Results 31 to 40 of about 43,163 (273)

Participation of the endoplasmic reticulum protein chaperone thio-oxidoreductase in gonadotropin-releasing hormone receptor expression at the plasma membrane

Brazilian Journal of Medical and Biological Research, 2009
Chaperone members of the protein disulfide isomerase family can catalyze the thiol-disulfide exchange reaction with pairs of cysteines. There are 14 protein disulfide isomerase family members, but the ability to catalyze a thiol disulfide exchange ...
W. Lucca-Junior, J.A. Janovick, P.M. Conn   +2 more
doaj   +1 more source

Protein disulfide isomerase family member 4 promotes triple-negative breast cancer tumorigenesis and radiotherapy resistance through JNK pathway. [PDF]

Breast Cancer Res
Tao J, Xue C, Cao M, Ye J, Sun Y, Chen H, Guan Y, Zhang W, Zhang W, Yao Y.   +9 more
europepmc   +3 more sources

Redox Control of Exofacial Protein Thiols/Disulfides by Protein Disulfide Isomerase [PDF]

Journal of Biological Chemistry, 1999
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, M, Fitzgerald, C M, Grant, P J, Hogg   +3 more
openaire   +2 more sources

Murine tissue factor coagulant activity is critically dependent on the presence of an intact allosteric disulfide

Haematologica, 2013
Tissue factor activation (decryption) has been proposed to be dependent on the cysteine 186-cysteine 209 allosteric disulfide in the tissue factor extracellular domain.
Lisa G. van den Hengel, Susanne Osanto, Pieter H. Reitsma, Henri H. Versteeg   +3 more
doaj   +1 more source

Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space [PDF]

, 2016
Mitochondria are organelles that play a central role in cellular metabolism, as they are responsible for processes such as iron/sulfur cluster biogenesis, respiration and apoptosis.
MacPherson, Lisa, Manganas, Phanee, Tokatlidis, Kostas   +2 more
core   +1 more source

Protein disulfide isomerase interacts with tau protein and inhibits its fibrillization. [PDF]

PLoS ONE, 2013
BACKGROUND: Tau protein is implicated in the pathogenesis of neurodegenerative disorders such as tauopathies including Alzheimer disease, and Tau fibrillization is thought to be related to neuronal toxicity. Physiological inhibitors of Tau fibrillization
Li-Rong Xu, Xiao-Ling Liu, Jie Chen, Yi Liang   +3 more
doaj   +1 more source

Prolyl 4-hydroxlase activity is essential for development and cuticle formation in the human infective parasitic nematode Brugia malayi [PDF]

, 2013
Collagen prolyl 4-hydroxylases (C-P4H) are required for formation of extracellular matrices in higher eukaryotes. These enzymes convert proline residues within the repeat regions of collagen polypeptides to 4-hydroxyproline, a modification essential for ...
Alan D. Winter, Antony P. Page, Bendtsen, Cox, Ellgaard, Evans, Ghedin, Gillian McCormack, Hotez, Jex, Johanna Myllyharju, John, Kamath, Kelly, Kivirikko, Koivunen, Lamberg, Landmann, Lappi, Lok, Maule, Merriweather, Mitreva, Myllyharju, Myllyharju, Myllyharju, Opperman, Ottesen, Page, Petralanda, Pirneskoski, Rajan, Riihimaa, Stiernagle, Takacs, Timmons, Wang, Winter, Winter, Winter, Winter   +40 more
core   +1 more source

Recognition and ER Quality Control of Misfolded Formylglycine-Generating Enzyme by Protein Disulfide Isomerase

Cell Reports, 2018
Summary: Multiple sulfatase deficiency (MSD) is a fatal, inherited lysosomal storage disorder characterized by reduced activities of all sulfatases in patients.
Lars Schlotawa, Michaela Wachs, Olaf Bernhard, Franz J. Mayer, Thomas Dierks, Bernhard Schmidt, Karthikeyan Radhakrishnan   +6 more
doaj   +1 more source

Expression of Functional Human Sialyltransferases ST3Gal1 and ST6Gal1 in Escherichia coli. [PDF]

PLoS ONE, 2016
Sialyltransferases (STs) are disulfide-containing, type II transmembrane glycoproteins that catalyze the transfer of sialic acid to proteins and lipids and participate in the synthesis of the core structure oligosaccharides of human milk.
Maria Elena Ortiz-Soto, Jürgen Seibel
doaj   +1 more source

Roles of Protein Disulfide Isomerase in Breast Cancer [PDF]

Cancers, 2022
Protein disulfide isomerase (PDI) is the endoplasmic reticulum (ER)’s most abundant and essential enzyme and serves as the primary catalyst for protein folding. Due to its apparent role in supporting the rapid proliferation of cancer cells, the selective blockade of PDI results in apoptosis through sustained activation of UPR pathways. The functions of
Suhui Yang, Chanel Jackson, Eduard Karapetyan, Pranabananda Dutta, Dulcie Kermah, Yong Wu, Yanyuan Wu, John Schloss, Jaydutt V. Vadgama   +8 more
openaire   +2 more sources