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Investigation of Thiol/Disulfide Balance in Obese Rats with Non-Alcoholic Fatty Liver Disease.

Pediatric gastroenterology, hepatology & nutrition

Tursun S, Gülerman HF, Gazyağcı S, Şahin Y, Erel Ö, Neşelioğlu S.
PMID: 34557397
Pediatr Gastroenterol Hepatol Nutr. 2021 Sep;24(5):443-454. doi: 10.5223/pghn.2021.24.5.443. Epub 2021 Sep 08.

PURPOSE: Due to the increasing prevalence of obesity worldwide, non-alcoholic fatty liver disease (NAFLD) has reached epidemic dimensions over time. NAFLD is the most common cause of childhood chronic liver disease. There is a relationship between NAFLD and oxidative...

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Tursun S, Gülerman HF, Gazyağcı S, et al. Investigation of Thiol/Disulfide Balance in Obese Rats with Non-Alcoholic Fatty Liver Disease. Pediatr Gastroenterol Hepatol Nutr. 2021;24(5):443-454doi: 10.5223/pghn.2021.24.5.443.
Tursun, S., Gülerman, H. F., Gazyağcı, S., Şahin, Y., Erel, �. �., & Neşelioğlu, S. (2021). Investigation of Thiol/Disulfide Balance in Obese Rats with Non-Alcoholic Fatty Liver Disease. Pediatric gastroenterology, hepatology & nutrition, 24(5), 443-454. https://doi.org/10.5223/pghn.2021.24.5.443
Tursun, Serkan, et al. "Investigation of Thiol/Disulfide Balance in Obese Rats with Non-Alcoholic Fatty Liver Disease." Pediatric gastroenterology, hepatology & nutrition vol. 24,5 (2021): 443-454. doi: https://doi.org/10.5223/pghn.2021.24.5.443
Tursun S, Gülerman HF, Gazyağcı S, Şahin Y, Erel Ö, Neşelioğlu S. Investigation of Thiol/Disulfide Balance in Obese Rats with Non-Alcoholic Fatty Liver Disease. Pediatr Gastroenterol Hepatol Nutr. 2021 Sep;24(5):443-454. doi: 10.5223/pghn.2021.24.5.443. Epub 2021 Sep 08. PMID: 34557397; PMCID: PMC8443854.
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High-quality WS.

Nanoscale

Wang X, Liu P, Yap B, Xia R, Wong WY, He Z.
PMID: 34585178
Nanoscale. 2021 Oct 14;13(39):16589-16597. doi: 10.1039/d1nr03728e.

Liquid-exfoliated 2D transition metal disulfides (TMDs) are potential substitutes for poly(3,4-ethylenedioxythiophene):poly(styrenesulfonate) (PEDOT:PSS) as hole transport layers (HTLs) in Organic Solar Cells (OSCs). Herein, high-yield and high-quality WS

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Wang X, Liu P, Yap B, et al. High-quality WS. Nanoscale. 2021;13(39):16589-16597doi: 10.1039/d1nr03728e.
Wang, X., Liu, P., Yap, B., Xia, R., Wong, W. Y., & He, Z. (2021). High-quality WS. Nanoscale, 13(39), 16589-16597. https://doi.org/10.1039/d1nr03728e
Wang, Xiaojing, et al. "High-quality WS." Nanoscale vol. 13,39 (2021): 16589-16597. doi: https://doi.org/10.1039/d1nr03728e
Wang X, Liu P, Yap B, Xia R, Wong WY, He Z. High-quality WS. Nanoscale. 2021 Oct 14;13(39):16589-16597. doi: 10.1039/d1nr03728e. PMID: 34585178.
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Ligand-induced transition in conformations of vicinal cysteine disulfides in proteins.

Proteins

Reddy KKA, Jayashree M, Govindu PCV, Gowd KH.
PMID: 33378101
Proteins. 2021 Jun;89(6):599-613. doi: 10.1002/prot.26039. Epub 2021 Mar 25.

Vicinal cysteine disulfides are thought to be associated with specific conformations of cysteine disulfides due to the restricted rotation of single bonds in an eight-membered cyclic disulfide loop. Conformations of vicinal cysteine disulfides are analyzed using χ

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Reddy KKA, Jayashree M, Govindu PCV, et al. Ligand-induced transition in conformations of vicinal cysteine disulfides in proteins. Proteins. 2021;89(6):599-613doi: 10.1002/prot.26039.
Reddy, K. K. A., Jayashree, M., Govindu, P. C. V., & Gowd, K. H. (2021). Ligand-induced transition in conformations of vicinal cysteine disulfides in proteins. Proteins, 89(6), 599-613. https://doi.org/10.1002/prot.26039
Reddy, K Kasi Amarnath, et al. "Ligand-induced transition in conformations of vicinal cysteine disulfides in proteins." Proteins vol. 89,6 (2021): 599-613. doi: https://doi.org/10.1002/prot.26039
Reddy KKA, Jayashree M, Govindu PCV, Gowd KH. Ligand-induced transition in conformations of vicinal cysteine disulfides in proteins. Proteins. 2021 Jun;89(6):599-613. doi: 10.1002/prot.26039. Epub 2021 Mar 25. PMID: 33378101.
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Base-free catalytic aerobic oxidation of mercaptans over MOF-derived Co/CN catalyst with controllable composition and structure.

Journal of colloid and interface science

Zhang C, Gao H, Hai G, Zeng Y, Wang X, Xing L, Zhao J, Wang G, Shu X.
PMID: 34695736
J Colloid Interface Sci. 2022 Feb;607:1836-1848. doi: 10.1016/j.jcis.2021.10.013. Epub 2021 Oct 06.

The oxidation of mercaptans under mild and base-free conditions is of vital importance in terms of economy and environment for petroleum processing industry. Here, we developed a series of MOF-derived cobalt-based nitrogen-doped (N-doped) carbon (Co/CN-x) catalysts for the base-free...

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Zhang C, Gao H, Hai G, et al. Base-free catalytic aerobic oxidation of mercaptans over MOF-derived Co/CN catalyst with controllable composition and structure. J Colloid Interface Sci. 2021;607:1836-1848doi: 10.1016/j.jcis.2021.10.013.
Zhang, C., Gao, H., Hai, G., Zeng, Y., Wang, X., Xing, L., Zhao, J., Wang, G., & Shu, X. (2022). Base-free catalytic aerobic oxidation of mercaptans over MOF-derived Co/CN catalyst with controllable composition and structure. Journal of colloid and interface science, 6071836-1848. https://doi.org/10.1016/j.jcis.2021.10.013
Zhang, Canyang, et al. "Base-free catalytic aerobic oxidation of mercaptans over MOF-derived Co/CN catalyst with controllable composition and structure." Journal of colloid and interface science vol. 607 (2022): 1836-1848. doi: https://doi.org/10.1016/j.jcis.2021.10.013
Zhang C, Gao H, Hai G, Zeng Y, Wang X, Xing L, Zhao J, Wang G, Shu X. Base-free catalytic aerobic oxidation of mercaptans over MOF-derived Co/CN catalyst with controllable composition and structure. J Colloid Interface Sci. 2022 Feb;607:1836-1848. doi: 10.1016/j.jcis.2021.10.013. Epub 2021 Oct 06. PMID: 34695736.
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Synthesis and Biological Evaluation of Dithiobisacetamides as Novel Urease Inhibitors.

ChemMedChem

Liu ML, Li WY, Fang HL, Ye YX, Li SY, Song WQ, Xiao ZP, Ouyang H, Zhu HL.
PMID: 34687265
ChemMedChem. 2021 Oct 23; doi: 10.1002/cmdc.202100618. Epub 2021 Oct 23.

Thirty-eight disulfides containing N-arylacetamide were designed and synthesized in an effort to develop novel urease inhibitors. Biological evaluation revealed that some of the synthetic compounds exhibited strong inhibitory potency against both cell-free urease and urease in intact cell with...

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Liu ML, Li WY, Fang HL, et al. Synthesis and Biological Evaluation of Dithiobisacetamides as Novel Urease Inhibitors. ChemMedChem. 2021;doi: 10.1002/cmdc.202100618.
Liu, M. L., Li, W. Y., Fang, H. L., Ye, Y. X., Li, S. Y., Song, W. Q., Xiao, Z. P., Ouyang, H., & Zhu, H. L. (2021). Synthesis and Biological Evaluation of Dithiobisacetamides as Novel Urease Inhibitors. ChemMedChem, . https://doi.org/10.1002/cmdc.202100618
Liu, Mei-Ling, et al. "Synthesis and Biological Evaluation of Dithiobisacetamides as Novel Urease Inhibitors." ChemMedChem vol. (2021). doi: https://doi.org/10.1002/cmdc.202100618
Liu ML, Li WY, Fang HL, Ye YX, Li SY, Song WQ, Xiao ZP, Ouyang H, Zhu HL. Synthesis and Biological Evaluation of Dithiobisacetamides as Novel Urease Inhibitors. ChemMedChem. 2021 Oct 23; doi: 10.1002/cmdc.202100618. Epub 2021 Oct 23. PMID: 34687265.
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Production of Alkyl Aryl Sulfides from Aromatic Disulfides and Alkyl Carboxylates via a Disilathiane-Disulfide Interchange Reaction.

Chemistry, an Asian journal

Nakajima T, Takano K, Maeda H, Ogiwara Y, Sakai N.
PMID: 34693645
Chem Asian J. 2021 Oct 25; doi: 10.1002/asia.202101101. Epub 2021 Oct 25.

The results of this study show that disilathiane is an effective mediator in the synthesis of alkyl aryl sulfides with disulfides and alkyl carboxylates. Mechanistic studies suggest that disilathiane promotes cleavage of the sulfur-sulfur bond of disulfides to generate...

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Nakajima T, Takano K, Maeda H, et al. Production of Alkyl Aryl Sulfides from Aromatic Disulfides and Alkyl Carboxylates via a Disilathiane-Disulfide Interchange Reaction. Chem Asian J. 2021;doi: 10.1002/asia.202101101.
Nakajima, T., Takano, K., Maeda, H., Ogiwara, Y., & Sakai, N. (2021). Production of Alkyl Aryl Sulfides from Aromatic Disulfides and Alkyl Carboxylates via a Disilathiane-Disulfide Interchange Reaction. Chemistry, an Asian journal, . https://doi.org/10.1002/asia.202101101
Nakajima, Takumi, et al. "Production of Alkyl Aryl Sulfides from Aromatic Disulfides and Alkyl Carboxylates via a Disilathiane-Disulfide Interchange Reaction." Chemistry, an Asian journal vol. (2021). doi: https://doi.org/10.1002/asia.202101101
Nakajima T, Takano K, Maeda H, Ogiwara Y, Sakai N. Production of Alkyl Aryl Sulfides from Aromatic Disulfides and Alkyl Carboxylates via a Disilathiane-Disulfide Interchange Reaction. Chem Asian J. 2021 Oct 25; doi: 10.1002/asia.202101101. Epub 2021 Oct 25. PMID: 34693645.
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Specific domain V reduction of beta-2-glycoprotein I induces protein flexibility and alters pathogenic antibody binding.

Scientific reports

Buchholz I, McDonnell T, Nestler P, Tharad S, Kulke M, Radziszewska A, Ripoll VM, Schmidt F, Hammer E, Toca-Herrera JL, Rahman A, Delcea M.
PMID: 33633190
Sci Rep. 2021 Feb 25;11(1):4542. doi: 10.1038/s41598-021-84021-2.

Beta-2-glycoprotein I (β2GPI) is a blood protein and the major antigen in the autoimmune disorder antiphospholipid syndrome (APS). β2GPI exists mainly in closed or open conformations and comprises of 11 disulfides distributed across five domains. The terminal Cys288/Cys326 disulfide...

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Buchholz I, McDonnell T, Nestler P, et al. Specific domain V reduction of beta-2-glycoprotein I induces protein flexibility and alters pathogenic antibody binding. Sci Rep. 2021;11(1):4542doi: 10.1038/s41598-021-84021-2.
Buchholz, I., McDonnell, T., Nestler, P., Tharad, S., Kulke, M., Radziszewska, A., Ripoll, V. M., Schmidt, F., Hammer, E., Toca-Herrera, J. L., Rahman, A., & Delcea, M. (2021). Specific domain V reduction of beta-2-glycoprotein I induces protein flexibility and alters pathogenic antibody binding. Scientific reports, 11(1), 4542. https://doi.org/10.1038/s41598-021-84021-2
Buchholz, Ina, et al. "Specific domain V reduction of beta-2-glycoprotein I induces protein flexibility and alters pathogenic antibody binding." Scientific reports vol. 11,1 (2021): 4542. doi: https://doi.org/10.1038/s41598-021-84021-2
Buchholz I, McDonnell T, Nestler P, Tharad S, Kulke M, Radziszewska A, Ripoll VM, Schmidt F, Hammer E, Toca-Herrera JL, Rahman A, Delcea M. Specific domain V reduction of beta-2-glycoprotein I induces protein flexibility and alters pathogenic antibody binding. Sci Rep. 2021 Feb 25;11(1):4542. doi: 10.1038/s41598-021-84021-2. PMID: 33633190; PMCID: PMC7907366.
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Thiol-Mediated Uptake.

JACS Au

Laurent Q, Martinent R, Lim B, Pham AT, Kato T, López-Andarias J, Sakai N, Matile S.
PMID: 34467328
JACS Au. 2021 May 03;1(6):710-728. doi: 10.1021/jacsau.1c00128. eCollection 2021 Jun 28.

This Perspective focuses on thiol-mediated uptake, that is, the entry of substrates into cells enabled by oligochalcogenides or mimics, often disulfides, and inhibited by thiol-reactive agents. A short chronology from the initial observations in 1990 until today is followed...

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Laurent Q, Martinent R, Lim B, et al. Thiol-Mediated Uptake. JACS Au. 2021;1(6):710-728doi: 10.1021/jacsau.1c00128.
Laurent, Q., Martinent, R., Lim, B., Pham, A. T., Kato, T., López-Andarias, J., Sakai, N., & Matile, S. (2021). Thiol-Mediated Uptake. JACS Au, 1(6), 710-728. https://doi.org/10.1021/jacsau.1c00128
Laurent, Quentin, et al. "Thiol-Mediated Uptake." JACS Au vol. 1,6 (2021): 710-728. doi: https://doi.org/10.1021/jacsau.1c00128
Laurent Q, Martinent R, Lim B, Pham AT, Kato T, López-Andarias J, Sakai N, Matile S. Thiol-Mediated Uptake. JACS Au. 2021 May 03;1(6):710-728. doi: 10.1021/jacsau.1c00128. eCollection 2021 Jun 28. PMID: 34467328; PMCID: PMC8395643.
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RP-HPLC method for simultaneous quantification of free and total thiol groups in native and heat aggregated whey proteins.

MethodsX

Kurz F, Hengst C, Kulozik U.
PMID: 33194562
MethodsX. 2020 Oct 17;7:101112. doi: 10.1016/j.mex.2020.101112. eCollection 2020.

Disulfide formation of whey proteins during heat treatment via thiol oxidation is important with regard to techno-functional properties. Due to the formation of other oxidation products than disulfides, the decrease in free thiol concentration is not proportional to the...

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Kurz F, Hengst C, Kulozik U. RP-HPLC method for simultaneous quantification of free and total thiol groups in native and heat aggregated whey proteins. MethodsX. 2020;7:101112doi: 10.1016/j.mex.2020.101112.
Kurz, F., Hengst, C., & Kulozik, U. (2020). RP-HPLC method for simultaneous quantification of free and total thiol groups in native and heat aggregated whey proteins. MethodsX, 7101112. https://doi.org/10.1016/j.mex.2020.101112
Kurz, Franziska, et al. "RP-HPLC method for simultaneous quantification of free and total thiol groups in native and heat aggregated whey proteins." MethodsX vol. 7 (2020): 101112. doi: https://doi.org/10.1016/j.mex.2020.101112
Kurz F, Hengst C, Kulozik U. RP-HPLC method for simultaneous quantification of free and total thiol groups in native and heat aggregated whey proteins. MethodsX. 2020 Oct 17;7:101112. doi: 10.1016/j.mex.2020.101112. eCollection 2020. PMID: 33194562; PMCID: PMC7644750.
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A non-immunological role for γ-interferon-inducible lysosomal thiol reductase (GILT) in osteoclastic bone resorption.

Science advances

Ewanchuk BW, Arnold CR, Balce DR, Premnath P, Orsetti TL, Warren AL, Olsen A, Krawetz RJ, Yates RM.
PMID: 33893096
Sci Adv. 2021 Apr 23;7(17). doi: 10.1126/sciadv.abd3684. Print 2021 Apr.

The extracellular bone resorbing lacuna of the osteoclast shares many characteristics with the degradative lysosome of antigen-presenting cells. γ-Interferon-inducible lysosomal thiol reductase (GILT) enhances antigen processing within lysosomes through direct reduction of antigen disulfides and maintenance of cysteine protease...

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Ewanchuk BW, Arnold CR, Balce DR, et al. A non-immunological role for γ-interferon-inducible lysosomal thiol reductase (GILT) in osteoclastic bone resorption. Sci Adv. 2021;7(17)doi: 10.1126/sciadv.abd3684.
Ewanchuk, B. W., Arnold, C. R., Balce, D. R., Premnath, P., Orsetti, T. L., Warren, A. L., Olsen, A., Krawetz, R. J., & Yates, R. M. (2021). A non-immunological role for γ-interferon-inducible lysosomal thiol reductase (GILT) in osteoclastic bone resorption. Science advances, 7(17), . https://doi.org/10.1126/sciadv.abd3684
Ewanchuk, Benjamin W, et al. "A non-immunological role for γ-interferon-inducible lysosomal thiol reductase (GILT) in osteoclastic bone resorption." Science advances vol. 7,17 (2021). doi: https://doi.org/10.1126/sciadv.abd3684
Ewanchuk BW, Arnold CR, Balce DR, Premnath P, Orsetti TL, Warren AL, Olsen A, Krawetz RJ, Yates RM. A non-immunological role for γ-interferon-inducible lysosomal thiol reductase (GILT) in osteoclastic bone resorption. Sci Adv. 2021 Apr 23;7(17). doi: 10.1126/sciadv.abd3684. Print 2021 Apr. PMID: 33893096; PMCID: PMC8064644.
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Disulfide metathesis .

Organic & biomolecular chemistry

Mathuri A, Pramanik M, Parida A, Mal P.
PMID: 34546277
Org Biomol Chem. 2021 Oct 14;19(39):8539-8543. doi: 10.1039/d1ob01581h.

The idea of constitutional dynamic chemistry (CDC) and dynamic combinatorial chemistry (DCC) is widespread in the literature using the chemistry of disulfides. The synthesis of unsymmetrical diaryl disulfides is challenging due to the presence of a weak S-S bond....

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Mathuri A, Pramanik M, Parida A, et al. Disulfide metathesis . Org Biomol Chem. 2021;19(39):8539-8543doi: 10.1039/d1ob01581h.
Mathuri, A., Pramanik, M., Parida, A., & Mal, P. (2021). Disulfide metathesis . Organic & biomolecular chemistry, 19(39), 8539-8543. https://doi.org/10.1039/d1ob01581h
Mathuri, Ashis, et al. "Disulfide metathesis ." Organic & biomolecular chemistry vol. 19,39 (2021): 8539-8543. doi: https://doi.org/10.1039/d1ob01581h
Mathuri A, Pramanik M, Parida A, Mal P. Disulfide metathesis . Org Biomol Chem. 2021 Oct 14;19(39):8539-8543. doi: 10.1039/d1ob01581h. PMID: 34546277.
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Cu-Catalyzed Oxidative Thioesterification of Aroylhydrazides with Disulfides.

The Journal of organic chemistry

Xie S, Su L, Mo M, Zhou W, Zhou Y, Dong J.
PMID: 33301325
J Org Chem. 2021 Jan 01;86(1):739-749. doi: 10.1021/acs.joc.0c02328. Epub 2020 Dec 10.

An alternative thioesterification reaction via copper-catalyzed oxidative coupling of readily available aroylhydrazides with disulfides is developed, in which oxidative expulsion of N

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Xie S, Su L, Mo M, et al. Cu-Catalyzed Oxidative Thioesterification of Aroylhydrazides with Disulfides. J Org Chem. 2020;86(1):739-749doi: 10.1021/acs.joc.0c02328.
Xie, S., Su, L., Mo, M., Zhou, W., Zhou, Y., & Dong, J. (2021). Cu-Catalyzed Oxidative Thioesterification of Aroylhydrazides with Disulfides. The Journal of organic chemistry, 86(1), 739-749. https://doi.org/10.1021/acs.joc.0c02328
Xie, Shimin, et al. "Cu-Catalyzed Oxidative Thioesterification of Aroylhydrazides with Disulfides." The Journal of organic chemistry vol. 86,1 (2021): 739-749. doi: https://doi.org/10.1021/acs.joc.0c02328
Xie S, Su L, Mo M, Zhou W, Zhou Y, Dong J. Cu-Catalyzed Oxidative Thioesterification of Aroylhydrazides with Disulfides. J Org Chem. 2021 Jan 01;86(1):739-749. doi: 10.1021/acs.joc.0c02328. Epub 2020 Dec 10. PMID: 33301325.
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