ArticleMolecular and cellular biology1995
Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 79 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
79 citing papers in PubMed, 214 citations in OpenAlex.
- MAFF is a transcription factor that regulates contraction-induced skeletal muscle transcription.Life science alliance · 2026Article
- Sepsis-Induced Exosomal Transfer ofCells · 2026Article
- Transcription factors as essential regulators of myometrial smooth muscle cell function during pregnancy and labor.Cellular and molecular life sciences : CMLS · 2026Review
- Article
- MAFB: a key regulator of myeloid commitment involved in hematological diseases.Cell death discovery · 2025Review
- Review
- PRMT1 promotes epigenetic reprogramming associated with acquired chemoresistance in pancreatic cancer.Cell reports · 2024Article
- Nrf-2/ROS/NF-κB pathway is modulated by cynarin in human mesenchymal stem cells in vitro from ankylosing spondylitis.Clinical and translational science · 2024Article
- Crosstalk between phytochemicals and inflammatory signaling pathways.Inflammopharmacology · 2023Review
- Transcriptional and post-transcriptional regulation of checkpoint genes on the tumour side of the immunological synapse.Heredity · 2022Article
- ERK and p38 MAPK inhibition controls NF-E2 degradation and profibrotic signaling in renal proximal tubule cells.Life sciences · 2021Article
- The Persistent Pain Transcriptome: Identification of Cells and Molecules Activated by Hyperalgesia.The journal of pain · 2021Article
- MafF Is an Antiviral Host Factor That Suppresses Transcription from Hepatitis B Virus Core Promoter.Journal of virology · 2021Article
- Regulation of inflammation by the antioxidant haem oxygenase 1.Nature reviews. Immunology · 2021Review
- MAFG-driven osteosarcoma cell progression is inhibited by a novel miRNA miR-4660.Molecular therapy. Nucleic acids · 2021Article
- Redox and Inflammatory Signaling, the Unfolded Protein Response, and the Pathogenesis of Pulmonary Hypertension.Advances in experimental medicine and biology · 2021Article
- The Role of Nrf2 in Hearing Loss.Frontiers in pharmacology · 2021Review
- HTLV-1 basic leucine zipper factor protects cells from oxidative stress by upregulating expression of Heme Oxygenase I.PLoS pathogens · 2019Article
- Regulation of CXCL1 chemokine and CSF3 cytokine levels in myometrial cells by the MAFF transcription factor.Journal of cellular and molecular medicine · 2019Article
- RPA1 binding to NRF2 switches ARE-dependent transcriptional activation to ARE-NRE-dependent repression.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The maf oncogene encodes a bZip nuclear protein which recognizes sequences related to an AP-1 site either as a homodimer or as heterodimers with Fos and Jun. We describe here a novel maf-related gene, mafG, which shows extensive homology with two other maf-related genes, mafK and mafF. These three maf-related genes encode small basic-leucine zipper proteins lacking the trans-activator domain of v-Maf. Bacterially expressed small Maf proteins bind to DNA as homodimers with a sequence recognition profile that is virtually identical to that of v-Maf. As we have previously described, the three small Maf proteins also dimerize with the large subunit of NF-E2 (p45) to form an erythroid cell-specific transcription factor, NF-E2, which has distinct DNA-binding specificity. This study shows that the small Maf proteins can also dimerize among themselves and with Fos and a newly identified p45-related molecule (Ech) but not with v-Maf or Jun. Although the small Maf proteins preferentially recognize the consensus NF-E2 sequence as heterodimers with either NF-E2 p45, Ech, or Fos, these heterodimers seemed to be different in their transactivation potentials. Coexpression of Fos and small Mafs could not activate a promoter with tandem repeats of the NF-E2 site. These results raise the possibility that tissue-specific gene expression and differentiation of erythroid cells are regulated by competition among Fos, NF-E2 p45, and Ech for small Maf proteins and for binding sites.
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Registered trials
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.