ArticleThe Biochemical journal2001
Transcriptional and translational mechanisms of cytochrome b5 reductase isoenzyme generation in humans.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Three novel mutations in CYB5R3 gene causing NADH-cytochrome b5 reductase enzyme deficiency leads to recessive congenital methaemoglobinemia.Molecular biology reports · 2022Article
- Neurological and Neuroimaging Features ofBrain sciences · 2022Article
- GGPP depletion initiates metaflammation through disequilibrating CYB5R3-dependent eicosanoid metabolism.The Journal of biological chemistry · 2020Article
- Genetic cause for congenital methemoglobinemia in an Australian Pomeranian dog.Journal of veterinary internal medicine · 2019Article
- Cellular and Molecular Mechanisms of Recessive Hereditary Methaemoglobinaemia Type II.Journal of clinical medicine · 2018Review
- A comparative genomics study of carbohydrate/glucose metabolic genes: from fish to mammals.BMC genomics · 2018Article
- Familial Congenital Methemoglobinemia in Pomeranian Dogs Caused by a Missense Variant in the NADH-Cytochrome B5 Reductase Gene.Journal of veterinary internal medicine · 2018Article
- Membrane-bound CYB5R3 is a common effector of nutritional and oxidative stress response through FOXO3a and Nrf2.Antioxidants & redox signaling · 2014Article
- Reductive detoxification of arylhydroxylamine carcinogens by human NADH cytochrome b5 reductase and cytochrome b5.Chemical research in toxicology · 2006Article
- Severe neurological impairment in hereditary methaemoglobinaemia type 2.European journal of pediatrics · 2004Article
- Hydrogen peroxide- and cell-density-regulated expression of NADH-cytochrome b5 reductase in HeLa cells.Journal of bioenergetics and biomembranes · 2003Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytochrome b5 reductase (b5R) is an essential enzyme that exists in soluble and membrane-bound isoforms, each with specific functions. In the rat, the two forms are generated from alternative transcripts differing in the first exons. In contrast, the biogenesis of b5R isoforms in the human is not yet well understood. In the present study we have detected three novel alternative exons, designated 1S, S' and 1B, located between the first alternative exon 1M and the common second exon in the human b5R gene. Accordingly, multiple M-type, S-type and SS'-type and B-type transcripts are generated. All types of human b5R transcript are expressed ubiquitously. An analysis of in vitro translation products demonstrated an alternative use of different AUG initiators resulting in the production of various human b5R protein isoforms. Our results indicate that the organization of the 5' region of the b5R gene is not conserved between rodents and humans. Insertion of Alu elements into the human b5R gene, in particular just upstream of the S/S' region, could be responsible for dynamic events of gene rearrangement during evolution.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.