Results 41 to 50 of about 21,311 (187)
Soluble expression of human leukemia inhibitory factor with protein disulfide isomerase in Escherichia coli and its simple purification. [PDF]
PLoS ONE, 2013 Human leukemia inhibitory factor (hLIF) is a multifunctional cytokine that is essential for maintaining the pluripotency of embryonic stem cells. hLIF may be also be useful in aiding fertility through its effects on increasing the implantation rate of ...
Jung-A Song +12 more
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Influence of the Season and Region Factor on Phosphoproteome of Stallion Epididymal Sperm
Animals, 2021 Epididymal maturation can be defined as a scope of changes occurring during epididymal transit that prepare spermatozoa to undergo capacitation. One of the most common post-translational modifications involved in the sperm maturation process and their ...
Katarzyna Dyrda +3 more
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Functional Differences in Yeast Protein Disulfide Isomerases [PDF]
The Journal of Cell Biology, 2001 PDI1 is the essential gene encoding protein disulfide isomerase in yeast. The Saccharomyces cerevisiae genome, however, contains four other nonessential genes with homology to PDI1: MPD1, MPD2, EUG1, and EPS1. We have investigated the effects of simultaneous deletions of these genes. In several cases, we found that the ability of the PDI1 homologues to
P, Nørgaard +5 more
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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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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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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
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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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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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Proteins, Processing, and Properties of Adhesive Fluid Condensates Purified from Mussels
Advanced Functional Materials, EarlyView.Mussels exhibit an unmatched proficiency for adhering to wet surfaces in salty environments—a remarkable ability that could inspire new biomedical and technical glues. The fluid protein condensates used to form the underwater mussel glue are extracted, reconstituted and characterized with advanced spectroscopy and nanomechanical analysis, revealing ...
Mathieu D. Rivard +8 more
wiley +1 more source