アミリン (ホルモン) (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "アミリン (ホルモン)" in Japanese language version.

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amylin.com

“SYMLIN (pramlintide acetate)”. Amylin Pharmaceuticals, Inc. (2006年). 2008年6月13日時点のオリジナルよりアーカイブ。2008年5月28日閲覧。

diabetesjournals.org

diabetes.diabetesjournals.org

Defronzo RA (2009). “Banting Lecture. From the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus”. Diabetes 58 (4): 773–795. doi:10.2337/db09-9028. PMC 2661582. PMID 19336687.

doi.org

“Processing of synthetic pro-islet amyloid polypeptide (proIAPP) 'amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro”. Eur. J. Biochem. 267 (16): 4998–5004. (August 2000). doi:10.1046/j.1432-1327.2000.01548.x. PMID 10931181.
“Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus”. Proc. Natl. Acad. Sci. U.S.A. 86 (24): 9662–6. (December 1989). Bibcode: 1989PNAS...86.9662R. doi:10.1073/pnas.86.24.9662. PMC 298561. PMID 2690069.
“An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing”. J. Biol. Chem. 263 (33): 17243–6. (November 1988). doi:10.1016/S0021-9258(19)77825-9. PMID 3053705.
“Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells”. Endocrinology 146 (4): 1808–17. (April 2005). doi:10.1210/en.2004-1175. PMID 15618358.
Defronzo RA (2009). “Banting Lecture. From the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus”. Diabetes 58 (4): 773–795. doi:10.2337/db09-9028. PMC 2661582. PMID 19336687.
“Islet amyloid and type 2 diabetes mellitus”. N. Engl. J. Med. 343 (6): 411–9. (August 2000). doi:10.1056/NEJM200008103430607. PMID 10933741.
“TNF-α acutely upregulates amylin expression in murine pancreatic beta cells”. Diabetologia 54 (3): 617–26. (March 2011). doi:10.1007/s00125-010-1972-9. PMID 21116608.
“Fatty acids induce amylin expression and secretion by pancreatic beta-cells”. Am. J. Physiol. Endocrinol. Metab. 298 (1): E99–E107. (January 2010). doi:10.1152/ajpendo.00242.2009. PMID 19843871.
“Molecular physiology of amylin”. J. Cell. Biochem. 55 Suppl: 19–28. (1994). doi:10.1002/jcb.240550004. PMID 7929615.
“Amylin replacement with pramlintide as an adjunct to insulin therapy improves long-term glycaemic and weight control in Type 1 diabetes mellitus: a 1-year, randomized controlled trial”. Diabetic Medicine 21 (11): 1204–12. (2004). doi:10.1111/j.1464-5491.2004.01319.x. PMID 15498087.
“Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide”. J. Am. Chem. Soc. 130 (20): 6424–9. (May 2008). doi:10.1021/ja710484d. PMC 4163023. PMID 18444645.
“A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity”. Biochemistry 47 (48): 12680–8. (December 2008). doi:10.1021/bi801427c. PMC 2645932. PMID 18989933.
“Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy”. Biochemistry 47 (48): 12689–97. (December 2008). doi:10.1021/bi8014357. PMC 2953382. PMID 18989932.
“Membrane Fragmentation by an Amyloidogenic Fragment of Human Islet Amyloid Polypeptide Detected by Solid-State NMR Spectroscopy of Membrane Nanotubes”. Biochim. Biophys. Acta 1768 (9): 2026–9. (September 2007). doi:10.1016/j.bbamem.2007.07.001. PMC 2042489. PMID 17662957.
Palmieri, Leonardo C; Melo-Ferreira, Bruno; Braga, Carolina A; Fontes, Giselle N; Mattos, Luana J; Lima, Luis Mauricio (2013). “Stepwise oligomerization of murine amylin and assembly of amyloid fibrils”. Biophys Chem 181: 135–144. doi:10.1016/j.bpc.2013.07.013. PMID 23974296.
Erthal, Luiza C; Marques, Adriana F; Almeida, Fábio C; Melo, Gustavo L; Carvalho, Camila M; Palmieri, Leonardo C; Cabral, Kátia M; Fontes, Giselle N; Lima, Luis Mauricio (2016). “Regulation of the assembly and amyloid aggregation of murine amylin by zinc”. Biophys. Chem. 218: 58–70. doi:10.1016/j.bpc.2016.09.008. PMID 27693831.
“Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients”. Proc Natl Acad Sci USA 84 (23): 8628–32. (1987). Bibcode: 1987PNAS...84.8628C. doi:10.1073/pnas.84.23.8628. PMC 299599. PMID 3317417.
“Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells”. Proc Natl Acad Sci USA 84 (11): 3881–3885. (1987). Bibcode: 1987PNAS...84.3881W. doi:10.1073/pnas.84.11.3881. PMC 304980. PMID 3035556.
“Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation”. Diabetes 54 (7): 2117–25. (July 2005). doi:10.2337/diabetes.54.7.2117. PMID 15983213.
“Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death”. Diabetes 55 (8): 2192–201. (August 2006). doi:10.2337/db05-1566. PMID 16873681.
“Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets”. Diabetologia 49 (6): 1237–46. (June 2006). doi:10.1007/s00125-006-0206-7. PMID 16570161.
“Abeta and human amylin share a common toxicity pathway via mitochondrial dysfunction”. Proteomics 10 (8): 1621–33. (April 2010). doi:10.1002/pmic.200900651. PMID 20186753.
“Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus”. Nature 368 (6473): 756–60. (April 1994). Bibcode: 1994Natur.368..756L. doi:10.1038/368756a0. PMID 8152488.
“Leptin responsiveness restored by amylin agonism in diet-induced obesity: evidence from nonclinical and clinical studies”. Proc. Natl. Acad. Sci. U.S.A. 105 (20): 7257–62. (May 2008). Bibcode: 2008PNAS..105.7257R. doi:10.1073/pnas.0706473105. PMC 2438237. PMID 18458326.
“Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism”. Nature 443 (7113): 870–4. (October 2006). Bibcode: 2006Natur.443..870S. doi:10.1038/nature05143. PMC 3366509. PMID 17051221.
“Amylin receptors: molecular composition and pharmacology”. Biochem. Soc. Trans. 32 (Pt 5): 865–7. (November 2004). doi:10.1042/BST0320865. PMID 15494035.

ensembl.org

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000121351 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000041681 - Ensembl, May 2017

harvard.edu

ui.adsabs.harvard.edu

jbc.org

“An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing”. J. Biol. Chem. 263 (33): 17243–6. (November 1988). doi:10.1016/S0021-9258(19)77825-9. PMID 3053705.

nih.gov

pubmed.ncbi.nlm.nih.gov

“Processing of synthetic pro-islet amyloid polypeptide (proIAPP) 'amylin' by recombinant prohormone convertase enzymes, PC2 and PC3, in vitro”. Eur. J. Biochem. 267 (16): 4998–5004. (August 2000). doi:10.1046/j.1432-1327.2000.01548.x. PMID 10931181.
“Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus”. Proc. Natl. Acad. Sci. U.S.A. 86 (24): 9662–6. (December 1989). Bibcode: 1989PNAS...86.9662R. doi:10.1073/pnas.86.24.9662. PMC 298561. PMID 2690069.
“An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing”. J. Biol. Chem. 263 (33): 17243–6. (November 1988). doi:10.1016/S0021-9258(19)77825-9. PMID 3053705.
“Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells”. Endocrinology 146 (4): 1808–17. (April 2005). doi:10.1210/en.2004-1175. PMID 15618358.
Defronzo RA (2009). “Banting Lecture. From the triumvirate to the ominous octet: a new paradigm for the treatment of type 2 diabetes mellitus”. Diabetes 58 (4): 773–795. doi:10.2337/db09-9028. PMC 2661582. PMID 19336687.
“Islet amyloid and type 2 diabetes mellitus”. N. Engl. J. Med. 343 (6): 411–9. (August 2000). doi:10.1056/NEJM200008103430607. PMID 10933741.
“TNF-α acutely upregulates amylin expression in murine pancreatic beta cells”. Diabetologia 54 (3): 617–26. (March 2011). doi:10.1007/s00125-010-1972-9. PMID 21116608.
“Fatty acids induce amylin expression and secretion by pancreatic beta-cells”. Am. J. Physiol. Endocrinol. Metab. 298 (1): E99–E107. (January 2010). doi:10.1152/ajpendo.00242.2009. PMID 19843871.
“Molecular physiology of amylin”. J. Cell. Biochem. 55 Suppl: 19–28. (1994). doi:10.1002/jcb.240550004. PMID 7929615.
“Amylin replacement with pramlintide as an adjunct to insulin therapy improves long-term glycaemic and weight control in Type 1 diabetes mellitus: a 1-year, randomized controlled trial”. Diabetic Medicine 21 (11): 1204–12. (2004). doi:10.1111/j.1464-5491.2004.01319.x. PMID 15498087.
“Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide”. J. Am. Chem. Soc. 130 (20): 6424–9. (May 2008). doi:10.1021/ja710484d. PMC 4163023. PMID 18444645.
“A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity”. Biochemistry 47 (48): 12680–8. (December 2008). doi:10.1021/bi801427c. PMC 2645932. PMID 18989933.
“Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy”. Biochemistry 47 (48): 12689–97. (December 2008). doi:10.1021/bi8014357. PMC 2953382. PMID 18989932.
“Membrane Fragmentation by an Amyloidogenic Fragment of Human Islet Amyloid Polypeptide Detected by Solid-State NMR Spectroscopy of Membrane Nanotubes”. Biochim. Biophys. Acta 1768 (9): 2026–9. (September 2007). doi:10.1016/j.bbamem.2007.07.001. PMC 2042489. PMID 17662957.
Palmieri, Leonardo C; Melo-Ferreira, Bruno; Braga, Carolina A; Fontes, Giselle N; Mattos, Luana J; Lima, Luis Mauricio (2013). “Stepwise oligomerization of murine amylin and assembly of amyloid fibrils”. Biophys Chem 181: 135–144. doi:10.1016/j.bpc.2013.07.013. PMID 23974296.
Erthal, Luiza C; Marques, Adriana F; Almeida, Fábio C; Melo, Gustavo L; Carvalho, Camila M; Palmieri, Leonardo C; Cabral, Kátia M; Fontes, Giselle N; Lima, Luis Mauricio (2016). “Regulation of the assembly and amyloid aggregation of murine amylin by zinc”. Biophys. Chem. 218: 58–70. doi:10.1016/j.bpc.2016.09.008. PMID 27693831.
“Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients”. Proc Natl Acad Sci USA 84 (23): 8628–32. (1987). Bibcode: 1987PNAS...84.8628C. doi:10.1073/pnas.84.23.8628. PMC 299599. PMID 3317417.
“Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells”. Proc Natl Acad Sci USA 84 (11): 3881–3885. (1987). Bibcode: 1987PNAS...84.3881W. doi:10.1073/pnas.84.11.3881. PMC 304980. PMID 3035556.
“Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation”. Diabetes 54 (7): 2117–25. (July 2005). doi:10.2337/diabetes.54.7.2117. PMID 15983213.
“Impaired NH2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death”. Diabetes 55 (8): 2192–201. (August 2006). doi:10.2337/db05-1566. PMID 16873681.
“Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets”. Diabetologia 49 (6): 1237–46. (June 2006). doi:10.1007/s00125-006-0206-7. PMID 16570161.
Hayden MR (September 2002). “Islet amyloid, metabolic syndrome, and the natural progressive history of type 2 diabetes mellitus”. JOP 3 (5): 126–38. PMID 12221327.
“Abeta and human amylin share a common toxicity pathway via mitochondrial dysfunction”. Proteomics 10 (8): 1621–33. (April 2010). doi:10.1002/pmic.200900651. PMID 20186753.
“Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus”. Nature 368 (6473): 756–60. (April 1994). Bibcode: 1994Natur.368..756L. doi:10.1038/368756a0. PMID 8152488.
“Leptin responsiveness restored by amylin agonism in diet-induced obesity: evidence from nonclinical and clinical studies”. Proc. Natl. Acad. Sci. U.S.A. 105 (20): 7257–62. (May 2008). Bibcode: 2008PNAS..105.7257R. doi:10.1073/pnas.0706473105. PMC 2438237. PMID 18458326.
“Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism”. Nature 443 (7113): 870–4. (October 2006). Bibcode: 2006Natur.443..870S. doi:10.1038/nature05143. PMC 3366509. PMID 17051221.
“Amylin receptors: molecular composition and pharmacology”. Biochem. Soc. Trans. 32 (Pt 5): 865–7. (November 2004). doi:10.1042/BST0320865. PMID 15494035.

ncbi.nlm.nih.gov

pharmascitech.in

Suva, Manoj (July 2015). “Role of Amylin in Obesity”. Journal of PharmaSciTech 5: 5–10.

sandiegouniontribune.com

Facebook (2011年3月16日). “Amylin halts trial of weight-loss therapy” (英語). San Diego Union-Tribune. 2021年10月23日閲覧。

web.archive.org

“SYMLIN (pramlintide acetate)”. Amylin Pharmaceuticals, Inc. (2006年). 2008年6月13日時点のオリジナルよりアーカイブ。2008年5月28日閲覧。

wikipedia.org

en.wikipedia.org

GRCh38: Ensembl release 89: ENSG00000121351 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000041681 - Ensembl, May 2017

yakuji.co.jp

“【武田薬品／アミリン】抗肥満薬「プラムリンタイド／メトレレプチン」の開発を中止｜薬事日報ウェブサイト”. 2021年10月23日閲覧。