| Title |
Structural and Biochemical Studies of Human 4-hydroxy-2-oxoglutarate Aldolase: Implications for Hydroxyproline Metabolism in Primary Hyperoxaluria
|
|---|---|
| Published in |
PLOS ONE, October 2011
|
| DOI | 10.1371/journal.pone.0026021 |
| Pubmed ID | |
| Authors |
Travis J. Riedel, Lynnette C. Johnson, John Knight, Roy R. Hantgan, Ross P. Holmes, W. Todd Lowther |
| Abstract |
4-hydroxy-2-oxoglutarate (HOG) aldolase is a unique enzyme in the hydroxyproline degradation pathway catalyzing the cleavage of HOG to pyruvate and glyoxylate. Mutations in this enzyme are believed to be associated with the excessive production of oxalate in primary hyperoxaluria type 3 (PH3), although no experimental data is available to support this hypothesis. Moreover, the identity, oligomeric state, enzymatic activity, and crystal structure of human HOGA have not been experimentally determined. |
Mendeley readers
The data shown below were compiled from readership statistics for 46 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| United Kingdom | 1 | 2% |
| Unknown | 45 | 98% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 16 | 35% |
| Student > Master | 5 | 11% |
| Student > Bachelor | 5 | 11% |
| Other | 4 | 9% |
| Researcher | 4 | 9% |
| Other | 6 | 13% |
| Unknown | 6 | 13% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 13 | 28% |
| Biochemistry, Genetics and Molecular Biology | 11 | 24% |
| Medicine and Dentistry | 7 | 15% |
| Chemistry | 5 | 11% |
| Pharmacology, Toxicology and Pharmaceutical Science | 1 | 2% |
| Other | 5 | 11% |
| Unknown | 4 | 9% |