Sandbox Reserved 1585
From Proteopedia
(Difference between revisions)
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<StructureSection load='2cab' size='340' side='right' caption='Human Carbonic Anhydrase' scene=''> | <StructureSection load='2cab' size='340' side='right' caption='Human Carbonic Anhydrase' scene=''> | ||
This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | This is a default text for your page ''''''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
- | You may include any references to papers as in: the use of JSmol in Proteopedia | + | You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol <ref name="ref1">PMID:6430186</ref> to the rescue. <ref>DOI 10.1002/ijch.201300024</ref> |
== Overview == | == Overview == | ||
- | Test text<ref | + | Test text<ref name="ref1" /> |
- | 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. 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. Developing an inhibitor for human carbonic anhydrase 1 is contributing to the treatment of these diseases. | + | 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. |
== Function == | == Function == |
Revision as of 00:49, 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). |
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More help: Help:Editing. For an example of a student Proteopedia page, please see Photosystem II, Tetanospasmin, or Guanine riboswitch. |
Human Carbonic Anhydrase 1
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References
- ↑ 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
- ↑ 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
- ↑ 3.0 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