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RNA-binding protein

About: RNA-binding protein is a(n) research topic. Over the lifetime, 11184 publication(s) have been published within this topic receiving 703109 citation(s). The topic is also known as: RNA-binding protein. more


Journal ArticleDOI: 10.1038/NATURE03120
11 Nov 2004-Nature
Abstract: MicroRNAs (miRNAs) are a growing family of small non-protein-coding regulatory genes that regulate the expression of homologous target-gene transcripts. They have been implicated in the control of cell death and proliferation in flies, haematopoietic lineage differentiation in mammals, neuronal patterning in nematodes and leaf and flower development in plants. miRNAs are processed by the RNA-mediated interference machinery. Drosha is an RNase III enzyme that was recently implicated in miRNA processing. Here we show that human Drosha is a component of two multi-protein complexes. The larger complex contains multiple classes of RNA-associated proteins including RNA helicases, proteins that bind double-stranded RNA, novel heterogeneous nuclear ribonucleoproteins and the Ewing's sarcoma family of proteins. The smaller complex is composed of Drosha and the double-stranded-RNA-binding protein, DGCR8, the product of a gene deleted in DiGeorge syndrome. In vivo knock-down and in vitro reconstitution studies revealed that both components of this smaller complex, termed Microprocessor, are necessary and sufficient in mediating the genesis of miRNAs from the primary miRNA transcript. more

Topics: Microprocessor complex (68%), Drosha (67%), DGCR8 (66%) more

2,567 Citations

Open accessJournal ArticleDOI: 10.1016/J.CELL.2010.03.009
Markus Hafner1, Markus Landthaler1, Lukas Burger2, Mohsen Khorshid2  +11 moreInstitutions (3)
02 Apr 2010-Cell
Abstract: RNA transcripts are subject to posttranscriptional gene regulation involving hundreds of RNA-binding proteins (RBPs) and microRNA-containing ribonucleoprotein complexes (miRNPs) expressed in a cell-type dependent fashion. We developed a cell-based crosslinking approach to determine at high resolution and transcriptome-wide the binding sites of cellular RBPs and miRNPs. The crosslinked sites are revealed by thymidine to cytidine transitions in the cDNAs prepared from immunopurified RNPs of 4-thiouridine-treated cells. We determined the binding sites and regulatory consequences for several intensely studied RBPs and miRNPs, including PUM2, QKI, IGF2BP1-3, AGO/EIF2C1-4 and TNRC6A-C. Our study revealed that these factors bind thousands of sites containing defined sequence motifs and have distinct preferences for exonic versus intronic or coding versus untranslated transcript regions. The precise mapping of binding sites across the transcriptome will be critical to the interpretation of the rapidly emerging data on genetic variation between individuals and how these variations contribute to complex genetic diseases. more

Topics: RNA-binding protein (63%), Ribonomics (59%), PAR-CLIP (58%) more

2,499 Citations

Journal ArticleDOI: 10.1126/SCIENCE.8036511
Christopher G. Burd1, Gideon Dreyfuss1Institutions (1)
29 Jul 1994-Science
Abstract: In eukaryotic cells, a multitude of RNA-binding proteins play key roles in the posttranscriptional regulation of gene expression. Characterization of these proteins has led to the identification of several RNA-binding motifs, and recent experiments have begun to illustrate how several of them bind RNA. The significance of these interactions is reflected in the recent discoveries that several human and other vertebrate genetic disorders are caused by aberrant expression of RNA-binding proteins. The major RNA-binding motifs are described and examples of how they may function are given. more

Topics: RNA Recognition Motif Proteins (60%), RNA-binding protein (57%), RNA (54%) more

1,851 Citations

Open accessJournal ArticleDOI: 10.1038/NBT.3300
Abstract: The binding specificities of RNA- and DNA-binding proteins are determined from experimental data using a ‘deep learning’ approach. more

Topics: RNA (57%), RNA-binding protein (54%), DNA (53%) more

1,832 Citations

Open accessJournal ArticleDOI: 10.1038/NATURE12730
Xiao Wang1, Zhike Lu1, Adrian Gomez1, Gary C. Hon2  +9 moreInstitutions (2)
02 Jan 2014-Nature
Abstract: N(6)-methyladenosine (m(6)A) is the most prevalent internal (non-cap) modification present in the messenger RNA of all higher eukaryotes. Although essential to cell viability and development, the exact role of m(6)A modification remains to be determined. The recent discovery of two m(6)A demethylases in mammalian cells highlighted the importance of m(6)A in basic biological functions and disease. Here we show that m(6)A is selectively recognized by the human YTH domain family 2 (YTHDF2) 'reader' protein to regulate mRNA degradation. We identified over 3,000 cellular RNA targets of YTHDF2, most of which are mRNAs, but which also include non-coding RNAs, with a conserved core motif of G(m(6)A)C. We further establish the role of YTHDF2 in RNA metabolism, showing that binding of YTHDF2 results in the localization of bound mRNA from the translatable pool to mRNA decay sites, such as processing bodies. The carboxy-terminal domain of YTHDF2 selectively binds to m(6)A-containing mRNA, whereas the amino-terminal domain is responsible for the localization of the YTHDF2-mRNA complex to cellular RNA decay sites. Our results indicate that the dynamic m(6)A modification is recognized by selectively binding proteins to affect the translation status and lifetime of mRNA. more

Topics: MRNA modification (64%), RNA-binding protein (62%), RNA (62%) more

1,755 Citations

No. of papers in the topic in previous years

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Topic's top 5 most impactful authors

Myriam Gorospe

69 papers, 4.6K citations

Gene W. Yeo

42 papers, 4K citations

Jack D. Keene

40 papers, 6.5K citations

Gideon Dreyfuss

29 papers, 10.3K citations

Marvin Wickens

29 papers, 2.8K citations

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