ArticleFEBS open bio2014
Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction.
Article in FEBS open bio, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 23 citations in OpenAlex.
- A viral protein disrupts rice cell wall integrity and modulates interactions with viruses and insects.Stress biology · 2026Article
- Storage Drives Alterations of Proteomic and Protein Structural Properties in Rice (Foods (Basel, Switzerland) · 2022Article
- Genetic Background Negates Improvements in Rice Flour Characteristics and Food Processing Properties Caused by a Mutant Allele of the PDIL1-1 Seed Storage Protein Gene.Rice (New York, N.Y.) · 2022Article
- The thiol-disulfide exchange activity of AtPDI1 is involved in the response to abiotic stresses.BMC plant biology · 2021Article
- Towards coeliac-safe bread.Plant biotechnology journal · 2020Article
- Multi-omics profiling of calcium-induced human keratinocytes differentiation reveals modulation of unfolded protein response signaling pathways.Cell cycle (Georgetown, Tex.) · 2019Article
- Identification and Functional Analysis of a Protein Disulfide Isomerase (Frontiers in plant science · 2018Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1, PDIL1;4, and PDIL2;3) and found that PDIL1;1 exhibited the highest catalytic activity for both disulfide bond formation and disulfide bond reduction. The activity of PDIL1;1-catalyzed disulfide bond reduction, in which two redox-active sites were involved, was enhanced by increasing the glutathione concentration. These results suggest that PDIL1;1 plays primary roles in both disulfide bond formation and disulfide bond reduction, which allow for redox control of protein quality and packaging.
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Registered trials
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