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DPP9 gene

Known as: DIPEPTIDYL PEPTIDASE IX, DPP9, DIPEPTIDYL PEPTIDASE IV-RELATED PROTEIN 2 
This gene is involved in dipeptidyl aminopeptidase activity.
National Institutes of Health

Related topics

Related topics

4 relations
DPP6 geneDPP9 protein, humanHydrolysisProteolysis

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Review
2015
Review
2015
The Dipeptidyl Peptidase Family, Prolyl Oligopeptidase, and Prolyl Carboxypeptidase in the Immune System and Inflammatory Disease, Including Atherosclerosis
Research from over the past 20 years has implicated dipeptidyl peptidase (DPP) IV and its family members in many processes and… 
Highly Cited
2013
Highly Cited
2013
Dipeptidyl peptidases in atherosclerosis: expression and role in macrophage differentiation, activation and apoptosis
Atherosclerosis is a chronic inflammatory disorder of the arterial wall leading to coronary artery disease, stroke, and… 
Review
2013
Review
2013
Advances in Understanding the Expression and Function of Dipeptidyl Peptidase 8 and 9
DPP8 and DPP9 are recently identified members of the dipeptidyl peptidase IV (DPPIV) enzyme family, which is characterized by the… 
Highly Cited
2012
Highly Cited
2012
A Novel SUMO1-specific Interacting Motif in Dipeptidyl Peptidase 9 (DPP9) That Is Important for Enzymatic Regulation*
Background: Interactions of SUMO isoforms/paralogs involve a groove on SUMO1–3 and a SIM on the downstream effector. Results: A… 
Highly Cited
2012
Highly Cited
2012
DA-1229, a novel and potent DPP4 inhibitor, improves insulin resistance and delays the onset of diabetes.
Review
2009
Review
2009
Dipeptidyl peptidase-4 (CD26): knowing the function before inhibiting the enzyme.
Dipeptidyl peptidase-4 (DPP4) or adenosine deaminase complexing protein 2 (ADCP 2) or T-cell activation antigen CD26 (EC 3.4.14.5… 
Highly Cited
2009
Highly Cited
2009
The Cytoplasmic Peptidase DPP9 Is Rate-limiting for Degradation of Proline-containing Peptides*
Protein degradation is an essential process that continuously takes place in all living cells. Regulated degradation of most… 
Highly Cited
2009
Highly Cited
2009
Biochemistry, pharmacokinetics, and toxicology of a potent and selective DPP8/9 inhibitor.
Highly Cited
2005
Highly Cited
2005
Dipeptidyl peptidase IV inhibition for the treatment of type 2 diabetes: potential importance of selectivity over dipeptidyl peptidases 8 and 9.
Dipeptidyl peptidase (DPP)-IV inhibitors are a new approach to the treatment of type 2 diabetes. DPP-IV is a member of a family… 
Highly Cited
2004
Highly Cited
2004
Discovery of potent and selective phenylalanine based dipeptidyl peptidase IV inhibitors.
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