ArticleScientific reports2019
Enzyme activity and structural features of three single-domain phloem cyclophilins from Brassica napus.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
4 citing papers in PubMed, 6 citations in OpenAlex.
- Characterization and regulation of salt upregulated cyclophilin from a halotolerant strain of Penicillium oxalicum.Scientific reports · 2023Article
- The mRNA mobileome: challenges and opportunities for deciphering signals from the noise.The Plant cell · 2023Review
- Cyclophilin anaCyp40 regulates photosystem assembly and phycobilisome association in a cyanobacterium.Nature communications · 2022Article
- Plant Cyclophilins: Multifaceted Proteins With Versatile Roles.Frontiers in plant science · 2020Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cyclophilins (CYPs) are a group of ubiquitous prolyl cis/trans isomerases (PPIases). It was shown that plants possess the most diverse CYP families and that these are abundant in the phloem long-distance translocation stream. Since phloem exudate showed PPIase activity, three single-domain CYPs that occur in phloem samples from Brassica napus were characterised on functional and structural levels. It could be shown that they exhibit isomerase activity and that this activity is controlled by a redox regulation mechanism, which has been postulated for divergent CYPs. The structure determination by small-angle X-ray scattering experiments revealed a conserved globular shape. In addition, the high-resolution crystal structure of BnCYP19-1 was resolved and refined to 2.0 Å resolution, and the active sites of related CYPs as well as substrate binding were modelled. The obtained data and results support the hypothesis that single domain phloem CYPs are active phloem PPIases that may function as chaperones.
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Registered trials
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