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PRMT1-mediated methylation of the Large Drosha Complex regulates microRNA biogenesis
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1 of the 98 references listed on this page is in the Retraction Watch database as retracted (export 2026-11-04): 10.1038/ncb1577 (notice 2014-10-31).
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dataset doi:10.7910/DVN/WT8VOA (CC BY 4.0).
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/ijc.25366openalex-snapshotDysregulation of PRMT1 and PRMT6, Type I arginine methyltransferases, is involved in various types of human cancers
inferredcites →https://doi.org/10.1007/s10930-009-9174-3openalex-snapshotProteomic Analysis of Methylarginine-Containing Proteins in HeLa Cells by Two-Dimensional Gel Electrophoresis and Immunoblotting with a Methylarginine-Specific Antibody
inferredcites →https://doi.org/10.1038/nbt.1511openalex-snapshotMaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
inferredcites →https://doi.org/10.1038/ncb1577openalex-snapshotDEAD-box RNA helicase subunits of the Drosha complex are required for processing of rRNA and a subset of microRNAs
inferredcites →https://doi.org/10.1038/ncomms7758openalex-snapshotComprehensive identification of arginine methylation in primary T cells reveals regulatory roles in cell signalling
inferredcites →https://doi.org/10.1038/srep01311openalex-snapshotLoss of the major Type I arginine methyltransferase PRMT1 causes substrate scavenging by other PRMTs
inferredcites →https://doi.org/10.1039/c3mb00009eopenalex-snapshotMass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome
inferredcites →https://doi.org/10.1042/bj3040903openalex-snapshotEffect of enzymic methylation of heterogeneous ribonucleoprotein particle A1 on its nucleic-acid binding and controlled proteolysis
inferredcites →https://doi.org/10.1074/jbc.m105161200openalex-snapshotDual Mechanisms for Repression of the Monomeric Orphan Receptor Liver Receptor Homologous Protein-1 by the Orphan Small Heterodimer Partner
inferredcites →https://doi.org/10.1074/jbc.m116.748210openalex-snapshotSuppression of MicroRNA-7 (miR-7) Biogenesis by Nuclear Factor 90-Nuclear Factor 45 Complex (NF90-NF45) Controls Cell Proliferation in Hepatocellular Carcinoma
inferredcites →https://doi.org/10.1074/mcp.m115.055384openalex-snapshotLarge Scale Mass Spectrometry-based Identifications of Enzyme-mediated Protein Methylation Are Subject to High False Discovery Rates
inferredcites →https://doi.org/10.1093/hmg/ddi429openalex-snapshotIdentification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp
inferredcites →https://doi.org/10.1093/hmg/ddr448openalex-snapshotArginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
inferredcites →https://doi.org/10.1101/gad.1201404openalex-snapshotThe action of ARGONAUTE1 in the miRNA pathway and its regulation by the miRNA pathway are crucial for plant development
inferredcites →https://doi.org/10.1128/mcb.00042-09openalex-snapshotA Mouse PRMT1 Null Allele Defines an Essential Role for Arginine Methylation in Genome Maintenance and Cell Proliferation
inferredcites →https://doi.org/10.1186/1756-8935-7-38openalex-snapshotGenome-wide analysis of H3.3 dissociation reveals high nucleosome turnover at distal regulatory regions of embryonic stem cells
inferredcites →https://doi.org/10.1371/journal.pone.0038658openalex-snapshotCoaggregation of RNA-Binding Proteins in a Model of TDP-43 Proteinopathy with Selective RGG Motif Methylation and a Role for RRM1 Ubiquitination
inferredcites →https://doi.org/10.4161/cc.22871openalex-snapshotAlternatively spliced protein arginine methyltransferase 1 isoform PRMT1v2 promotes the survival and invasiveness of breast cancer cells
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