ArticleThe Journal of biological chemistry2019
The carbon monoxide dehydrogenase accessory protein CooJ is a histidine-rich multidomain dimer containing an unexpected Ni(II)-binding site.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Nickel-chelatase activity of SirB variants mimicking the His arrangement in the naturally occurring nickel-chelatase CfbA.FEBS open bio · 2024Article
- Structural analysis of human CEACAM1 oligomerization.Communications biology · 2022Article
- Anaerobic carboxydotrophy in sulfur-respiring haloarchaea from hypersaline lakes.The ISME journal · 2022Article
- Structure, function, and biosynthesis of nickel-dependent enzymes.Protein science : a publication of the Protein Society · 2020Review
- Adaptive Laboratory Evolution ofFrontiers in microbiology · 2020Article
- Structural insight into metallocofactor maturation in carbon monoxide dehydrogenase.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Activation of nickel enzymes requires specific accessory proteins organized in multiprotein complexes controlling metal transfer to the active site. Histidine-rich clusters are generally present in at least one of the metallochaperones involved in nickel delivery. The maturation of carbon monoxide dehydrogenase in the proteobacterium
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Registered trials
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