Results 51 to 60 of about 43,163 (273)
Molecules, 2021 Oxidative protein folding is a biological process to obtain a native conformation of a protein through disulfide-bond formation between cysteine residues.
Shunsuke Okada +3 more
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Disulphide production by Ero1alpha-PDI relay is rapid and effectively regulated [PDF]
, 2010 The molecular networks that control endoplasmic reticulum (ER) redox conditions in mammalian cells are incompletely understood. Here, we show that after reductive challenge the ER steady-state disulphide content is restored on a time scale of seconds ...
Appenzeller-Herzog, Christian +6 more
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Interaction of Calreticulin with Protein Disulfide Isomerase [PDF]
Journal of Biological Chemistry, 1995 We report here that calreticulin interacts with protein disulfide isomerase (PDI). The PDI-calreticulin complex can be dissociated by Zn(2+)-iminodiacetate-substituted Sepharose-agarose chromatography, suggesting that these interactions may be Zn2+-dependent.
S, Baksh +3 more
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Oxidative Protein-Folding Systems in Plant Cells
International Journal of Cell Biology, 2013 Plants are unique among eukaryotes in having evolved organelles: the protein storage vacuole, protein body, and chloroplast. Disulfide transfer pathways that function in the endoplasmic reticulum (ER) and chloroplasts of plants play critical roles in the
Yayoi Onda
doaj +1 more source
The role and mechanism of TXNDC5 in diseases
European Journal of Medical Research, 2022 Thioredoxin domain-containing protein 5 (TXNDC5) is a member of the protein disulfide isomerase (PDI) family. It can promote the formation and rearrangement of disulfide bonds, ensuring proper protein folding. TXNDC5 has three Trx-like domains, which can
Xueling Wang, Haoran Li, Xiaotian Chang
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Inactivation of mammalian Ero 1α is catalysed by specific protein disulfide isomerases [PDF]
, 2014 Disulfide formation within the endoplasmic reticulum is a complex process requiring a disulfide exchange protein such as protein disulfide isomerase and a mechanism to form disulfides de novo.
Appenzeller-Herzog +22 more
core +1 more source
Engineered Pathways for Correct Disulfide Bond Oxidation [PDF]
, 2011 Correct formation of disulfide bonds is critical for protein folding. We find that cells lacking protein disulfide isomerases (PDIs) can use alternative mechanisms for correct disulfide bond formation.
Bardwell, James C. A., Ren, Guoping
core +2 more sources
Microbial Cell Factories, 2011 Background Disulfide bonds are one of the most common post-translational modifications found in proteins. The production of proteins that contain native disulfide bonds is challenging, especially on a large scale.
Enlund Eveliina +5 more
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Cell Propagation of Cholera Toxin CTA ADP-Ribosylating Factor by Exosome Mediated Transfer [PDF]
, 2018 In this study, we report how the cholera toxin (CT) A subunit (CTA), the enzyme moiety responsible for signaling alteration in host cells, enters the exosomal pathway, secretes extracellularly, transmits itself to a cell population.
Boussadia, Zaira +11 more
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Substrate recognition by the protein disulfide isomerases [PDF]
The FEBS Journal, 2007 Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role.
Hatahet Feras, Ruddock Lloyd
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