Results 121 to 130 of about 97,846 (317)

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

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 Role of Oxidative Stress in Periodontitis

Journal of Periodontal Research, EarlyView.
Oxidative stress is involved in multiple chemical reactions that take place in different intracellular organelles: mitochondria, rough endoplasmic reticulum, peroxisomes, autophagy, and aging, and can be influenced by exogenous factors: nutrition, physical activity, psychological status, environmental conditions, microbiome, and drugs.
Pedro Bullon, Francesca Giampieri, Beatriz Bullon, Maurizio Battino   +3 more
wiley   +1 more source

The Unfolded Protein Response and the Role of Protein Disulfide Isomerase in Neurodegeneration

Front. Cell Dev. Biol., 2016
The maintenance and regulation of proteostasis is a critical function for post-mitotic neurons and its dysregulation is increasingly implicated in neurodegenerative diseases. Despite having different clinical manifestations, these disorders share similar
E. Perri, Colleen J. Thomas, S. Parakh, D. Spencer, J. Atkin   +4 more
semanticscholar   +1 more source

Stage-specific proteomes from onchocerca ochengi, sister species of the human river blindness parasite, uncover adaptations to a nodular lifestyle [PDF]

, 2016
Despite 40 years of control efforts, onchocerciasis (river blindness) remains one of the most important neglected tropical diseases, with 17 million people affected.
Adam, Altschul, Altschul, Anon, Argueta, Armstrong, Armstrong, Arumugam, Babayan, Bazzocchi, Bendtsen, Benjamini, Bennuru, Bennuru, Berry, Berry, Board, Boatin, Brattig, Brattig, Brophy, Bulman, Burbelo, Burchard, Burket, Butler, Chandrashekar, Chawade, Chhabra, Choi, Claros, Constam, Cooray, Crump, Darby, Darby, Desjardins, Duckert, Edgar, Edwards, Erttmann, Finn, Franceschini, Frank, Gallin, Gardon, GBD 2013 Mortality and Causes of Death Collaborators, Geary, Ghali, Ghedin, Ghosh, Gilbert, Globisch, Godel, Gomez-Escobar, Gopal, Gotenstein, Gottsch, Grainger, Gretes, Guan, Guiliano, Hansen, Henrichfreise, Hewitson, Hewitson, Hewitson, Hotez, Hunter, Ichishita, Joseph, Joza, Kanazawa, Klion, Ko, Koonin, Korten, Krogh, Larkin, Li, Li, Liebau, Liebau, Liebau, Liebau, Littler, Liu, Longo, Lu, Lundquist, Lustigman, Lustigman, Mackenzie, Makepeace, Marti, McGarry, McSorley, Melnikow, Meyer, Michalski, Morales-Hojas, Moreno, Moreno, Morris, Mossmann, Nana-Djeunga, Nfon, Nicholson, Nomura, Ohtsuki, Ohtsuki, Osei-Atweneboana, Page, Pant, Parra, Petersen, Plaisier, Quintana, Ranjan, Rew, Rogalski, Roth, Saitou, Schulz-Key, Schulz-Key, Scocchi, Sheehan, Silva, Sommer, Srivastava, Tamarozzi, Tanikawa, Taylor, Tchakouté, Ternent, Tew, Thompson, Tiwari, Trees, Vogel, Wahl, Waterhouse, Westermann, Wildenburg, Willenbucher, Wilson, Wisniewski, Wu, Wu, Xie, Xie, Yamaguchi, Yang, Yasuda, Zanetti, Zipfel   +155 more
core   +6 more sources

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

Unfolding Plant Defence: Endoplasmic Reticulum Stress Signalling at the Plant‐Pathogen Interface

Plant Biotechnology Journal, EarlyView.
ABSTRACT The endoplasmic reticulum (ER) stress response, a conserved proteostasis network, has emerged as a central hub that reprograms plant immunity during pathogen attack. This review synthesises how plants harness ER‐stress signalling to mount multilayered defences and how pathogens have evolved counterstrategies to subvert these pathways.
Zhe Meng, Shuqin Zheng, Federica Brandizzi, Yiran Liu, Chunlei Li, Congcong Ai, Yujiao Wang, Jiadong Qi, Xiuguo Zhang   +8 more
wiley   +1 more source

Protein Disulfide Isomerase Modulates the Activation of Thyroid Hormone Receptors

Frontiers in Endocrinology, 2019
Thyroid hormone receptors (TRs) are responsible for mediating thyroid hormone (T3 and T4) actions at a cellular level. They belong to the nuclear receptor (NR) superfamily and execute their main functions inside the cell nuclei as hormone-regulated ...
Jessica L. O. Campos, Jessica L. O. Campos, Tabata R. Doratioto, Tabata R. Doratioto, Natalia B. Videira, Natalia B. Videira, Helder V. Ribeiro Filho, Helder V. Ribeiro Filho, Fernanda A. H. Batista, Juliana Fattori, Nathalia de C. Indolfo, Nathalia de C. Indolfo, Marcel Nakahira, Marcio C. Bajgelman, Aleksandra Cvoro, Francisco R. M. Laurindo, Paul Webb, Ana Carolina M. Figueira   +17 more
doaj   +1 more source

Selective Inhibition of Protein Disulfide Isomerase by Estrogens

Journal of Biological Chemistry, 1989
Protein disulfide isomerase (PDI) is a multifunctional microsomal enzyme that participates in the formation of protein disulfide bonds. PDI catalyzes the reduction of protein disulfide bonds in the presence of excess reduced glutathione and has been implicated in the reductive degradation of insulin; E.
J C, Tsibris, L T, Hunt, G, Ballejo, W C, Barker, L J, Toney, W N, Spellacy   +5 more
openaire   +2 more sources

High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility [PDF]

, 2013
ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist of two thioredoxinfold domains homologous with the non-catalytic b and b domains of ...
A. Katrine Wallis, Alanen, Barak, Barbato, Brünger, Byrne, Cornilescu, Delaglio, Denisov, Ellgaard, Freedman, Guddat, Holm, Jacobs, Jansen, Jimenez-Roldan, Kemmink, Klappa, Kober, Koradi, Kozlov, Kozlov, Kozlov, Lappi, Laskowski, Laskowski, Li, Lipari, Lipari, Mark J. Howard, Michelle L. Rowe, Nader T. Amin, Neuhaus, Nguyen, Palmer, Piotto, Richard A. Williamson, Rieping, Robert B. Freedman, Rowe, States, Stephen A. Wells, Suhre, Tian, Wallis, Wang, Wang, Waters, Wells, Wells, Williamson, Wim, Wishart   +52 more
core   +5 more sources