Amilina (Galician Wikipedia)

Analysis of information sources in references of the Wikipedia article "Amilina" in Galician language version.

refsWebsite

Global rank Galician rank

16nih.gov

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14doi.org

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1archive.org

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1amylin.com

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amylin.com

"SYMLIN (pramlintide acetate)". Amylin Pharmaceuticals, Inc. 2006. Consultado o 2008-05-28.

archive.org

Ratner RE, Dickey R, Fineman M, Maggs DG, Shen L, Strobel SA, Weyer C, Kolterman OG (2004). "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". Diabet Med 21 (11): 1204–12. PMID 15498087. doi:10.1111/j.1464-5491.2004.01319.x.

doi.org

dx.doi.org

Lorenzo A, Razzaboni B, Weir GC, Yankner BA (1994). "Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus". Nature 368 (6473): 756–60. PMID 8152488. doi:10.1038/368756a0.
Roth JD and al. (2008). "Leptin responsiveness restored by amylin agonism in diet-induced obesity: Evidence from nonclinical and clinical studies". PNAS 105 (20): 7257–7262. PMC 2438237. PMID 18458326. doi:10.1073/pnas.0706473105.
Lim YA, Rhein V, Baysang G, Meier F, Poljak A, Raftery MJ, Guilhaus M, Ittner LM, Eckert A, Götz J. (2010). "Abeta and human amylin share a common toxicity pathway via mitochondrial dysfunction". Proteomics 10 (8): 1621–33. PMID 20186753. doi:10.1002/pmic.200900651.
Pittner RA, Albrandt K, Beaumont K; et al. (1994). "Molecular physiology of amylin". J. Cell. Biochem. 55 Suppl: 19–28. PMID 7929615. doi:10.1002/jcb.240550004.
Ratner RE, Dickey R, Fineman M, Maggs DG, Shen L, Strobel SA, Weyer C, Kolterman OG (2004). "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". Diabet Med 21 (11): 1204–12. PMID 15498087. doi:10.1111/j.1464-5491.2004.01319.x.
Roberts AN, Leighton B, Todd JA; et al. (1990). "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. PMC 298561. PMID 2690069. doi:10.1073/pnas.86.24.9662.
Brender JR, Lee EL, Cavitt MA, Gafni A, Steel DG, Ramamoorthy A (2008). "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. PMID 18444645. doi:10.1021/ja710484d.
Brender JR, Hartman K, Reid KR, Kennedy RT, Ramamoorthy A (2008). "A Single Mutation in the Non-Amyloidogenic Region of IAPP (Amylin) Greatly Reduces Toxicity". Biochemistry 47 (48): 12680–8. PMC 2645932. PMID 18989933. doi:10.1021/bi801427c.
Nanga RP, Brender JR, Xu J, Veglia G, Ramamoorthy A (2008). "Structures of Rat and Human Islet Amyloid Polypeptide IAPP1–19 in Micelles by NMR Spectroscopy". Biochemistry 47 (48): 12689–97. PMC 2953382. PMID 18989932. doi:10.1021/bi8014357.
Brender JR, Dürr UH, Heyl D, Budarapu MB, Ramamoorthy A (2007). "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. PMC 2042489. PMID 17662957. doi:10.1016/j.bbamem.2007.07.001.
Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB (1987). "Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients". Proc Natl Acad Sci USA 84 (23): 8628–32. PMC 299599. PMID 3317417. doi:10.1073/pnas.84.23.8628.
Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH (1987). "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. PMC 304980. PMID 3035556. doi:10.1073/pnas.84.11.3881.
Shen Y, Joachimiak A, Rosner MR, Tang WJ (2006). "Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism". Nature 443 (7113): 870–4. PMID 17051221. doi:10.1038/nature05143.
Hay DL, Christopoulos G, Christopoulos A, Sexton PM (2004). "Amylin receptors: molecular composition and pharmacology". Biochem Soc Trans 32 (5): 865–7. PMID 15494035. doi:10.1042/BST0320865.

nih.gov

ncbi.nlm.nih.gov

"Entrez Gene: IAPP islet amyloid polypeptide".
Hayden MR (2002). "Islet amyloid, metabolic syndrome, and the natural progressive history of type 2 diabetes mellitus". JOP 3 (5): 126–38. PMID 12221327.
Lorenzo A, Razzaboni B, Weir GC, Yankner BA (1994). "Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus". Nature 368 (6473): 756–60. PMID 8152488. doi:10.1038/368756a0.
Roth JD and al. (2008). "Leptin responsiveness restored by amylin agonism in diet-induced obesity: Evidence from nonclinical and clinical studies". PNAS 105 (20): 7257–7262. PMC 2438237. PMID 18458326. doi:10.1073/pnas.0706473105.
Lim YA, Rhein V, Baysang G, Meier F, Poljak A, Raftery MJ, Guilhaus M, Ittner LM, Eckert A, Götz J. (2010). "Abeta and human amylin share a common toxicity pathway via mitochondrial dysfunction". Proteomics 10 (8): 1621–33. PMID 20186753. doi:10.1002/pmic.200900651.
Pittner RA, Albrandt K, Beaumont K; et al. (1994). "Molecular physiology of amylin". J. Cell. Biochem. 55 Suppl: 19–28. PMID 7929615. doi:10.1002/jcb.240550004.
Ratner RE, Dickey R, Fineman M, Maggs DG, Shen L, Strobel SA, Weyer C, Kolterman OG (2004). "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". Diabet Med 21 (11): 1204–12. PMID 15498087. doi:10.1111/j.1464-5491.2004.01319.x.
Roberts AN, Leighton B, Todd JA; et al. (1990). "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. PMC 298561. PMID 2690069. doi:10.1073/pnas.86.24.9662.
Brender JR, Lee EL, Cavitt MA, Gafni A, Steel DG, Ramamoorthy A (2008). "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. PMID 18444645. doi:10.1021/ja710484d.
Brender JR, Hartman K, Reid KR, Kennedy RT, Ramamoorthy A (2008). "A Single Mutation in the Non-Amyloidogenic Region of IAPP (Amylin) Greatly Reduces Toxicity". Biochemistry 47 (48): 12680–8. PMC 2645932. PMID 18989933. doi:10.1021/bi801427c.
Nanga RP, Brender JR, Xu J, Veglia G, Ramamoorthy A (2008). "Structures of Rat and Human Islet Amyloid Polypeptide IAPP1–19 in Micelles by NMR Spectroscopy". Biochemistry 47 (48): 12689–97. PMC 2953382. PMID 18989932. doi:10.1021/bi8014357.
Brender JR, Dürr UH, Heyl D, Budarapu MB, Ramamoorthy A (2007). "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. PMC 2042489. PMID 17662957. doi:10.1016/j.bbamem.2007.07.001.
Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB (1987). "Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients". Proc Natl Acad Sci USA 84 (23): 8628–32. PMC 299599. PMID 3317417. doi:10.1073/pnas.84.23.8628.
Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH (1987). "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. PMC 304980. PMID 3035556. doi:10.1073/pnas.84.11.3881.
Shen Y, Joachimiak A, Rosner MR, Tang WJ (2006). "Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism". Nature 443 (7113): 870–4. PMID 17051221. doi:10.1038/nature05143.
Hay DL, Christopoulos G, Christopoulos A, Sexton PM (2004). "Amylin receptors: molecular composition and pharmacology". Biochem Soc Trans 32 (5): 865–7. PMID 15494035. doi:10.1042/BST0320865.