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Emily Berkman/Sandbox 2
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==Introduction== | ==Introduction== | ||
Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref> | Starting in 1900, amylin deposits were first discovered in [https://en.wikipedia.org/wiki/Pancreatic_islets pancreatic islet] cells in diabetic patients. Later in 1943, more characterization was done and it was determined that these amylin deposits were [https://en.wikipedia.org/wiki/Amyloid amyloid] in nature. More research was done over the years and by the 1980s, amylin was properly identified and the 37 amino acid sequence was identified. By 1995, the first analog of amylin, [https://en.wikipedia.org/wiki/Pramlintide pramlintide], was synthesized. In the late 1990s, it was discovered through [https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy cryogenic electron microscopy] that the amylin receptor was made of the calcitonin receptor core. The calcitonin heterodimerizes with a receptor-activating modifying protein, or RAMP, to form different amylin receptors.<ref name="Bower">PMID:27061187</ref> | ||
| - | [[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species.]] | + | [[Image:conserved residues.png|400 px|left|thumb|Figure 1. Sequence alignment comparing the amylin residues across species. <ref name="Bower">PMID:27061187</ref>]] |
==Amylin== | ==Amylin== | ||
Revision as of 19:44, 16 April 2024
amylin images
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References
- ↑ 1.0 1.1 1.2 Bower RL, Hay DL. Amylin structure-function relationships and receptor pharmacology: implications for amylin mimetic drug development. Br J Pharmacol. 2016 Jun;173(12):1883-98. PMID:27061187 doi:10.1111/bph.13496
- ↑ Cao J, Belousoff MJ, Liang YL, Johnson RM, Josephs TM, Fletcher MM, Christopoulos A, Hay DL, Danev R, Wootten D, Sexton PM. A structural basis for amylin receptor phenotype. Science. 2022 Mar 25;375(6587):eabm9609. PMID:35324283 doi:10.1126/science.abm9609
