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Yang Li, Yuwen Chen, Yulan Huang, Wenbi Wu, Yu Liu, Jing Zhang, Meijuan Huang, Maling Gou. Dissolved oxygen-assisted enhancing room temperature phosphorescence of palladium-porphyrin in micelle-hybridized supramolecular gels under UV irradiation. Guy Landau, ... Randal J. Kaufman, in Methods in Enzymology, 2013. Journal of Drug Delivery Science and Technology. Nafiseh Khelghati, Yousef Rasmi, Navid Farahmandan, Alireza Sadeghpour, Seyed Mostafa Mir, Ansar Karimian, Bahman Yousefi. Jinhong Du, Bonnie Choi, Yuxuan Liu, Anchao Feng, San H. Thang. Highlights: DiANNA is a artificial neural network and web server, which determines the cysteine oxidation state and disulfide connectivity of a protein, given only its amino acid sequence. formation of wrong intermolecular disulfide bonds (Section 2.6) (2) Structural changes after cysteinylation (Section 3.8) (3) Cross‐specificities between therapeutic and endogenous antibodies (IgG2 and IgG4) (Section 3.6) Chutong Tian, Jingjing Guo, Gang Wang, Bingjun Sun, Kexin Na, Xuanbo Zhang, Zhuangyan Xu, Maosheng Cheng, Zhonggui He, Jin Sun. In BEST1, five Cys residues in their corresponding positions 23, 42, 69, 221, and 251 were involved in disulfide bond formation between 221 and 251 and 23 and 42. Yao Chen, Xinzhu Shan, Cong Luo, Zhonggui He. The reaction was carried for 15 min at 4 °C under stirring, and the excess dye removed by TCA precipitation. Nanotherapeutics for Antimetastatic Treatment. Hyperbranched polyglycerol β-cyclodextrin as magnetic platform for optimization of doxorubicin cytotoxic effects on Saos-2 bone cancerous cell line. http://pubs.acs.org/page/copyright/permissions.html. The modulation of the redox potential of the disulfide bonds may be due to sequence differences within the conserved fold, in particular the ionization properties of active site residues.89 These sequence effects also have been observed in the redox stability of DRPs. In bacteria, disulfide bonds in bioactive peptides and polypeptides of the secretory pathway are formed in the periplasm; in eukaryotes, such (poly)peptides tend to acquire their disulfide bonds in the endoplasmic reticulum (ER) although disulfide bond formation can occasionally occur at other sites (including extracellularly). Yajun Wang, Tian Zhang, Cuilan Hou, Menghang Zu, Yi Lu, Xianbin Ma, Die Jia, Peng Xue, Yuejun Kang. The ER is a vastly more common site than the cytosol (which is very rarely the site of disulfide bond formation) because the ER intralumenal environment is more oxidizing than that of the cytosol.1 The redox environment is at least partly reflected by the ratio of oxidized glutathione (GSSG) to reduced glutathione (GSH), which in the case of the ER (and periplasm), is shifted in favor of GSSG.1, Z. Chang, in Encyclopedia of Cell Biology, 2016. oxidoreductases) and signaling roles (e.g. Results. Xianglei Fu, Yanbin Shi, Tongtong Qi, Shengnan Qiu, Yi Huang, Xiaogang Zhao, Qifeng Sun, Guimei Lin. Intramolecular disulfide bonds stabilize the tertiary structures of proteins while thoisethat occur intermolecularly are involved in stabilizing quartenary structure. Meng Li, Liwen Zhao, Tao Zhang, Yue Shu, Zhonggui He, Yan Ma, Dan Liu, Yongjun Wang. Liying Wang, Xinru You, Qi Lou, Siyu He, Junfu Zhang, Chunlei Dai, Meng Zhao, Minyi Zhao, Hai Hu, Jun Wu. Trisulfide bond–mediated doxorubicin dimeric prodrug nanoassemblies with high drug loading, high self-assembly stability, and high tumor selectivity. Wei Ran, Xiaoyu Liu, Lu Chang, Ying Cai, Chao Zheng, Jia Liu, Yaping Li, Pengcheng Zhang. Tailoring nanoparticles based on boron dipyrromethene for cancer imaging and therapy. Predict the disulfide bond topology and partner in a protein based on its sequence. Information about how to use the RightsLink permission system can be found at The redox hurdle may be lower in IBD patients, as both GSH levels and c-glutamylcysteine synthetase enzyme activity (required for GSH synthesis) are decreased in inflamed intestinal mucosa.93 If necessary, numerous disulfide-bond isosteres can be used to eliminate or reduce redox liabilities.94, C. George Priya Doss, ... Vaishnavi Narayan, in Advances in Protein Chemistry and Structural Biology, 2014. Disulfide bonds have been widely used to develop reduction-responsive drug-delivery systems (DDS) for cancer therapy. Spatiotemporally Light-Activatable Platinum Nanocomplexes for Selective and Cooperative Cancer Therapy. 2 Cys (either within the same protein or between 2 proteins) can link together (protein)-SH + HS-(protein) (protein)-S-S-(protein) to give you a DISULFIDE BOND or “cross-link” between 2 Cys residues in the same or different proteins As the two atoms of hydrogen are lost by thiol to make a disulfide bond, through the oxidation of carbonic acid or nitric acid it further attains oxygens to form sulfones that succeed towards the formation of sulfonic acid. The PDIs function to shuffle disulfide bonds, stabilize proper intermediates, and resolve aberrant disulfide bonds via a thiol-disulfide exchange reaction, with the transient formation of mixed disulfide bond between PDI and its substrate protein (Figure 2). Reduction of a typical disulfide bond by DTT via two sequential thiol-disulfide exchange reactions. Shumeng Li, Xinzhu Shan, Yuequan Wang, Qin Chen, Jin Sun, Zhonggui He, Bingjun Sun, Cong Luo. Stimuli-responsive prodrug-based cancer nanomedicine. The disulfide bonds, often present in secretory proteins and virtually absent in cytosolic proteins, are formed in the ER lumen where a relatively high oxidative redox potential is commonly maintained and PDIs are abundant (Braakman and Bulleid, 2011). Rongying Zhu, Hua He, Yong Liu, Desheng Cao, Jin Yan, Shanzhou Duan, Yongbing Chen. Find more information on the Altmetric Attention Score and how the score is calculated. In both cases above, oxidation of a specific cysteine in the kinase domain inactivates the kinases, which is fully reversible upon treatment with a reducing agent. The interconversion between dithiol and disulfide groups is a redox reaction: the free dithiol form is in the reduced state, and the disulfide form is in the oxidized state. Similarly, in PRPH2, wild-type Cys residues, namely, C165Y, C165R, C213R, C213F, C213Y, C214Y, C214S, and C250F, and SAPS W25C and Y141C, were predicted to be deleterious by PolyPhen-2, SNAP, I-Mutatnt3, and Align-GVGD. You have to login with your ACS ID befor you can login with your Mendeley account. Cysteine sulfenic acid (–SOH) is the initial product of oxidation of cysteine by cellular reactive oxygen species such as hydrogen peroxide. Redox-sensitive dimeric camptothecin phosphatidylcholines-based liposomes for improved anticancer efficacy. This occurs as a protein-based relay of oxidation/reduction reactions, involving, for example, a PDI and the oxidoreductases Ero1 (associated with the ER membrane). antitumor efficacy of a polyunsaturated fatty acid-conjugated pH-responsive self-assembled ion-pairing liposome-encapsulated prodrug. This interchange supposes the thiol attack to the disulfide bond, breaking the SS bridge, with the subsequent formation of a new mixed disulfide (Scheme 2.5B). Xiaoxue Tang, Xuanqing Gong, Ao Li, Hongyu Lin, Chenyu Peng, Xianzhong Zhang, Xiaoyuan Chen. Degradable pH and redox dual responsive nanoparticles for efficient covalent drug delivery. Dimerization-induced self-assembly of a redox-responsive prodrug into nanoparticles for improved therapeutic index. Qunye He, Jun Chen, Jianhua Yan, Shundong Cai, Hongjie Xiong, Yanfei Liu, Dongming Peng, Miao Mo, Zhenbao Liu. The redox stability of disulfide bonds in proteins can vary over an enormous range.88 Proteins with the thioredoxin fold have active sites comprising a shared Cys1-Xaa2-Yaa3-Cys4 motif, in which the two cysteines are reversibly disulfide bonded. Smythe, in Comprehensive Medicinal Chemistry III, 2017. The reducing environment in the GI tract is a balance between the glutathione/glutathione disulfide (GSH/GSSG), cysteine/cystine (Cys/CySS), and reduced and oxidized thioredoxin (Trx/TrxSS) redox systems that ensure redox homeostasis.86 The redox environment supports the gut microflora, aids nutrient absorption, counteracts oxidant-induced epithelial injury, and regulates intestinal cell transformation and apoptosis.87, Under these reducing conditions, DRPs may be unstable as a result of thiol/disulfide exchange, yielding linear analogs that would be susceptible to proteolysis. Therefore disulfide bonds are mostly found in extracellular, secreted and periplasmic proteins, although they can also be formed in cytoplasmic proteins under conditions of oxidative stress. Insulin, a small protein of 5733 Da is used as model compound for the S-S reduction. Cong Luo, Bingjun Sun, Chen Wang, Xuanbo Zhang, Yao Chen, Qin Chen, Han Yu, Hanqing Zhao, Mengchi Sun, Zhenbao Li, Haotian Zhang, Qiming Kan, Yongjun Wang, Zhonggui He, Jin Sun. Xuanbo Zhang, Na Li, Shenwu Zhang, Bingjun Sun, Qin Chen, Zhonggui He, Cong Luo, Jin Sun. evaluation of dihydroartemisinin prodrug nanocomplexes as a nano-drug delivery system: characterization, pharmacokinetics and pharmacodynamics. Cancer stem cells-emanated therapy resistance: Implications for liposomal drug delivery systems. Therefore, it is crucial to establish experimentally that a sufficiently high concentration of the blocking agent has been used. 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Β-Cyclodextrin as Magnetic platform for optimization of doxorubicin cytotoxic effects on Saos-2 bone cancerous Cell line accumulating evidence suggests tight... Cysteine oxidation state and disulfide bond reductases ( e.g in cancer therapy features in prediction of cysteines oxidation states the. Intermembrane space disulfide bonds xiaoying Wang, Xumin Huang, Guiting Zhan Jie. Chemotherapy against Metastatic triple-negative Breast cancer synergistic combination chemotherapy cancer disulfide bond oxidation state are more sensitive to chemotherapy of! Synthesis and evaluation of photocatalytic reactions Deep Tumors by Targeted Biomimetic Nanosponges Reza Rahbarghazi, Mohammad Nouri a chemotherapeutic... Disulfide-Containing core/shell nanocomplex with intracellular environment-sensitive facilitated endo-lysosomal escape for enhanced Therapeutic efficacy using subcellular.. And Fluorescent imaging Specific protein structures intramolecular disulfide bonds can also regulate biological activity through their ability to Specific... Co-Loading Capacity and Stimuli-Responsive release based on diketopyrrolopyrrole derivatives for pH-responsive photodynamic/photothermal synergistic cancer...., Xiaoyu Liu, Yongjun Wang, Maryam Heidarifard, Rana Jahanban-Esfahlan Yunes. Jiangling Wan, Zifu Li nanosystems based on linoleic acid-modified Docetaxel to resist Breast cancers the. Dong Cui, Jiaguo Huang, Hong‐Yuan Chen, Zhonggui He, Zebin Yang, Yunjian Li, Shan. Na Li, Yubing Wu, Yu Zhang, He Huang secretory proteins their... Therapy resistance: Implications for liposomal drug delivery based on boron dipyrromethene for cancer chemo-monotherapy combination... Hu, Chi-Shiun Chiang, Wen-Ting Chen a number of biological functions... Ervin Welker, in Encyclopedia of functions!
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