Sandbox Reserved 1585

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== Overview ==
== Overview ==
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Test text<ref name="ref1" />
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Human carbonic anhydrase are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. This protein contains a zinc ion and 260 amino acid residues. Human carbonic anhydrase activation has been associated with cardiomyopathy in diabetics.<ref name="ref2">PMID:24670789</ref> In diabetic patents with postinfarct heart failure it was found that their level of human carbonic anhyrase 1 was significantly higher then the levels of non-diabetics.<ref name="ref2" /> Developing an inhibitor for human carbonic anhydrase 1 is contributing to the treatment of these diseases.
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Human carbonic anhydrase are zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. This protein contains a zinc ion and 260 amino acid residues. Human carbonic anhydrase activation has been associated with cardiomyopathy in diabetics.<ref name="ref2">PMID:24670789</ref> In diabetic patents with postinfarct heart failure it was found that their level of human carbonic anhyrase 1 was significantly higher then the levels of non-diabetics.<ref name="ref2" /> Developing an inhibitor for human carbonic anhydrase 1 is contributing to the treatment of these diseases.<ref>DOI 10.1038/nrd2467</ref>
== Function ==
== Function ==

Revision as of 00:50, 28 November 2019

This Sandbox is Reserved from September 14, 2021, through May 31, 2022, for use in the class Introduction to Biochemistry taught by User:John Means at the University of Rio Grande, Rio Grande, OH, USA. This reservation includes 5 reserved sandboxes (Sandbox Reserved 1590 through Sandbox Reserved 1594).
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
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Human Carbonic Anhydrase 1

Human Carbonic Anhydrase

Drag the structure with the mouse to rotate

References

  1. ↑ 1.0 1.1 Kannan KK, Ramanadham M, Jones TA. Structure, refinement, and function of carbonic anhydrase isozymes: refinement of human carbonic anhydrase I. Ann N Y Acad Sci. 1984;429:49-60. PMID:6430186
  2. ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  3. ↑ 3.0 3.1 Torella D, Ellison GM, Torella M, Vicinanza C, Aquila I, Iaconetti C, Scalise M, Marino F, Henning BJ, Lewis FC, Gareri C, Lascar N, Cuda G, Salvatore T, Nappi G, Indolfi C, Torella R, Cozzolino D, Sasso FC. Carbonic anhydrase activation is associated with worsened pathological remodeling in human ischemic diabetic cardiomyopathy. J Am Heart Assoc. 2014 Mar 26;3(2):e000434. doi: 10.1161/JAHA.113.000434. PMID:24670789 doi:http://dx.doi.org/10.1161/JAHA.113.000434
  4. ↑ Supuran CT. Carbonic anhydrases: novel therapeutic applications for inhibitors and activators. Nat Rev Drug Discov. 2008 Feb;7(2):168-81. doi: 10.1038/nrd2467. PMID:18167490 doi:http://dx.doi.org/10.1038/nrd2467
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