| Title |
High-Affinity Inhibitors of Human NAD+-Dependent 15-Hydroxyprostaglandin Dehydrogenase: Mechanisms of Inhibition and Structure-Activity Relationships
|
|---|---|
| Published in |
PLOS ONE, November 2010
|
| DOI | 10.1371/journal.pone.0013719 |
| Pubmed ID | |
| Authors |
Frank H. Niesen, Lena Schultz, Ajit Jadhav, Chitra Bhatia, Kunde Guo, David J. Maloney, Ewa S. Pilka, Minghua Wang, Udo Oppermann, Tom D. Heightman, Anton Simeonov |
| Abstract |
15-Hydroxyprostaglandin dehydrogenase (15-PGDH, EC 1.1.1.141) is the key enzyme for the inactivation of prostaglandins, regulating processes such as inflammation or proliferation. The anabolic pathways of prostaglandins, especially with respect to regulation of the cyclooxygenase (COX) enzymes have been studied in detail; however, little is known about downstream events including functional interaction of prostaglandin-processing and -metabolizing enzymes. High-affinity probes for 15-PGDH will, therefore, represent important tools for further studies. |
Mendeley readers
The data shown below were compiled from readership statistics for 47 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United States | 3 | 6% |
| United Kingdom | 2 | 4% |
| Romania | 1 | 2% |
| Unknown | 41 | 87% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 15 | 32% |
| Researcher | 12 | 26% |
| Student > Bachelor | 5 | 11% |
| Student > Postgraduate | 3 | 6% |
| Student > Doctoral Student | 2 | 4% |
| Other | 6 | 13% |
| Unknown | 4 | 9% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 14 | 30% |
| Chemistry | 13 | 28% |
| Biochemistry, Genetics and Molecular Biology | 7 | 15% |
| Medicine and Dentistry | 3 | 6% |
| Immunology and Microbiology | 2 | 4% |
| Other | 4 | 9% |
| Unknown | 4 | 9% |