ArticleHuman molecular genetics2015
Human FMRP contains an integral tandem Agenet (Tudor) and KH motif in the amino terminal domain.
Article in Human molecular genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.
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Who cites it
75 citing papers in PubMed, 113 citations in OpenAlex.
- Unraveling in vitro phase separation and aggregation properties of the structured region of FMRP and the impact of Fragile X syndrome-linked mutations.The FEBS journal · 2026Article
- The enigma of nuclear FMRP: facts and myths.Frontiers in cell and developmental biology · 2026Article
- RNA-Binding Proteins: Modulators of Canonical Wnt Signaling Pathway.International journal of molecular sciences · 2025Review
- A missense variant in the KH0-domain of FMRP downregulates the protein in a patient with the clinical hallmarks of fragile X syndrome.European journal of human genetics : EJHG · 2025Article
- Article
- Pathological and Functional Brain Amyloids: A New Concept Explaining the Differences.International journal of molecular sciences · 2025Review
- FMR1 KH0-KH1 domains coordinate mExperimental cell research · 2025Article
- From Discovery to Innovative Translational Approaches in 80 Years of Fragile X Syndrome Research.Biomedicines · 2025Review
- Age-dependent impairment of dopamine D1 receptor signalling in mouse striatum byBrain communications · 2025Article
- Review
- Nucleic acid-binding KH domain proteins influence a spectrum of biological pathways including as part of membrane-localized complexes.Journal of structural biology: X · 2024Article
- Article
- From wings to whiskers to stem cells: why every model matters in fragile X syndrome research.Journal of neurodevelopmental disorders · 2024Review
- The FXR1 network acts as signaling scaffold for actomyosin remodeling.bioRxiv : the preprint server for biology · 2024Article
- Fragile X Messenger Ribonucleoprotein Protein and Its Multifunctionality: From Cytosol to Nucleolus and Back.Biomolecules · 2024Review
- Article
- The nuclear isoforms of the Fragile X mental retardation RNA-binding protein associate with genomic DNA bridges.Molecular biology of the cell · 2023Article
- Mouse models of fragile X-related disorders.Disease models & mechanisms · 2023Review
- m6A readers, writers, erasers, and the m6A epitranscriptome in breast cancer.Journal of molecular endocrinology · 2023Review
- Prediction of Translational Regulation by Network Interaction in Synaptic Plasticity Induced withTheScientificWorldJournal · 2023Article
15 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Fragile X syndrome, a common cause of intellectual disability and autism, is due to mutational silencing of the FMR1 gene leading to the absence of its gene product, fragile X mental retardation protein (FMRP). FMRP is a selective RNA binding protein owing to two central K-homology domains and a C-terminal arginine-glycine-glycine (RGG) box. However, several properties of the FMRP amino terminus are unresolved. It has been documented for over a decade that the amino terminus has the ability to bind RNA despite having no recognizable functional motifs. Moreover, the amino terminus has recently been shown to bind chromatin and influence the DNA damage response as well as function in the presynaptic space, modulating action potential duration. We report here the amino terminal crystal structures of wild-type FMRP, and a mutant (R138Q) that disrupts the amino terminus function, containing an integral tandem Agenet and discover a novel KH motif.
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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.