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Mendeley readers
| Title |
A computational analysis of the three isoforms of glutamate dehydrogenase reveals structural features of the isoform EC 1.4.1.4 supporting a key role in ammonium assimilation by plants
|
|---|---|
| Published in |
Biology Direct, December 2006
|
| DOI | 10.1186/1745-6150-1-38 |
| Pubmed ID | |
| Authors |
Emmanuel Jaspard |
| Abstract |
There are three isoforms of glutamate dehydrogenase. The isoform EC 1.4.1.4 (GDH4) catalyses glutamate synthesis from 2-oxoglutarate and ammonium, using NAD(P)H. Ammonium assimilation is critical for plant growth. Although GDH4 from animals and prokaryotes are well characterized, there are few data concerning plant GDH4, even from those whose genomes are well annotated. |
Mendeley readers
The data shown below were compiled from readership statistics for 25 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 25 | 100% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Researcher | 7 | 28% |
| Student > Master | 3 | 12% |
| Student > Ph. D. Student | 3 | 12% |
| Student > Doctoral Student | 2 | 8% |
| Student > Postgraduate | 2 | 8% |
| Other | 3 | 12% |
| Unknown | 5 | 20% |
| Readers by discipline | Count | As % |
|---|---|---|
| Agricultural and Biological Sciences | 9 | 36% |
| Biochemistry, Genetics and Molecular Biology | 9 | 36% |
| Unspecified | 2 | 8% |
| Unknown | 5 | 20% |