Zobrazeno 1 - 10
of 1 079
pro vyhledávání: '"oxidative folding"'
Autor:
Bo Ma, Jinyuan Gong, Xin Li, Wenqiang Liu, Baoquan Chen, Zijian Lai, Shiying Shang, Yaohao Li, Jian Yin, Zhongping Tan
Publikováno v:
Results in Chemistry, Vol 6, Iss , Pp 101017- (2023)
Chemical synthesis has become an increasing popular approach for the production of proteins because of its flexibility and convenience in changing protein sequence and/or structure. However, at present, the efficiency of protein chemical synthesis is
Externí odkaz:
https://doaj.org/article/6d9e73af45ca47a6ad5037be19e87099
Publikováno v:
Microbial Cell Factories, Vol 21, Iss 1, Pp 1-12 (2022)
Abstract Background Escherichia coli is of central interest to biotechnological research and a widely used organism for producing proteins at both lab and industrial scales. However, many proteins remain difficult to produce efficiently in E. coli. T
Externí odkaz:
https://doaj.org/article/cb5a42f6086844d58eac50577ef0b87b
Autor:
Lisa R. Knoke, Jannik Zimmermann, Natalie Lupilov, Jannis F. Schneider, Beyzanur Celebi, Bruce Morgan, Lars I. Leichert
Publikováno v:
Redox Biology, Vol 64, Iss , Pp 102800- (2023)
The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative power and the DsbC/D system as its complement for isomerization of non-native disulfides. While the standard redox potentials of those systems are known, the
Externí odkaz:
https://doaj.org/article/23ab879427414116a4b54b45848aa989
Publikováno v:
Antioxidants, Vol 12, Iss 11, p 1949 (2023)
Protein import and oxidative folding within the intermembrane space (IMS) of mitochondria relies on the MIA40–ERV1 couple. The MIA40 oxidoreductase usually performs substrate recognition and oxidation and is then regenerated by the FAD-dependent ox
Externí odkaz:
https://doaj.org/article/6e01a29f4a7643ffb2f08d6fd7c7b65f
Autor:
Ersilia Varone, Alexander Chernorudskiy, Alessandro Cherubini, Angela Cattaneo, Angela Bachi, Stefano Fumagalli, Gizem Erol, Marco Gobbi, Michael J. Lenardo, Nica Borgese, Ester Zito
Publikováno v:
Redox Biology, Vol 56, Iss , Pp 102455- (2022)
N-glycosylation and disulfide bond formation are two essential steps in protein folding that occur in the endoplasmic reticulum (ER) and reciprocally influence each other. Here, to analyze crosstalk between N-glycosylation and oxidation, we investiga
Externí odkaz:
https://doaj.org/article/d175f4e69c8544f7a0d915547de36689
Publikováno v:
Molecules, Vol 28, Iss 8, p 3377 (2023)
In the chemical synthesis of conotoxins with multiple disulfide bonds, the oxidative folding process can result in diverse disulfide bond connectivities, which presents a challenge for determining the natural disulfide bond connectivities and leads t
Externí odkaz:
https://doaj.org/article/eced192c49f84deebb9db0d3ce85bc70
Autor:
Balamurugan Dhayalan, Michael D. Glidden, Alexander N. Zaykov, Yen-Shan Chen, Yanwu Yang, Nelson B. Phillips, Faramarz Ismail-Beigi, Mark A. Jarosinski, Richard D. DiMarchi, Michael A. Weiss
Publikováno v:
Frontiers in Endocrinology, Vol 13 (2022)
The mutant proinsulin syndrome is a monogenic cause of diabetes mellitus due to toxic misfolding of insulin’s biosynthetic precursor. Also designated mutant INS-gene induced diabetes of the young (MIDY), this syndrome defines molecular determinants
Externí odkaz:
https://doaj.org/article/ac8abdb348a7445ab68c20aba3dbef24
Autor:
Yanwu Yang, Michael D. Glidden, Balamurugan Dhayalan, Alexander N. Zaykov, Yen-Shan Chen, Nalinda P. Wickramasinghe, Richard D. DiMarchi, Michael A. Weiss
Publikováno v:
Frontiers in Endocrinology, Vol 13 (2022)
Toxic misfolding of proinsulin variants in β-cells defines a monogenic diabetes syndrome, designated mutant INS-gene induced diabetes of the young (MIDY). In our first study (previous article in this issue), we described a one-disulfide peptide mode
Externí odkaz:
https://doaj.org/article/81bdb69b388b4048aa3b5feb43d1bcd4
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