ReviewFree radical biology & medicine2020
Structure and functions of cellular redox sensor HSCARG/NMRAL1, a linkage among redox status, innate immunity, DNA damage response, and cancer.
Review in Free radical biology & medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Comparing DNA Methylation Landscapes in Peripheral Blood from Myalgic Encephalomyelitis/Chronic Fatigue Syndrome and Long COVID Patients.International journal of molecular sciences · 2025Article
- Tangeretin Suppresses Fumonisin Production by Modulating an NmrA- and HSCARG-like Protein inJournal of fungi (Basel, Switzerland) · 2025Article
- NMRAL1 as a Causal Factor in Postherpetic Neuralgia: A Proteome-Wide Mendelian Randomization Study.Journal of pain research · 2025Article
- Article
- The gut microbiota and its metabolite butyrate shape metabolism and antiviral immunity along the gut-lung axis in the chicken.Communications biology · 2024Article
- High-throughput screening unveils nitazoxanide as a potent PRRSV inhibitor by targeting NMRAL1.Nature communications · 2024Article
- Direct 3D Sampling of the Embryonic Mouse Head: Layer-wise Nanosecond Infrared Laser (NIRL) Ablation from Scalp to Cortex for Spatially Resolved Proteomics.Analytical chemistry · 2023Article
- Multitissue H3K27ac profiling of GTEx samples links epigenomic variation to disease.Nature genetics · 2023Article
- Fungal P450 Deconstructs the 2,5-Diazabicyclo[2.2.2]octane RingJournal of the American Chemical Society · 2023Article
- An NmrA-like enzyme-catalysed redox-mediated Diels-Alder cycloaddition with anti-selectivity.Nature chemistry · 2023Article
- CRISPR/Cas-Based Approaches to Study Schizophrenia and Other Neurodevelopmental Disorders.International journal of molecular sciences · 2022Review
- Functional variant rs2270363 on 16p13.3 confers schizophrenia risk by regulating NMRAL1.Brain : a journal of neurology · 2022Article
- Mitonuclear mismatch alters nuclear gene expression in naturally introgressed Rhinolophus bats.Frontiers in zoology · 2021Article
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
NmrA-like proteins are NAD(P) (H) interacting molecules whose structures are similar to that of short-chain dehydrogenases. In this review, we focus on an NADP(H) sensor, HSCARG (also named NMRAL1), which is a NmrA-like protein that is widely present in mammals, and provide a comprehensive overview of the current knowledge of its structure and physiological functions. HSCARG selectively binds to the reduced form of type II coenzyme NADPH via its Rossmann fold domain. In response to reduction of intracellular NADPH concentration, HSCARG transforms from homodimer to monomer and exhibits enhanced interactions with its binding partners. In the cytoplasm, HSCARG negatively regulates innate immunity through impairing the activities of NF-κB and RLR pathways. Besides, HSCARG regulates redox homeostasis via suppression of ROS and NO generation. Intensive and persistent oxidative stress leads to translocation of HSCARG from the cytoplasm to the nucleus, where it regulates the DNA damage response. Taken together, HSCARG functions as a linkage between cellular redox status and other signaling pathways and fine-tunes cellular response to redox changes.
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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.