Arginyltransferase, Its Specificity, Putative Substrates, Bidirectional Promoter, and Splicing-derived Isoforms [PDF]
Substrates of the N-end rule pathway include proteins with destabilizing N-terminal residues. Three of them, Asp, Glu, and (oxidized) Cys, function through their conjugation to Arg, one of destabilizing N-terminal residues that are recognized directly by
Brower, Christopher S. +7 more
core +2 more sources
Soluble expression of human leukemia inhibitory factor with protein disulfide isomerase in Escherichia coli and its simple purification. [PDF]
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
doaj +1 more source
Redox Control of Exofacial Protein Thiols/Disulfides by Protein Disulfide Isomerase [PDF]
Protein disulfide isomerase (PDI) facilitates proper folding and disulfide bonding of nascent proteins in the endoplasmic reticulum and is secreted by cells and associates with the cell surface. We examined the consequence of over- or underexpression of PDI in HT1080 fibrosarcoma cells for the redox state of cell-surface protein thiols/disulfides ...
X M, Jiang +3 more
openaire +2 more sources
ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor [PDF]
ERdj5 is a member of the protein disulfide isomerase family of proteins localized to the endoplasmic reticulum (ER) of mammalian cells. To date, only a limited number of substrates for ERdj5 are known.
Braakman, Ineke +4 more
core +1 more source
SUMMARY Mitochondrial dynamics are tightly controlled by fusion and fission, and their dysregulation and excess reactive oxygen species (ROS) contribute to endothelial cell (EC) dysfunction.
Young-Mee Kim +15 more
semanticscholar +1 more source
Correct folding of nascent peptides occurs in the endoplasmic reticulum (ER). It is a complicate process primarily accomplished by the coordination of multiple redox proteins including members of the protein disulfide isomerase (PDI) family.
Hedy A. Chawsheen +3 more
doaj +1 more source
Analysis of the interaction of calcitriol with the disulfide isomerase ERp57 [PDF]
Calcitriol, the active form of vitamin D3, can regulate the gene expression through the binding to the nuclear receptor VDR, but it can also display nongenomic actions, acting through a membrane- associated receptor, which has been discovered as the ...
Altieri, Fabio +7 more
core +1 more source
N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
Fungal pathogenesis depends on accurate secretion and location of virulence factors which drive host colonization. Protein glycosylation is a common posttranslational modification of cell wall components and other secreted factors, typically required for
Miriam Marín-Menguiano +4 more
semanticscholar +1 more source
Influence of the Season and Region Factor on Phosphoproteome of Stallion Epididymal Sperm
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
doaj +1 more source
Protein disulfide isomerase as an antithrombotic target [PDF]
Protein disulfide isomerase (PDI) is a ubiquitously expressed oxidoreductase required for proper protein folding. It is highly concentrated in the endoplasmic reticulum, but can also be released into the extracellular environment. Several in vivo thrombosis models have demonstrated that vascular PDI secreted by platelets and endothelial cells is ...
openaire +2 more sources

