ArticleRNA (New York, N.Y.)1998
Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP A1.
Article in RNA (New York, N.Y.), 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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.
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Who cites it
31 citing papers in PubMed, 49 citations in OpenAlex.
- hnRNPH1 Inhibits Influenza Virus Replication by Binding Viral RNA.Microorganisms · 2024Article
- Mechanistic Insights into Alternative Gene Splicing in Oxidative Stress and Tissue Injury.Antioxidants & redox signaling · 2024Review
- Phase Separation of Heterogeneous Nuclear Ribonucleoprotein A1 upon Specific RNA-Binding Observed by Magnetic Resonance.Angewandte Chemie (International ed. in English) · 2022Article
- hnRNP A/B Proteins: An Encyclopedic Assessment of Their Roles in Homeostasis and Disease.Biology · 2021Review
- A Comprehensive Analysis of the Role of hnRNP A1 Function and Dysfunction in the Pathogenesis of Neurodegenerative Disease.Frontiers in molecular biosciences · 2021Review
- Structural basis for terminal loop recognition and stimulation of pri-miRNA-18a processing by hnRNP A1.Nature communications · 2018Article
- Interferon regulatory factor 1 and a variant of heterogeneous nuclear ribonucleoprotein L coordinately silence the gene for adhesion protein CEACAM1.The Journal of biological chemistry · 2018Article
- Article
- The First Crystal Structure of the UP1 Domain of hnRNP A1 Bound to RNA Reveals a New Look for an Old RNA Binding Protein.Journal of molecular biology · 2015Article
- A truncated hnRNP A1 isoform, lacking the RGG-box RNA binding domain, can efficiently regulate HIV-1 splicing and replication.Biochimica et biophysica acta · 2014Article
- Norovirus genome circularization and efficient replication are facilitated by binding of PCBP2 and hnRNP A1.Journal of virology · 2013Article
- hnRNP A1: the Swiss army knife of gene expression.International journal of molecular sciences · 2013Review
- High-affinity interaction of hnRNP A1 with conserved RNA structural elements is required for translation and replication of enterovirus 71.RNA biology · 2013Article
- Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology.Journal of biomolecular NMR · 2013Article
- Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms.RNA (New York, N.Y.) · 2013Article
- The hnRNP A1 homolog Hrp36 is essential for normal development, female fecundity, omega speckle formation and stress tolerance in Drosophila melanogaster.Journal of biosciences · 2012Article
- hnRNP H and hnRNP F complex with Fox2 to silence fibroblast growth factor receptor 2 exon IIIc.Molecular and cellular biology · 2008Article
- In-vitro dual binding activity of a evolutionarily related subgroup of hnRNP proteins.Molecular and cellular biochemistry · 2005Article
- Molecular phylogenetics and functional evolution of major RNA recognition domains of recently cloned and characterized autoimmune RNA-binding particle.Genomics, proteomics & bioinformatics · 2003Article
- hnRNP A1 controls HIV-1 mRNA splicing through cooperative binding to intron and exon splicing silencers in the context of a conserved secondary structure.RNA (New York, N.Y.) · 2002Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
hnRNP A1 regulates alternative splicing by antagonizing SR proteins. It consists of two closely related, tandem RNA-recognition motifs (RRMs), followed by a glycine-rich domain. Analysis of variant proteins with duplications, deletions, or swaps of the RRMs showed that although both RRMs are required for alternative splicing function, each RRM plays distinct roles, and their relative position is important. Surprisingly, RRM2 but not RRM1 could support this function when duplicated, despite their very similar structure. Specific RNA binding and annealing are not sufficient for hnRNP A1 alternative splicing function. These observations, together with phylogenetic and structural data, suggest that the two RRMs are quasi-symmetric but functionally nonequivalent modules that evolved as components of a single bipartite domain.
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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.