Relevant bibliographies by topics / Serpinopathie

Academic literature on the topic 'Serpinopathie'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Serpinopathie"

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Faull, Sarah V., Emma L. K. Elliston, Bibek Gooptu, Alistair M. Jagger, Ibrahim Aldobiyan, Adam Redzej, Magd Badaoui, et al. "The structural basis for Z α1-antitrypsin polymerization in the liver." Science Advances 6, no. 43 (October 2020): eabc1370. http://dx.doi.org/10.1126/sciadv.abc1370.

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The serpinopathies are among a diverse set of conformational diseases that involve the aberrant self-association of proteins into ordered aggregates. α1-Antitrypsin deficiency is the archetypal serpinopathy and results from the formation and deposition of mutant forms of α1-antitrypsin as “polymer” chains in liver tissue. No detailed structural analysis has been performed of this material. Moreover, there is little information on the relevance of well-studied artificially induced polymers to these disease-associated molecules. We have isolated polymers from the liver tissue of Z α1-antitrypsin homozygotes (E342K) who have undergone transplantation, labeled them using a Fab fragment, and performed single-particle analysis of negative-stain electron micrographs. The data show structural equivalence between heat-induced and ex vivo polymers and that the intersubunit linkage is best explained by a carboxyl-terminal domain swap between molecules of α1-antitrypsin.
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Belorgey, Didier, Peter Hägglöf, Susanna Karlsson-Li, and David A. Lomas. "Protein Misfolding and the Serpinopathies." Prion 1, no. 1 (January 2007): 15–20. http://dx.doi.org/10.4161/pri.1.1.3974.

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Lomas, David A., and Robin W. Carrell. "Serpinopathies and the conformational dementias." Nature Reviews Genetics 3, no. 10 (October 2002): 759–68. http://dx.doi.org/10.1038/nrg907.

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DAVIES, M., and D. LOMAS. "The molecular aetiology of the serpinopathies." International Journal of Biochemistry & Cell Biology 40, no. 6-7 (June 2008): 1273–86. http://dx.doi.org/10.1016/j.biocel.2007.12.017.

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Lomas, D. A., D. Belorgey, M. Mallya, E. Miranda, K. J. Kinghorn, L. K. Sharp, R. L. Phillips, R. Page, A. S. Robertson, and D. C. Crowther. "Molecular mousetraps and the serpinopathies1." Biochemical Society Transactions 33, no. 2 (April 1, 2005): 321–30. http://dx.doi.org/10.1042/bst0330321.

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Members of the serine proteinase inhibitor or serpin superfamily inhibit their target proteinases by a remarkable conformational transition that involves the enzyme being translocated more than 70 Å (1 Å=10−10 m) from the upper to the lower pole of the inhibitor. This elegant mechanism is subverted by point mutations to form ordered polymers that are retained within the endoplasmic reticulum of secretory cells. The accumulation of polymers underlies the retention of mutants of α1-antitrypsin and neuroserpin within hepatocytes and neurons to cause cirrhosis and dementia respectively. The formation of polymers results in the failure to secrete mutants of other members of the serpin superfamily: antithrombin, C1 inhibitor and α1-antichymotrypsin, to cause a plasma deficiency that results in the clinical syndromes of thrombosis, angio-oedema and emphysema respectively. Understanding the common mechanism underlying the retention and deficiency of mutants of the serpins has allowed us to group these conditions as the serpinopathies. We review in this paper the molecular and structural basis of the serpinopathies and show how this has allowed the development of specific agents to block the polymerization that underlies disease.
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Miyata, Toshio, Reiko Inagi, Satoshi Sugiyama, and Nobuteru Usuda. "Serpinopathy and endoplasmic reticulum stress." Medical Molecular Morphology 38, no. 2 (June 10, 2005): 73–78. http://dx.doi.org/10.1007/s00795-004-0281-0.

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Ekeowa, Ugo I., Bibek Gooptu, Didier Belorgey, Peter Hägglöf, Susanna Karlsson-Li, Elena Miranda, Juan Pérez, et al. "α1-Antitrypsin deficiency, chronic obstructive pulmonary disease and the serpinopathies." Clinical Science 116, no. 12 (May 14, 2009): 837–50. http://dx.doi.org/10.1042/cs20080484.

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α1-Antitrypsin is the prototypical member of the serine proteinase inhibitor or serpin superfamily of proteins. The family includes α1-antichymotrypsin, C1 inhibitor, antithrombin and neuroserpin, which are all linked by a common molecular structure and the same suicidal mechanism for inhibiting their target enzymes. Point mutations result in an aberrant conformational transition and the formation of polymers that are retained within the cell of synthesis. The intracellular accumulation of polymers of mutant α1-antitrypsin and neuroserpin results in a toxic gain-of-function phenotype associated with cirrhosis and dementia respectively. The lack of important inhibitors results in overactivity of proteolytic cascades and diseases such as COPD (chronic obstructive pulmonary disease) (α1-antitrypsin and α1-antichymotrypsin), thrombosis (antithrombin) and angio-oedema (C1 inhibitor). We have grouped these conditions that share the same underlying disease mechanism together as the serpinopathies. In the present review, the molecular and pathophysiological basis of α1-antitrypsin deficiency and other serpinopathies are considered, and we show how understanding this unusual mechanism of disease has resulted in the development of novel therapeutic strategies.
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Ekeowa, U. I., J. Freeke, E. Miranda, B. Gooptu, M. F. Bush, J. Perez, J. Teckman, C. V. Robinson, and D. A. Lomas. "Defining the mechanism of polymerization in the serpinopathies." Proceedings of the National Academy of Sciences 107, no. 40 (September 20, 2010): 17146–51. http://dx.doi.org/10.1073/pnas.1004785107.

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Lomas, David A. "Molecular mousetraps, α1-antitrypsin deficiency and the serpinopathies." Clinical Medicine 5, no. 3 (May 1, 2005): 249–57. http://dx.doi.org/10.7861/clinmedicine.5-3-249.

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Gooptu, Bibek, and David A. Lomas. "Polymers and inflammation: disease mechanisms of the serpinopathies." Journal of Experimental Medicine 205, no. 7 (June 30, 2008): 1529–34. http://dx.doi.org/10.1084/jem.20072080.

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Members of the serpin (serine proteinase inhibitor) superfamily play a central role in the control of inflammatory, coagulation, and fibrinolytic cascades. Point mutations that cause abnormal conformational transitions in these proteins can trigger disease. Recent work has defined three pathways by which these conformers cause tissue damage. Here, we describe how these three mechanisms can be integrated into a new model of the pathogenesis of emphysema caused by mutations in the serpin α1-antitrypsin.
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Dissertations / Theses on the topic "Serpinopathie"

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BROGGINI, LUCA. "MOLECULAR DETERMINANTS UNDERLYING PROTEIN MISFOLDING AND AGGREGATION." Doctoral thesis, Università degli Studi di Milano, 2021. http://hdl.handle.net/2434/831967.

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Proteins have evolved to adopt distinctive and well-defined functional states under physiological conditions, either as monomers or complexes. The achievement of a three-dimensional structure allows proteins to exert their physiological functions. Nevertheless, when proteins lose – or fail to acquire – their spatial organization, they can convert into aggregated species that can be harmful to the organism. Conformational diseases gather all those pathologies characterized by the misfolding and aggregation of proteins. Indeed, while the formation and deposition of proteinaceous aggregates can be toxic to cells, the lack of active folded protein disrupts normal physiological pathways. Although considerable progresses have been made in the recent years, to date conformational diseases are still incurable. Indeed, the incomplete understanding of the causes guiding protein misfolding and aggregation prevents the development of efficient treatments. At the same time, the complexity and the diversity of the processes leading to the formation of aggregated species make the task extremely challenging. This PhD project was developed to provide a more comprehensive overview of the molecular bases underlying the conversion of soluble and functional states into aggregated and potentially toxic species. To reach such aims, we applied an integrative approach on two model systems, neuroserpin (NS) and beta-2 microglobulin (2m). In particular, we combined a series of biophysical, biochemical and structural techniques to study these two proteins which have been largely used as model systems for serpin polymerization and amyloid formation, respectively. We found that protein misfolding and aggregation processes depend on several molecular properties, including primary sequence, denatured state compactness, thermal stability, ability to form oligomers under physiological conditions, and the presence of post-translation modifications. The data presented in this PhD thesis add valuable information to depict the complex framework of protein misfolding and aggregation.
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Books on the topic "Serpinopathie"

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Silverman, Gary A., and David A. Lomas. Molecular and Cellular Aspects of the Serpinopathies and Disorders in Serpin Activity. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/6215.

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(Editor), Gary A. Silverman, and David A. Lomas (Editor), eds. Molecular and Cellular Aspects of the Serpinopathies and Disorders in Serpin Activity. World Scientific Publishing Company, 2007.

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Book chapters on the topic "Serpinopathie"

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Lomas, David A., James A. Irving, and Bibek Gooptu. "Serpinopathies." In α1-Antitrypsin Deficiency, 6–26. Sheffield, United Kingdom: European Respiratory Society, 2019. http://dx.doi.org/10.1183/2312508x.10032318.

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Fra, Annamaria, Emanuela D’Acunto, Mattia Laffranchi, and Elena Miranda. "Cellular Models for the Serpinopathies." In Methods in Molecular Biology, 109–21. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8645-3_7.

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Ordóñez, Adriana, and Stefan J. Marciniak. "Endoplasmic Reticulum Stress and the Protein Overload Response in the Serpinopathies." In The Serpin Family, 229–51. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-22711-5_14.

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Irving, James A., Ugo I. Ekeowa, Didier Belorgey, Imran Haq, Bibek Gooptu, Elena Miranda, Juan Pérez, et al. "The Serpinopathies." In Methods in Enzymology, 421–66. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-12-385950-1.00018-3.

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Blanco, Ignacio. "Serpins and Serpinopathies." In Blanco's Overview of Alpha-1 Antitrypsin Deficiency, 13–22. Elsevier, 2017. http://dx.doi.org/10.1016/b978-0-12-809530-0.00002-7.

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Lomas, David A., Didier Belorgey, Elena Miranda, Meera Mallya, Peter Hägglöf, Lynda K. Sharp, Russell L. Phillips, Richard Page, Mark J. Davies, and Damian C. Crowther. "The Serpinopathies and Respiratory Disease." In Molecular and Cellular Aspects of the Serpinopathies and Disorders in Serpin Activity, 445–82. WORLD SCIENTIFIC, 2007. http://dx.doi.org/10.1142/9789812707543_0020.

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Long, Olivia S., Sager J. Gosai, Joon Hyeok Kwak, Dale E. King, David H. Perlmutter, Gary A. Silverman, and Stephen C. Pak. "Using Caenorhabditis elegans to Study Serpinopathies." In Biology of Serpins, 259–81. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-12-386471-0.00013-4.

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Lomas, David A., Didier Belorgey, Meera Mallya, Maki Onda, Kerri J. Kinghorn, Lynda K. Sharp, Russell L. Phillips, Richard Page, Elena Miranda, and Damian C. Crowther. "Serpinopathies and the Central Nervous System." In Amyloid and Amyloidosis, 388–90. CRC Press, 2004. http://dx.doi.org/10.1201/9781420037494-138.

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Kinghorn, Kerri, Damian Crowther, Meera Mallya, Didier Belorgey, Lynda Sharp, Elena Miranda, Russell Phillips, Maki Onda, Richard Page, and David Lomas. "Serpinopathies and the Central Nervous System." In Amyloid and Amyloidosis, 388–90. CRC Press, 2004. http://dx.doi.org/10.1201/9781420037494.ch133.

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Lomas, David A. "α‎1-Antitrypsin deficiency and the serpinopathies." In Oxford Textbook of Medicine, 1780–84. Oxford University Press, 2010. http://dx.doi.org/10.1093/med/9780199204854.003.1213_update_001.

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α‎1-Antitrypsin is an acute phase glycoprotein synthesized by the liver that functions as an inhibitor of a range of proteolytic enzymes, most importantly neutrophil elastase. Severe plasma deficiency of α‎1-antitrypsin results from homozygocity for the Z allele, which causes the protein to undergo a conformational transition and form ordered polymers that are retained within hepatocytes as PAS-positive inclusions....
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