Emily Berkman/Sandbox 2: Difference between revisions
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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== | ||
