Academic literature on the topic 'Islet Amyloid Polypeptide – genetics'

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Journal articles on the topic "Islet Amyloid Polypeptide – genetics"

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Hull, Rebecca L., Melissah R. Watts, Keiichi Kodama, et al. "Genetic background determines the extent of islet amyloid formation in human islet amyloid polypeptide transgenic mice." American Journal of Physiology-Endocrinology and Metabolism 289, no. 4 (2005): E703—E709. http://dx.doi.org/10.1152/ajpendo.00471.2004.

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Genetic background is important in determining susceptibility to metabolic abnormalities such as insulin resistance and β-cell dysfunction. Islet amyloid is associated with reduced β-cell mass and function and develops in the majority of our C57BL/6J × DBA/2J (F1) male human islet amyloid polypeptide (hIAPP) transgenic mice after 1 yr of increased fat feeding. To determine the relative contribution of each parental strain, C57BL/6J (BL6) and DBA/2J (DBA2), to islet amyloid formation, we studied male hIAPP mice on each background strain (BL6, n = 13; and DBA2 n = 11) and C57BL/6J × DBA/2J F1mic
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Wookey, Peter J., Loredanna Xuereb, Christos Tikellis, and Mark E. Cooper. "Amylin in the Periphery." Scientific World JOURNAL 3 (2003): 163–75. http://dx.doi.org/10.1100/tsw.2003.17.

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Amylin (islet amyloid polypeptide) is a peptide synthesized principally in the b-cells of the pancreatic islets together with insulin and has actions as a hormone, growth factor, and modifier of behavior. As a hormone, amylin acts to modify gastric motility, renal resorption, and has metabolic actions. It is postulated that the principal function of amylin as a hormone is the activation of physiological processes associated with feeding. As a growth factor, amylin acts on bone cells, renal proximal tubular cells, and islet b-cells. Amylin has important targets in the brain that mediate its act
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Christmanson, Lars, Fredrik Rorsman, Göran Stenman, Per Westermark, and Christer Betsholtz. "The human islet amyloid polypeptide (IAPP) gene." FEBS Letters 267, no. 1 (1990): 160–66. http://dx.doi.org/10.1016/0014-5793(90)80314-9.

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Zhang, Xin, Biao Cheng, Hao Gong, et al. "Porcine islet amyloid polypeptide fragments are refractory to amyloid formation." FEBS Letters 585, no. 1 (2010): 71–77. http://dx.doi.org/10.1016/j.febslet.2010.11.050.

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Westermark, Gunilla T., Samuel Gebre-Medhin, Donald F. Steiner, and Per Westermark. "Islet Amyloid Development in a Mouse Strain Lacking Endogenous Islet Amyloid Polypeptide (IAPP) but Expressing Human IAPP." Molecular Medicine 6, no. 12 (2000): 998–1007. http://dx.doi.org/10.1007/bf03402051.

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Fortin, Jessica S., Nurhanis B. M. Isa, Anisa M. Rashid, Thomas L. Thompson, and Malikah O’Dell. "Small molecules breaking down islet amyloid polypeptide self‐assembly." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.08776.

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Wakabayashi, Masaki, and Katsumi Matsuzaki. "Ganglioside-induced amyloid formation by human islet amyloid polypeptide in lipid rafts." FEBS Letters 583, no. 17 (2009): 2854–58. http://dx.doi.org/10.1016/j.febslet.2009.07.044.

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Kanatsuka, A., H. Makino, H. Ohsawa, et al. "Secretion of islet amyloid polypeptide in response to glucose." FEBS Letters 259, no. 1 (1989): 199–201. http://dx.doi.org/10.1016/0014-5793(89)81527-3.

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Nishi, M., G. I. Bell, and D. F. Steiner. "Sequence of a cDNA encoding Syrian hamster islet amyloid polypeptide precursor." Nucleic Acids Research 18, no. 22 (1990): 6726. http://dx.doi.org/10.1093/nar/18.22.6726.

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Cheung, David L. "Effect of surface chemistry on islet amyloid polypeptide conformation." Biointerphases 15, no. 5 (2020): 051001. http://dx.doi.org/10.1116/6.0000417.

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Dissertations / Theses on the topic "Islet Amyloid Polypeptide – genetics"

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Paulsson, Johan F. "Proislet Amyloid Polypeptide (proIAPP) : Impaired Processing is an Important Factor in Early Amyloidogenesis in Type 2 Diabetes." Doctoral thesis, Linköping : Linköping University, 2006. http://www.bibl.liu.se/liupubl/disp/disp2006/med967s.pdf.

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Wiltzius, Jed John William. "Structural studies of islet amyloid polypeptide." Diss., Restricted to subscribing institutions, 2008. http://proquest.umi.com/pqdweb?did=1691848941&sid=6&Fmt=2&clientId=1564&RQT=309&VName=PQD.

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Jaikaran, Emma Tracy Araminta Sunita. "Factors influencing human islet amyloid polypeptide fibril formation." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.342537.

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Hull, Rebecca L. "Pro-islet amyloid polypeptide and type 2 diabetes." Thesis, University of Nottingham, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.285837.

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Westwell-Roper, Clara Yolande. "Islet amyloid polypeptide aggregation is a local trigger for pancreatic islet inflammation." Thesis, University of British Columbia, 2014. http://hdl.handle.net/2429/46729.

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Patients with type 2 diabetes experience an inevitable deterioration of glycemic control leading to long-term complications and dependence on exogenous insulin. Amyloid deposition, macrophage infiltration, and upregulation of pro-inflammatory cytokines are common pathological features of both type 2 diabetic and transplanted islets. Islet amyloid is comprised primarily of aggregates of islet amyloid polypeptide (IAPP), a peptide that is co-secreted with insulin by beta cells. IAPP fibrils share a common cross-β-sheet structure with other amyloids of mammalian and microbial origin that activate
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MacArthur, Diane L. A. "Amyloid fibril formation in islets of transgenic mice expressing human islet amyloid polypeptide." Thesis, University of Oxford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325942.

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Higham, Claire Emily. "Biophysical properties, fibril formation and processing of islet amyloid polypeptide." Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.312105.

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Bhogal, Rashpal Kaur. "Factors influencing islet amyloid polypeptide degradation, cytotoxicity and fibril formation." Thesis, University of Oxford, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.401100.

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Oskarsson, Marie. "Islet amyloid polypeptide (IAPP) in Type 2 diabetes and Alzheimer disease." Doctoral thesis, Uppsala universitet, Institutionen för medicinsk cellbiologi, 2015. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-265501.

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The misfolding and aggregation of the beta cell hormone islet amyloid polypeptide (IAPP) into amyloid fibrils is the main pathological finding in islets of Langerhans in type 2 diabetes. Pathological assemblies of IAPP are cytotoxic and believed to contribute to the loss of insulin-producing beta cells. Changes in the microenvironment that could trigger the aggregation of IAPP are largely unknown. So is the possibility that islet amyloid can spread within or between tissues. The present thesis have explored the roles of glycosaminoglycan heparan sulfate (HS) and the novel anti-amyloid chaperon
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Courtade, Jaques. "Impaired pro-islet amyloid polypeptide processing promotes beta-cell dysfunction in diabetes and islet transplants." Thesis, University of British Columbia, 2016. http://hdl.handle.net/2429/59064.

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Soaring rates of diabetes highlight the importance of controlling this global epidemic, with an estimated 415 million people thought to be living with diabetes in 2015. The defining characteristic of diabetes is elevated fasting blood glucose levels, or hyperglycemia, which if not controlled promotes long-term complications such as neuropathy, kidney failure and damage to blood vessels. Glucose homeostasis is primarily controlled by pancreatic islets, cell clusters that mediate the endocrine functions of the pancreas. To manage circulating glucose concentrations, islet beta cells synthesize pr
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Books on the topic "Islet Amyloid Polypeptide – genetics"

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Skeby, Katrine Kirkeby. Computational Modelling of the Human Islet Amyloid Polypeptide. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-20040-8.

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Skeby, Katrine Kirkeby. Computational Modelling of the Human Islet Amyloid Polypeptide. Springer, 2018.

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Computational Modelling of the Human Islet Amyloid Polypeptide. Springer, 2016.

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Book chapters on the topic "Islet Amyloid Polypeptide – genetics"

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Abedini, Andisheh, and Daniel P. Raleigh. "Islet Amyloid Polypeptide." In Protein Misfolding Diseases. John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470572702.ch23.

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Chiaravalli, Anna Maria. "Islet Amyloid Polypeptide." In Encyclopedia of Pathology. Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-319-28845-1_5088-1.

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Mulder, Hindrik, Bo Ahrén, Eva Ekblad, et al. "Islet Amyloid Polypeptide and Adrenomedullin." In Gastrointestinal Endocrinology. Humana Press, 1999. http://dx.doi.org/10.1007/978-1-59259-695-9_21.

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Skeby, Katrine Kirkeby. "Amyloid and Amyloid Fibrils." In Computational Modelling of the Human Islet Amyloid Polypeptide. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-20040-8_1.

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Westermark, Gunilla T. "Physiological and Pathophysiological Role of Islet Amyloidislet amyloid Polypeptide islet amyloid polypeptide (IAPPIAPP , Amylinamylin )." In BetaSys. Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6956-9_15.

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Butler, Peter C., Norman L. Eberhardt, and Timothy D. O’Brien. "Islet Amyloid Polypeptide (IAPP) and Insulin Secretion." In Molecular Biology of Diabetes. Humana Press, 1994. http://dx.doi.org/10.1007/978-1-4612-0241-7_16.

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Westermark, Per, Kenneth H. Johnson, Ulla Engström, et al. "Islet Amyloid Polypeptide: Synthetic Peptides for Study of the Pathogenesis of Islet Amyloid." In Amyloid and Amyloidosis 1990. Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-011-3284-8_112.

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Skeby, Katrine Kirkeby. "Imaging Agent Binding to Amyloid Protofibrils." In Computational Modelling of the Human Islet Amyloid Polypeptide. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-20040-8_3.

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Skeby, Katrine Kirkeby. "Coarse Grained Study of Amyloid Protofibril Aggregation." In Computational Modelling of the Human Islet Amyloid Polypeptide. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-20040-8_6.

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Seeliger, Janine, and Roland Winter. "Islet Amyloid Polypeptide: Aggregation and Fibrillogenesisin vitroand Its Inhibition." In Protein Aggregation and Fibrillogenesis in Cerebral and Systemic Amyloid Disease. Springer Netherlands, 2012. http://dx.doi.org/10.1007/978-94-007-5416-4_8.

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Conference papers on the topic "Islet Amyloid Polypeptide – genetics"

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Abioye, Raliat, and Chibuike Udenigwe. "Inhibition of islet amyloid polypeptide fibril formation by natural polyphenols." In Virtual 2021 AOCS Annual Meeting & Expo. American Oil Chemists' Society (AOCS), 2021. http://dx.doi.org/10.21748/am21.601.

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Ladjimi, Moncef, Ali Chaari, and David Eliezer. "Inhibition of Human Islet Amyloid Polypeptide Aggregation in Type 2 Diabetes by Hsp70 Molecular Chaperones." In Qatar Foundation Annual Research Conference Proceedings. Hamad bin Khalifa University Press (HBKU Press), 2016. http://dx.doi.org/10.5339/qfarc.2016.hbpp2702.

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