ArticleScientific reports2019
Identification of the laccase-like multicopper oxidase gene family of sweet cherry (Prunus avium L.) and expression analysis in six ancient Tuscan varieties.
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 9 papers.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Contribution of theInternational journal of molecular sciences · 2023Review
- Molecular mechanism of Cu metal and drought stress resistance triggered byFrontiers in plant science · 2022Article
- Laccases as green and versatile biocatalysts: from lab to enzyme market-an overview.Bioresources and bioprocessing · 2021Review
- The role of JrLACs in the lignification of walnut endocarp.BMC plant biology · 2021Article
- Plant Copper Metalloenzymes As Prospects for New Metabolism Involving Aromatic Compounds.Frontiers in plant science · 2021Review
- Molecular investigation of Tuscan sweet cherries sampled over three years: gene expression analysis coupled to metabolomics and proteomics.Horticulture research · 2021Article
- Evolutionary divergence of function and expression of laccase genes in plants.Journal of genetics · 2020Article
- Identification of Jasmonic Acid Biosynthetic Genes in Sweet Cherry and Expression Analysis in Four Ancient Varieties from Tuscany.International journal of molecular sciences · 2019Article
- Tuscan Varieties of Sweet Cherry Are Rich Sources of Ursolic and Oleanolic Acid: Protein Modeling Coupled to Targeted Gene Expression and Metabolite Analyses.Molecules (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Laccase-like multicopper oxidases (LMCOs) are versatile enzymes used as biocatalysts performing the oxidation of different substrates of industrial relevance, with or without the intervention of a mediator. They have attracted a lot of interest for biotechnological applications in light of their eco-friendliness: they indeed oxidize the substrate(s) by coupling the four electron reduction of the final acceptor, molecular oxygen (O
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Registered trials
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