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Relevant bibliographies by topics / Protein disulphide isomerase (PDI)

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Academic literature on the topic 'Protein disulphide isomerase (PDI)'

Author: Grafiati

Published: 10 December 2022

Last updated: 29 January 2023

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Journal articles on the topic "Protein disulphide isomerase (PDI)"

1

Tang, B., S. Zhang, and K. Yang. "Assisted refolding of recombinant prochymosin with the aid of protein disulphide isomerase." Biochemical Journal 301, no. 1 (1994): 17–20. http://dx.doi.org/10.1042/bj3010017.

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Protein disulphide isomerase (PDI) was shown to be able to accelerate the refolding of unfolded recombinant prochymosin and to enhance the overall yield of active protein. Unlike previous reports in this study PDI was found to be active at pH values as high as 11. The coincidence of the similar apparent optimum pH values of uncatalysed and PDI-catalysed reactions suggests that conditions favourable to spontaneous refolding of proteins may help PDI to catalyse thiol/disulphide interchange. Under the conditions described here no exogenously added dithiothreitol was required for PDI-catalysed ren

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ROOT, Paul, Inga SLISKOVIC, and Bulent MUTUS. "Platelet cell-surface protein disulphide-isomerase mediated S-nitrosoglutathione consumption." Biochemical Journal 382, no. 2 (2004): 575–80. http://dx.doi.org/10.1042/bj20040759.

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S-nitrosothiols (RSNOs) regulate several aspects of platelet physiology including inhibition of activation, adhesion and aggregation. PDI (protein disulphide-isomerase) has recently been found to be localized to the cell surface, where it exhibits both disulphide-exchange and denitrosation activities. The disulphide-exchange activity of PDI has been linked to aspects of platelet aggregation. The present study suggests that the metabolism of RSNOs by platelets is a function of PDI denitrosation activity. Exposure of washed human platelets to increasing concentrations of GSNO (S-nitrosoglutathio

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Lambert, N., and R. B. Freedman. "The latency of rat liver microsomal protein disulphide-isomerase." Biochemical Journal 228, no. 3 (1985): 635–45. http://dx.doi.org/10.1042/bj2280635.

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Protein disulphide-isomerase (PDI) activity was not detectable in freshly prepared rat liver microsomes (microsomal fraction), but became detectable after treatments that damage membrane integrity, e.g. sonication, detergent treatment or freezing and thawing. Maximum activity was detectable after sonication. Identical latency was observed in microsomes prepared by gel filtration and in those prepared by high-speed centrifugation. PDI activity was latent in all particulate subcellular fractions, but not latent in the high-speed supernatant. When all fractions were sonicated to expose total PDI

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FERRARI, David M., and Hans-Dieter SÖLING. "The protein disulphide-isomerase family: unravelling a string of folds." Biochemical Journal 339, no. 1 (1999): 1–10. http://dx.doi.org/10.1042/bj3390001.

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The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95–110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys- tetrapeptide. In addition to their known roles as redox catalysts and isome

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Dias-Gunasekara, S., and A. M. Benham. "Defining the protein–protein interactions of the mammalian endoplasmic reticulum oxidoreductases (EROs)." Biochemical Society Transactions 33, no. 6 (2005): 1382–84. http://dx.doi.org/10.1042/bst0331382.

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The ER (endoplasmic reticulum) is the site of protein folding for all eukaryotic secreted and plasma membrane proteins. Disulphide bonds are formed in many of these proteins through a dithiol–disulphide exchange chain comprising two types of protein catalysts: PDI (protein disulphide-isomerase) and ERO (ER oxidoreductase) proteins. This review will examine what we know about ERO function, and will then consider ERO interactions and their implications for mammalian oxidative protein folding.

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Okuda, Aya, Motonori Matsusaki, Taro Masuda, et al. "A novel soybean protein disulphide isomerase family protein possesses dithiol oxidation activity: identification and characterization of GmPDIL6." Journal of Biochemistry 168, no. 4 (2020): 393–405. http://dx.doi.org/10.1093/jb/mvaa058.

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Abstract Secretory and membrane proteins synthesized in the endoplasmic reticulum (ER) are folded with intramolecular disulphide bonds, viz. oxidative folding, catalysed by the protein disulphide isomerase (PDI) family proteins. Here, we identified a novel soybean PDI family protein, GmPDIL6. GmPDIL6 has a single thioredoxin-domain with a putative N-terminal signal peptide and an active centre (CKHC). Recombinant GmPDIL6 forms various oligomers binding iron. Oligomers with or without iron binding and monomers exhibited a dithiol oxidase activity level comparable to those of other soybean PDI f

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RIGOBELLO, Maria Pia, Arianna DONELLA-DEANA, Luca CESARO, and Alberto BINDOLI. "Distribution of protein disulphide isomerase in rat liver mitochondria." Biochemical Journal 356, no. 2 (2001): 567–70. http://dx.doi.org/10.1042/bj3560567.

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Here we report the localization of protein disulphide isomerase (PDI) in the mitochondrial compartments, comparing it with that of thioredoxin reductase. The latter enzyme is present mostly in the matrix, whereas PDI is located at the level of the outer membrane. We characterize the different submitochondrial fractions with specific marker enzymes. PDI, whether isolated from whole mitochondria or from purified outer membranes, exhibits the same electrophoretic mobility, indicating identical molecular masses. Moreover, immunoblot analysis with monoclonal anti-PDI antibody shows immunoreactivity

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Medraño-Fernandez, Iria, Claudio Fagioli, Alexandre Mezghrani, Mieko Otsu, and Roberto Sitia. "Different redox sensitivity of endoplasmic reticulum associated degradation clients suggests a novel role for disulphide bonds in secretory proteins." Biochemistry and Cell Biology 92, no. 2 (2014): 113–18. http://dx.doi.org/10.1139/bcb-2013-0090.

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To maintain proteostasis in the endoplasmic reticulum (ER), terminally misfolded secretory proteins must be recognized, partially unfolded, and dislocated to the cytosol for proteasomal destruction, in a complex process called ER-associated degradation (ERAD). Dislocation implies reduction of inter-chain disulphide bonds. When in its reduced form, protein disulphide isomerase (PDI) can act not only as a reductase but also as an unfoldase, preparing substrates for dislocation. PDI oxidation by Ero1 favours substrate release and transport across the ER membrane. Here we addressed the redox depen

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Jessop, C. E., S. Chakravarthi, R. H. Watkins, and N. J. Bulleid. "Oxidative protein folding in the mammalian endoplasmic reticulum." Biochemical Society Transactions 32, no. 5 (2004): 655–58. http://dx.doi.org/10.1042/bst0320655.

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Native disulphide bonds are essential for the structure and function of many membrane and secretory proteins. Disulphide bonds are formed, reduced and isomerized in the endoplasmic reticulum of mammalian cells by a family of oxidoreductases, which includes protein disulphide isomerase (PDI), ERp57, ERp72, P5 and PDIR. This review will discuss how these enzymes are maintained in either an oxidized redox state that allows them to form disulphide bonds in substrate proteins or a reduced form that allows them to perform isomerization and reduction reactions, how these opposing pathways may co-exis

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Hawkins, H. C., E. C. Blackburn, and R. B. Freedman. "Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate." Biochemical Journal 275, no. 2 (1991): 349–53. http://dx.doi.org/10.1042/bj2750349.

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1. The activities of protein disulphide-isomerase (PDI) and thioredoxin in catalysing disulphide bond isomerization in a protein substrate were compared by using the standard assay, namely the re-activation of ‘scrambled’ RNAase. 2. The specific activity of PDI was 25-fold greater than that of thioredoxin. 3. The greater efficiency of PDI compared with thioredoxin is considered to be due more to the presence of multiple catalytic domains in PDI than to differences in their active-site sequences. 4. Data and procedures were defined for expressing enzyme activity in standard units, i.e. mumol of

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Dissertations / Theses on the topic "Protein disulphide isomerase (PDI)"

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Byrne, Lee J. "Investigations into the protein disulphide isomerase-related proteins of Saccharomyces cerevisiae." Thesis, University of Kent, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.314283.

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Springate, Jennifer. "The role of PDI and ERp46 in oxidative protein folding in the endoplasmic reticulum." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/the-role-of-pdi-and-erp46-in-oxidative-protein-folding-in-the-endoplasmic-reticulum(0318ed57-52f0-47ef-afd5-60238e3cdca4).html.

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Currently the mammalian endoplasmic reticulum (ER) is known to contain at least 20 different protein disulphide isomerase (PDI) family members. The oxidoreductases in the PDI family are thought to catalyse the formation and rearrangement of disulphide bonds in newly synthesised proteins. The focus of this work was to characterise two of the PDI family members: PDI and ERp46. In vitro translation reactions of major histocompatibility complex (MHC), β1-integrin (β1-I), haemagglutinin (HA), procollagen α1(III) and preprolaction (pPL) were carried out in untreated or PDI-depleted cells. The deplet

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Lappi, A. K. (Anna-Kaisa). "Mechanisms of protein disulphide isomerase catalyzed disulphide bond formation." Doctoral thesis, Oulun yliopisto, 2010. http://urn.fi/urn:isbn:9789514262753.

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Abstract Protein folding of outer membrane and secreted proteins, including receptors, cytokines and antibodies is often linked to disulphide bond formation. Native disulphide bond formation is complex and is usually the rate limiting step in the folding of such proteins. The enzymes which catalyse the slow steps in disulphide bond formation belong to the protein disulphide isomerase (PDI) family. PDI catalyses formation, reduction and isomerization of newly synthesized disulphide bonds. The mechanisms of action of the PDIs are currently poorly understood and this not only inhibits our underst

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Sidhu, Ateesh. "Structural studies on protein disulphide isomerase." Thesis, University of Warwick, 2008. http://wrap.warwick.ac.uk/2370/.

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Protein disulphide isomerase (POI; EC 5.3.4.1) is a multifunctional enzyme which resides in the lumen of the endoplasmic reticulum (ER). It is approximated that over one-third of all human proteins fold in the ER. POI is one of the main folding catalysts, specifically facilitating native disulphide bond formation. POI has four domains, three of which have been solved and all possessing a thioredoxin-type fold consisting of the J3-a-J3-a-J3-a-J3-J3-a structure. Due to the intransigent nature of the b' domain of POI, it remains structurally unelucidated. The b' domain is vitally important as it

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Natalia, Dessy. "Studies on yeast protein disulphide isomerase." Thesis, University of Kent, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.240649.

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Blackburn, E. C. "Protein disulphide isomerase activity in Escherichia coli." Thesis, University of Kent, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.304490.

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Murant, Susan J. "A molecular biological study of protein disulphide isomerase." Thesis, University of Kent, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.238542.

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Blood, John Philip. "Single-molecule FRET studies of protein disulphide-isomerase." Thesis, University of Warwick, 2013. http://wrap.warwick.ac.uk/61692/.

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Protein disulphide-isomerase (PDI) is the key element of the machinery which ensures correct and efficient folding of proteins that pass through the export compartments of the cell. PDI brings about both conformational and chemical change in the proteins on which it acts, but it has been impossible to probe its mechanism due to a lack of information regarding its inter-domain motion. PDI comprises a series of thioredoxin-like domains, represented as a-b-b’-x-a’-c, where a and a’ are highly similar domains containing dithiol active sites, the b and b’ –domains form a stable base, x is a flexibl

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Gonzalez, Veronica. "The role of protein disulfide isomerase (PDI) in oxidative folding." To access this resource online via ProQuest Dissertations and Theses @ UTEP, 2008. http://0-proquest.umi.com.lib.utep.edu/login?COPT=REJTPTU0YmImSU5UPTAmVkVSPTI=&clientId=2515.

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Paver, J. "The function and sub-cellular location of protein disulphide isomerase." Thesis, University of Kent, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.376120.

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Books on the topic "Protein disulphide isomerase (PDI)"

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Humphreys, David Paul. Expression of human protein disulphide isomerase (PDI) in Escherichia coli, and protein folding in vivo: Y David Paul Humphreys. University of Birmingham, 1995.

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Koivu, Juha. Protein disulphide isomerase and disulphide bond formation in collagen biosynthesis. University of Oulu, 1987.

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Book chapters on the topic "Protein disulphide isomerase (PDI)"

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"Protein Disulphide Isomerase." In Encyclopedia of Cancer. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16483-5_4796.

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"PDI (protein disulfide isomerase)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics. Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_12461.

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"PROTEIN DISULPHIDE-ISOMERASE: A CATALYST OF THIOL: DISULPHIDE INTERCHANGE AND ASSOCIATED PROTEIN FOLDING." In Molecular Chaperones and Folding Catalysts. CRC Press, 1999. http://dx.doi.org/10.1201/9781482283440-31.

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Conference papers on the topic "Protein disulphide isomerase (PDI)"

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Duncan, Ravyn M., Leticia Reyes, Katelyn Moats, Reeder M. Robinson, Holly A. Stessman, and Nathan G. Dolloff. "Abstract 3840: ATF3 drives synergy between protein disulfide isomerase (PDI) inhibitors and epigenetic cancer therapy." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3840.

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Duncan, Ravyn M., Leticia Reyes, Katelyn Moats, Reeder M. Robinson, Holly A. Stessman, and Nathan G. Dolloff. "Abstract 3840: ATF3 drives synergy between protein disulfide isomerase (PDI) inhibitors and epigenetic cancer therapy." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3840.

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Kenche, Harshavardan, Jeremy A. Brown, and Anna Blumental-Perry. "One Time Cigarette Smoking (CS) Results In Oxidation Of Protein Disulfide Isomerase (PDI) And Induction Of Unfolded Protein Response (UPR)." In American Thoracic Society 2012 International Conference, May 18-23, 2012 • San Francisco, California. American Thoracic Society, 2012. http://dx.doi.org/10.1164/ajrccm-conference.2012.185.1_meetingabstracts.a1262.

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Prevost, Gregoire P., Marine Garrido, Maria Serova, et al. "Abstract 3760: XCE853 is a promising protein disulfide isomerase (PDI) inhibitor exhibiting a strong inhibitory activity in preclinical tumor models." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3760.

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Xu, Shili, Alexey N. Butkevich, Roppei Yamada, et al. "Abstract 5513: Discovery of an orally active small-molecule irreversible inhibitor of protein disulfide isomerase (PDI) for ovarian cancer treatment." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5513.

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Reports on the topic "Protein disulphide isomerase (PDI)"

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Christopher, David A., and Avihai Danon. Plant Adaptation to Light Stress: Genetic Regulatory Mechanisms. United States Department of Agriculture, 2004. http://dx.doi.org/10.32747/2004.7586534.bard.

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Original Objectives: 1. Purify and biochemically characterize RB60 orthologs in higher plant chloroplasts; 2. Clone the gene(s) encoding plant RB60 orthologs and determine their structure and expression; 3. Manipulate the expression of RB60; 4. Assay the effects of altered RB60 expression on thylakoid biogenesis and photosynthetic function in plants exposed to different light conditions. In addition, we also examined the gene structure and expression of RB60 orthologs in the non-vascular plant, Physcomitrella patens and cloned the poly(A)-binding protein orthologue (43 kDa RB47-like protein).

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