Results 41 to 50 of about 7,315 (215)

Protein Disulfide Isomerase and Host-Pathogen Interaction [PDF]

The Scientific World JOURNAL, 2011
Reactive oxygen species (ROS) production by immunological cells is known to cause damage to pathogens. Increasing evidence accumulated in the last decade has shown, however, that ROS (and redox signals) functionally regulate different cellular pathways in the host-pathogen interaction.
Beatriz S. Stolf, Ioannis Smyrnias, Lucia R. Lopes, Alcione Vendramin, Hiro Goto, Francisco R. M. Laurindo, Ajay M. Shah, Celio X. C. Santos   +7 more
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Anterior gradient protein 2 promotes survival, migration and invasion of papillary thyroid carcinoma cells [PDF]

, 2014
Through a transcriptome microarray analysis, we have isolated Anterior gradient protein 2 (AGR2) as a gene up-regulated in papillary thyroid carcinoma (PTC).
Chiappetta, G, Di Maro, G, Jarzab, B, Masullo, M, Monaco, M, Oczko-Wojciechowska, M, Orlandella, FM, Salerno, P, Salvatore, G, Santoro, M, Thomas, G, Unger, K   +11 more
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Functional Differences in Yeast Protein Disulfide Isomerases [PDF]

The Journal of Cell Biology, 2001
PDI1 is the essential gene encoding protein disulfide isomerase in yeast. The Saccharomyces cerevisiae genome, however, contains four other nonessential genes with homology to PDI1: MPD1, MPD2, EUG1, and EPS1. We have investigated the effects of simultaneous deletions of these genes. In several cases, we found that the ability of the PDI1 homologues to
P, Nørgaard, V, Westphal, C, Tachibana, L, Alsøe, B, Holst, J R, Winther   +5 more
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Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation [PDF]

, 2017
The relationship between protein synthesis, folding and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested pre-existing disulfide links are absolutely required to allow protein folding and ...
Bulleid, Neil J., Pringle, Marie Anne, Robinson, Philip J., Woolhead, Cheryl A.   +3 more
core   +1 more source

Protein disulfide-isomerase interacts with a substrate protein at all stages along its folding pathway [PDF]

, 2014
In contrast to molecular chaperones that couple protein folding to ATP hydrolysis, protein disulfide-isomerase (PDI) catalyzes protein folding coupled to formation of disulfide bonds (oxidative folding).
A Jansens, A Land, A Pirneskoski, A. Katrine Wallis, Alistair G. Irvine, AR Karala, AR Karala, AY Denisov, B van den Berg, B van den Berg, B van den Berg, CB Anfinsen, Claudia A. Blindauer, CPM van Mierlo, CPM van Mierlo, CW Gruber, DP Goldenberg, E van Anken, F Hatahet, G Kozlov, G Wagner, HC Shin, HC Shin, J Riemer, JH Laity, JL Arolas, JS Weissman, JS Weissman, L Wang, LJ Byrne, Lloyd W. Ruddock, M Narayan, Mark J. Howard, Michelle L. Rowe, Narinder Sanghera, NJ Bulleid, NJ Darby, P Klappa, P Venetianer, RA Williamson, RB Freedman, RF Goldberger, Richard A. Williamson, RJ Ellis, Robert B. Freedman, S Masui, S Talluri, Salvador Ventura, TE Creighton, TE Creighton, TE Creighton, TE Creighton, VD Nguyen, VD Nguyen, WF Vranken   +54 more
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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, K, Burns, C, Andrin, M, Michalak   +3 more
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Myricetin, the Main Flavonoid in Syzygium cumini Leaf, Is a Novel Inhibitor of Platelet Thiol Isomerases PDI and ERp5

Frontiers in Pharmacology, 2020
BackgroundFlavonoids have been characterized as a prominent class of compounds to treat thrombotic diseases through the inhibition of thiol isomerases. Syzygium cumini is a flavonoid-rich medicinal plant that contains myricetin and gallic acid. Little is
Renato Simões Gaspar, Renato Simões Gaspar, Samira Abdalla da Silva, Jennifer Stapleton, João Lucas de Lima Fontelles, Hiran Reis Sousa, Vinicyus Teles Chagas, Shuruq Alsufyani, Andrés Trostchansky, Jonathan M. Gibbins, Antonio Marcus de Andrade Paes   +10 more
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Molecular characterization and expression profiling of the protein disulfide isomerase gene family in Brachypodium distachyon L. [PDF]

PLoS ONE, 2014
Protein disulfide isomerases (PDI) are involved in catalyzing protein disulfide bonding and isomerization in the endoplasmic reticulum and functions as a chaperone to inhibit the aggregation of misfolded proteins. Brachypodium distachyon is a widely used
Chong Zhu, Nana Luo, Miao He, Guanxing Chen, Jiantang Zhu, Guangjun Yin, Xiaohui Li, Yingkao Hu, Jiarui Li, Yueming Yan   +9 more
doaj   +1 more source

Analysis of the interaction of calcitriol with the disulfide isomerase ERp57 [PDF]

, 2016
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, Cervoni, Laura, Chichiarelli, Silvia, Eufemi, Margherita, Gaucci, Elisa, Grillo, Caterina, Nittari, Giulio, Raimondo, Domenico   +7 more
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Substrate recognition by the protein disulfide isomerases [PDF]

The FEBS Journal, 2007
Protein folding in the endoplasmic reticulum is often associated with the formation of native disulfide bonds. Their primary function is to stabilize the folded structure of the protein, although disulfide bond formation can also play a regulatory role.
Hatahet Feras, Ruddock Lloyd
openaire   +2 more sources