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Hep27, a member of the short-chain dehydrogenase/reductase family, is an NADPH-dependent dicarbonyl reductase expressed in vascular endothelial tissue

Overview of attention for article published in Cellular and Molecular Life Sciences, May 2006
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About this Attention Score

  • In the top 25% of all research outputs scored by Altmetric
  • Good Attention Score compared to outputs of the same age (71st percentile)
  • Average Attention Score compared to outputs of the same age and source

Mentioned by

patent
2 patents
wikipedia
1 Wikipedia page

Citations

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41 Dimensions

Readers on

mendeley
44 Mendeley
Title
Hep27, a member of the short-chain dehydrogenase/reductase family, is an NADPH-dependent dicarbonyl reductase expressed in vascular endothelial tissue
Published in
Cellular and Molecular Life Sciences, May 2006
DOI 10.1007/s00018-006-6013-y
Pubmed ID
Authors

N. Shafqat, J. Shafqat, G. Eissner, H. -U. Marschall, K. Tryggvason, U. Eriksson, F. Gabrielli, H. Lardy, H. Jörnvall, U. Oppermann

Abstract

Human Hep27 was originally isolated from growth-arrested HepG2 cells and identified as a member of the superfamily of short-chain dehydrogenases/reductases (SDR). Its substrate specificity has not been determined, but a cross-species comparison suggests that it occurs in widely divergent species, such as human, Cenorhabditis elegans, Drosophila and Arabidopsis thaliana. In this study, Hep27 was expressed as a His(6) fusion protein, and subjected to a substrate screen, using a compound library of SDR substrates, comprising steroids, retinoids, sugars and carbonyl compounds. Whereas no steroid dehydrogenase or retinoid activity was detected, it was found that Hep27 catalyzed the NADPH-dependent reduction of dicarbonyl compounds, like 3,4-hexanedione and 1-phenyl-1,2-propanedione with similar turnover numbers as DCXR (a mitochondrial dicarbonyl reductase/xylulose reductase). In contrast, Hep27 does not convert sugar substrates like xylulose or threose. Based on its substrate specificity and expression in endothelial tissues, it is suggested that Hep27 functions as a dicarbonyl reductase in enzymatic inactivation of reactive carbonyls, involved in covalent modification of cellular components.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 44 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
United States 1 2%
Ireland 1 2%
Unknown 42 95%

Demographic breakdown

Readers by professional status Count As %
Researcher 11 25%
Student > Ph. D. Student 8 18%
Professor 5 11%
Student > Doctoral Student 4 9%
Professor > Associate Professor 3 7%
Other 5 11%
Unknown 8 18%
Readers by discipline Count As %
Agricultural and Biological Sciences 16 36%
Biochemistry, Genetics and Molecular Biology 8 18%
Pharmacology, Toxicology and Pharmaceutical Science 2 5%
Immunology and Microbiology 2 5%
Chemical Engineering 1 2%
Other 4 9%
Unknown 11 25%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 6. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 07 July 2015.
All research outputs
#4,965,094
of 23,794,258 outputs
Outputs from Cellular and Molecular Life Sciences
#928
of 4,151 outputs
Outputs of similar age
#12,406
of 67,279 outputs
Outputs of similar age from Cellular and Molecular Life Sciences
#14
of 46 outputs
Altmetric has tracked 23,794,258 research outputs across all sources so far. Compared to these this one has done well and is in the 76th percentile: it's in the top 25% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 4,151 research outputs from this source. They typically receive a little more attention than average, with a mean Attention Score of 6.0. This one has gotten more attention than average, scoring higher than 70% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 67,279 tracked outputs that were published within six weeks on either side of this one in any source. This one has gotten more attention than average, scoring higher than 71% of its contemporaries.
We're also able to compare this research output to 46 others from the same source and published within six weeks on either side of this one. This one has gotten more attention than average, scoring higher than 50% of its contemporaries.