Dipeptidyl peptidase

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<StructureSection load='1jqp' size='350' side='right' caption='Glycosylated dipeptidyl peptidase I complex with sulfate and chloride ion (green) (PDB entry [[1jqp]])' scene='Dipeptidyl_peptidase/Cv/1'>
<StructureSection load='1jqp' size='350' side='right' caption='Glycosylated dipeptidyl peptidase I complex with sulfate and chloride ion (green) (PDB entry [[1jqp]])' scene='Dipeptidyl_peptidase/Cv/1'>
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DPP-IV level is alternating in certain malignancies.<ref>PMID:15375776</ref> DPP-IV inhibitors control body glucose levels and provide potential advantages in diabetes type 2 therapies.<ref>PMID:17073841</ref>
DPP-IV level is alternating in certain malignancies.<ref>PMID:15375776</ref> DPP-IV inhibitors control body glucose levels and provide potential advantages in diabetes type 2 therapies.<ref>PMID:17073841</ref>
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== Disease ==
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DPP-IV is involved in the development of various chronic liver disease like hepatitis C virus infection.<ref>PMID:23613622</ref>
</StructureSection>
</StructureSection>
== 3D Structures of Dipeptidyl peptidase ==
== 3D Structures of Dipeptidyl peptidase ==

Revision as of 10:13, 30 December 2015

Glycosylated dipeptidyl peptidase I complex with sulfate and chloride ion (green) (PDB entry 1jqp)

Drag the structure with the mouse to rotate

3D Structures of Dipeptidyl peptidase

Updated on 30-December-2015

References

  1. Pro B, Dang NH. CD26/dipeptidyl peptidase IV and its role in cancer. Histol Histopathol. 2004 Oct;19(4):1345-51. PMID:15375776
  2. Barnett A. DPP-4 inhibitors and their potential role in the management of type 2 diabetes. Int J Clin Pract. 2006 Nov;60(11):1454-70. PMID:17073841 doi:10.1111/j.1742-1241.2006.01178.x
  3. Itou M, Kawaguchi T, Taniguchi E, Sata M. Dipeptidyl peptidase-4: a key player in chronic liver disease. World J Gastroenterol. 2013 Apr 21;19(15):2298-306. doi:, 10.3748/wjg.v19.i15.2298. PMID:23613622 doi:http://dx.doi.org/10.3748/wjg.v19.i15.2298

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