ArticleThe Biochemical journal2004
Overexpression of inactive arylsulphatase mutants and in vitro activation by light-dependent oxidation with vanadate.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
1 citing paper in PubMed, 5 citations in OpenAlex.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Arylsulphatases B (ASB) and A (ASA) are subject to a unique post-translational modification that is required for their function. The modification reaction, conversion of an active-site cysteine into a formylglycine, becomes saturated when these enzymes are overexpressed. We have removed the possibility of in vivo modification by expressing mutants of ASB and ASA in which the active-site cysteine is substituted with a serine. These mutants are expressed much more efficiently when compared with the native enzymes under identical conditions. The purified ASB mutant can then be converted into catalytically active ASB in vitro using vanadate and light.
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Registered trials
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