baratashvili, Madina and Grzeschik, Nicola A. and Leuvenink, Henri G. D. and Kuijpers, Lucas and Huitema, Sippie and Schaap, Onno and Giepmans, Ben N. G. and Kuipers, Jeroen and Miljković, Jan Lj and Mitrović, Aleksandra D. and Bos, Eelke M. and Szabo, Csaba and Kampinga, Harm H. and Dijkers, Pascale F. and den Dunnen, Wilfred F. A. and Filipović, Miloš R. and van Goor, Harry and Sibon, Ody C. M.",
year = "2015",
publisher = "Feinstein Inst Med Res, Manhasset",
journal = "Molecular Medicine",
title = "Supplementary data for article: Snijder, P. M.; Baratashvili, M.; Grzeschik, N. A.; Leuvenink, H. G. D.; Kuijpers, L.; Huitema, S.; Schaap, O.; Giepmans, B. N. G.; Kuipers, J.; Miljkovic, J. L.; et al. Overexpression of Cystathionine γ-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3. Molecular Medicine 2015, 21, 758–768. https://doi.org/10.2119/molmed.2015.00221",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3402"
}

Snijder, P. M., Baratashvili, M., Grzeschik, N. A., Leuvenink, H. G. D., Kuijpers, L., Huitema, S., Schaap, O., Giepmans, B. N. G., Kuipers, J., Miljković, J. L., Mitrović, A. D., Bos, E. M., Szabo, C., Kampinga, H. H., Dijkers, P. F., den Dunnen, W. F. A., Filipović, M. R., van Goor, H.,& Sibon, O. C. M.. (2015). Supplementary data for article: Snijder, P. M.; Baratashvili, M.; Grzeschik, N. A.; Leuvenink, H. G. D.; Kuijpers, L.; Huitema, S.; Schaap, O.; Giepmans, B. N. G.; Kuipers, J.; Miljkovic, J. L.; et al. Overexpression of Cystathionine γ-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3. Molecular Medicine 2015, 21, 758–768. https://doi.org/10.2119/molmed.2015.00221. in Molecular Medicine
Feinstein Inst Med Res, Manhasset..
https://hdl.handle.net/21.15107/rcub_cherry_3402

Snijder PM, Baratashvili M, Grzeschik NA, Leuvenink HGD, Kuijpers L, Huitema S, Schaap O, Giepmans BNG, Kuipers J, Miljković JL, Mitrović AD, Bos EM, Szabo C, Kampinga HH, Dijkers PF, den Dunnen WFA, Filipović MR, van Goor H, Sibon OCM. Supplementary data for article: Snijder, P. M.; Baratashvili, M.; Grzeschik, N. A.; Leuvenink, H. G. D.; Kuijpers, L.; Huitema, S.; Schaap, O.; Giepmans, B. N. G.; Kuipers, J.; Miljkovic, J. L.; et al. Overexpression of Cystathionine γ-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3. Molecular Medicine 2015, 21, 758–768. https://doi.org/10.2119/molmed.2015.00221. in Molecular Medicine. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3402 .

Snijder, Pauline M., Baratashvili, Madina, Grzeschik, Nicola A., Leuvenink, Henri G. D., Kuijpers, Lucas, Huitema, Sippie, Schaap, Onno, Giepmans, Ben N. G., Kuipers, Jeroen, Miljković, Jan Lj, Mitrović, Aleksandra D., Bos, Eelke M., Szabo, Csaba, Kampinga, Harm H., Dijkers, Pascale F., den Dunnen, Wilfred F. A., Filipović, Miloš R., van Goor, Harry, Sibon, Ody C. M., "Supplementary data for article: Snijder, P. M.; Baratashvili, M.; Grzeschik, N. A.; Leuvenink, H. G. D.; Kuijpers, L.; Huitema, S.; Schaap, O.; Giepmans, B. N. G.; Kuipers, J.; Miljkovic, J. L.; et al. Overexpression of Cystathionine γ-Lyase Suppresses Detrimental Effects of Spinocerebellar Ataxia Type 3. Molecular Medicine 2015, 21, 758–768. https://doi.org/10.2119/molmed.2015.00221" in Molecular Medicine (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3402 .