Results 121 to 130 of about 86,419 (320)

Mechanisms of Disulfide Bond Formation in Nascent Polypeptides Entering the Secretory Pathway

Cells, 2020
Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER).
Philip J. Robinson, Neil J. Bulleid
doaj   +1 more source

Biochemical analysis of Komagataella phaffii oxidative folding proposes novel regulatory mechanisms of disulfide bond formation in yeast

Scientific Reports, 2023
Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide isomerase PDI and oxidoreductin Ero1. Their activity is tightly regulated and interconnected with the unfolded protein response (UPR).
Arianna Palma, Lukas A. Rettenbacher, Antti Moilanen, Mirva Saaranen, Christian Pacheco-Martinez, Brigitte Gasser, Lloyd Ruddock   +6 more
doaj   +1 more source

A humanized monoclonal antibody that inhibits platelet-surface ERp72 reveals a role for ERp72 in thrombosis [PDF]

, 2017
Background: Within the endoplasmic reticulum, thiol isomerase enzymes modulate the formation and rearrangement of disulphide bonds in newly folded proteins entering the secretory pathway to ensure correct protein folding.
Bicknell, A. B., Flora, G. D., Gibbins, J. M., Holbrook, L., Sahli, K., Sandhar, G. K., Sasikumar, P., Schenk, M. P., Stainer, A. R.   +8 more
core   +1 more source

DsbG, a Protein Disulfide Isomerase with Chaperone Activity [PDF]

Journal of Biological Chemistry, 2000
DsbG, a protein disulfide isomerase present in the periplasm of Escherichia coli, is shown to function as a molecular chaperone. Stoichiometric amounts of DsbG are sufficient to prevent the thermal aggregation of two classical chaperone substrate proteins, citrate synthase and luciferase.
F, Shao, M W, Bader, U, Jakob, J C, Bardwell   +3 more
openaire   +2 more sources

ER proteostasis meets mitochondrial function: contact sites as hubs of communication and therapeutic targets

The FEBS Journal, EarlyView.
Proteostasis ensures proper protein folding, modification, and degradation, while its impairment triggers ER stress. Chronic ER stress and maladaptive UPR via the CHOP–ERO1 axis remodel ERMCs, altering calcium signaling and mitochondrial metabolism.
Giorgia Maria Renna, Alessandro Cherubini, Ersilia Varone, Serena Germani, Alice Marrazza, Ester Zito   +5 more
wiley   +1 more source

The protein disulfide isomerase 1 of Phytophthora parasitica (PpPDI1) is associated with the haustoria-like structures and contributes to plant infection [PDF]

, 2015
The protein disulfide isomerase (PDI) is a ubiquitous and multifunction enzyme belonging to the thioredoxin (TRX) superfamily, which can reduce, oxidize, and catalyze dithiol-disulfide exchange reactions.
Biao Gu, Guiyan Huang, Meixiang Zhang, Qiang Zhang, Qinhu Wang, Weixing Shan, Yuling Meng   +6 more
core   +2 more sources

The competitive interplay of 12‐oxophytodienoic acid (OPDA), protein thiols, and glutathione

The FEBS Journal, EarlyView.
12‐Oxophytodienoic acid (OPDA) is a phytohormone involved in plant growth and stress defense. Due to its cyclopentenone moiety, OPDA can form Michael adducts with thiol‐containing compounds such as glutathione and cysteine residues of proteins, resulting in alterations of the cellular redox regulatory network.
Madita Knieper, Ruben Schwarz, Lara Vogelsang, Jens Sproß, Armağan Kaya, Maike Bittmann, Harald Gröger, Andrea Viehhauser, Karl‐Josef Dietz   +8 more
wiley   +1 more source

Natural Products Targeting Protein Disulfide Isomerases: New Frontiers for Diabetes, Cancer, and Coagulation

Food Frontiers
The protein disulfide isomerase (PDI) family comprises 21 members that have oxidase, reductase, isomerase, and foldase activities essential for human health and disease. Protein disulfide isomerase A4 (PDIA4) is the largest member in this family.
Yi‐San Lee, Catherine Ortega, Tien‐Fen Kuo, Greta Yang, Wen‐Chin Yang   +4 more
doaj   +1 more source

The Interplay between Chemistry and Mechanics in the Transduction of a Mechanical Signal into a Biochemical Function [PDF]

, 2007
There are many processes in biology in which mechanical forces are generated. Force-bearing networks can transduce locally developed mechanical signals very extensively over different parts of the cell or tissues.
Ainavarapu, Alon, Altmann, Baker, Barakat, Barsegov, Becker, Bell, Best, Best, Bhasin, Braun, Brockwell, Brooks, Brooks, Bruno Samorì, Bryant, Bustamante, Bustanji, Bustanji, Cao, Carl, Carrion-Vazquez, Carson, Chang, Chtcheglova, Cieplak, Cluzel, De Keulenaer, De Los Rios, Dembo, Dettmann, Dietz, Discher, Doggett, Doggett, Dudko, Ericson, Evans, Evans, Evans, Evans, Evans, Evans, Fantner, Fantner, Fenouillet, Fernandez, Finger, Fisher, Fisher, Fowler, Francesco Valle, Fritz, Gao, Grandi, Guo, Heslot, Higgins, Hotchkiss, Hsiai, Hummer, Hyeon, Jackson, Jiang, Julien, Kawakami, Kellermayer, Kozuka, Kung, Lambert-Vidmar, Lawler, Lawrence, Lay, Lee, Lenne, Li, Li, Li, Li, Li, Li, Lincoln, Liphardt, Liphardt, Lou, Lou, Makarov, Marshall, Marszalek, Massimo Sandal, Matouschek, Matthias, Merkel, Mohamed, Morrow, Neupert, Oberhauser, Oberhauser, Pereverzev, Prajapati, Prakash, Qin, Rief, Rief, Rief, Rief, Ritort, Rouzina, Rubartelli, Rubenstein, Samori, Samori, Sandal, Sarasa-Renedo, Sarkar, Sato, Schnepel, Schulze, Schwaiger, Sengupta, Shimaoka, Smith, Smith, Smith, Smith, Stathakis, Stetefeld, Terada, Thirumalai, Thomas, Thomas, Thompson, Viani, Vladescu, Vogel, Vogel, Vologodskii, Waite, Welsh, West, Wiita, Wilcox, Williams, Xie, Xie, Yago, Yan, Yersin, Yoshimori, Yuan, Zhu, Ziegler   +152 more
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Conformational Resilience of Protein Disulfide Isomerase

The FASEB Journal, 2019
Protein disulfide isomerase (PDI) is a 57 kDa protein with both oxidoreductase and chaperone activities that is mainly localized to the endoplasmic reticulum. It is a U‐shaped protein with an abb'xa’ structural organization where the a and
Jessica Guyette, Baggio Evangelista, Suren A. Tatulian, Ken Teter   +3 more
openaire   +1 more source