A new family of 2-hydroxyacid dehydrogenases
Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 165, Issue: 3, Page: 1371-1374
1989
- 82Citations
- 25Captures
- 2Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations82
- Citation Indexes82
- 82
- CrossRef70
- Captures25
- Readers25
- 25
- Mentions2
- References2
- 2
Article Description
The NADH-dependent hydroxypyruvate reductase from cucumber and the pdxB gene product of E. coli display significant homology to E. coli D-3-phosphoglycerate dehydrogenase. In contrast, these proteins do not display much similarity with other oxidoreductases or with other 2-hydroxyacid dehydrogenases in particular. On the basis of their relatedness and the structure of their substrates, these three enzymes constitute a new family of 2-hydroxyacid dehydrogenases distinct from malate and lactate dehydrogenase.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0006291X89927551; http://dx.doi.org/10.1016/0006-291x(89)92755-1; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0024835757&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/2692566; https://linkinghub.elsevier.com/retrieve/pii/0006291X89927551; http://linkinghub.elsevier.com/retrieve/pii/0006291X89927551; http://api.elsevier.com/content/article/PII:0006291X89927551?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:0006291X89927551?httpAccept=text/plain; http://dx.doi.org/10.1016/0006-291x%2889%2992755-1; https://dx.doi.org/10.1016/0006-291x%2889%2992755-1
Elsevier BV
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