Results 61 to 70 of about 86,419 (320)
N-glycosylation of the protein disulfide isomerase Pdi1 ensures full Ustilago maydis virulence
PLoS Pathogens, 2019 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
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
openaire +2 more sources
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
doaj +1 more source
Oxidative protein folding in the mitochondrial intermembrane space [PDF]
, 2010 Disulfide bond formation is a crucial step for oxidative folding and necessary for the acquisition of a protein's native conformation. Introduction of disulfide bonds is catalyzed in specialized subcellular compartments and requires the coordinated ...
Anfinsen CB +4 more
core +1 more source
Cancer Research, 2019 Patients with glioblastoma multiforme (GBM) survive on average 12 to 14 months after diagnosis despite surgical resection followed by radiotheraphy and temozolomide therapy.
Yajing Liu +9 more
semanticscholar +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
doaj +1 more source
Protein disulfide isomerase plays a crucial role in mediating chemically-induced, glutathione depletion-associated hepatocyte injury in vitro and in vivo [PDF]
Cell Commun SignalYan-Yin Zhu +4 more
openalex +2 more sources
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
core +3 more sources
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
Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation [PDF]
, 2008 The activation of initiator protein tissue factor (TF) is likely to be a crucial step in the blood coagulation process, which leads to fibrin formation. The stimuli responsible for inducing TF activation are largely undefined.
Altmann, Berid +13 more
core +3 more sources