Results 51 to 60 of about 260,568 (212)
Quantification of thiols and disulfides [PDF]
Biochimica et Biophysica Acta (BBA) - General Subjects, 2014 Disulfide bond formation is a key posttranslational modification, with implications for structure, function and stability of numerous proteins. While disulfide bond formation is a necessary and essential process for many proteins, it is deleterious and disruptive for others.
Winther, Jakob R., Thorpe, Colin
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Thiol/Disulfide homeostasis in patients with rheumatoid arthritis
Romanian Journal of Internal Medicine, 2019 Background. Oxidative stress may play an important role in rheumatoid arthritis (RA) etiopathogenesis. The thiol group is a very strong antioxidant. In this study, we aimed to investigate the presence of oxidative stress in patients with RA by evaluating
Tuzcu Ayca +9 more
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Thiol-disulfide oxidoreductases: assays, inhibitors, and metabolic roles
, 2022 Thorpe, ColinDisulfide bonds are common post-translational modifications which serve to stabilize or impart function onto proteins. Although this product of oxidation between two cysteine thiols is relatively stable, disulfide bonds are able to undergo ...
Foster, Celia K.
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Frontiers in Plant Science, 2020 In proteins, hydrogen peroxide (H2O2) reacts with redox-sensitive cysteines to form cysteine sulfenic acid, also known as S-sulfenylation. These cysteine oxidation events can steer diverse cellular processes by altering protein interactions, trafficking,
Bo Wei +15 more
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, 2016 Exploring novel electrode materials is critical for the development of a next-generation rechargeable magnesium battery with high volumetric capacity. Here, we showed that a distinct amorphous molybdenum sulfide, being a coordination polymer of disulfide-
Yoshiyuki Gambe (2910662) +7 more
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Redox-Click Chemistry for Disulfide Formation from Thiols
, 2023 The dynamic disulfide linkage plays a vital role in various biological processes as well as drugs and biomaterials. Oxidation of thiols is a widely utilized approach for disulfide synthesis; however, achieving both optimal reactivity and selectivity ...
Xiaohe, Zhang +19 more
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Characterisation of the oxidoreductase Erol-Lß and the misfolding of the secretory pathway substrate HLA-B27 [PDF]
, 2007 The endoplasmic reticulum (ER) is the site of oxidative folding for proteins entering the secretory pathway. Here, nascent polypeptides acquire disulfide bonds, which confer both stability and functionality on secretory and ER-resident proteins.
Lemin, Andrew James
core
Disulfide-Cross-Linked Tetra-PEG Gels
The preparation of polymer gels via cross-linking of four-arm star-shaped poly(ethylene glycol) (Tetra-PEG) precursors is an attractive strategy to prepare networks with relatively well-defined topologies. Typically, Tetra-PEG gels are obtained by cross-
Zhao Meng (3307833) +4 more
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, 2022 Disulfide bonds in proteins have a substantial impact on protein structure, stability, and biological activity. Localizing disulfide bonds is critical for understanding protein folding and higher-order structure.
Muhammad, Zenaidee +6 more
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Pharmaceutics, 2020 Cystamine-based polymers may help to achieve controlled and targeted drug delivery to the colon due to their susceptibility to breakage of the disulfide linkage in the low redox potential environment of the colon.
Yoke Mooi Ng +3 more
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