On the public citation graph

PRMT1-mediated methylation of the Large Drosha Complex regulates microRNA biogenesis

0 signed · 101 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

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).

Dataset join, best-effort; this page does not check the publisher record. Retraction Watch data via Crossref Labs, used with credit; OpenCitations Index (CC0) and Meta (CC BY 4.0); dataset doi:10.7910/DVN/WT8VOA (CC BY 4.0).

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/0471250953.bi1315s35openalex-snapshot
Biological Sequence Motif Discovery Using motif‐x
inferredcites →https://doi.org/10.1002/ijc.25366openalex-snapshot
Dysregulation of PRMT1 and PRMT6, Type I arginine methyltransferases, is involved in various types of human cancers
inferredcites →https://doi.org/10.1002/jor.20884openalex-snapshot
Hip resurfacing increases bone strains associated with short‐term femoral neck fracture
inferredcites →https://doi.org/10.1002/mrd.22024openalex-snapshot
Arginine methylation of RNA‐binding proteins regulates cell function and differentiation
inferredcites →https://doi.org/10.1007/s10930-009-9174-3openalex-snapshot
Proteomic Analysis of Methylarginine-Containing Proteins in HeLa Cells by Two-Dimensional Gel Electrophoresis and Immunoblotting with a Methylarginine-Specific Antibody
inferredcites →https://doi.org/10.1007/s12035-013-8564-xopenalex-snapshot
TDP-43 Regulates the Microprocessor Complex Activity During In Vitro Neuronal Differentiation
inferredcites →https://doi.org/10.1016/j.bbrc.2003.09.070openalex-snapshot
A novel RNA splicing-mediated gene silencing mechanism potential for genome evolution
inferredcites →https://doi.org/10.1016/j.bbrc.2005.02.018openalex-snapshot
Transcriptional down-regulation through nuclear exclusion of EWS methylated by PRMT1
inferredcites →https://doi.org/10.1016/j.cell.2006.03.043openalex-snapshot
Molecular Basis for the Recognition of Primary microRNAs by the Drosha-DGCR8 Complex
inferredcites →https://doi.org/10.1016/j.cell.2008.10.053openalex-snapshot
Posttranscriptional Crossregulation between Drosha and DGCR8
inferredcites →https://doi.org/10.1016/j.cell.2012.04.017openalex-snapshot
Cell-free Formation of RNA Granules: Low Complexity Sequence Domains Form Dynamic Fibers within Hydrogels
inferredcites →https://doi.org/10.1016/j.cell.2013.01.031openalex-snapshot
Beyond Secondary Structure: Primary-Sequence Determinants License Pri-miRNA Hairpins for Processing
inferredcites →https://doi.org/10.1016/j.celrep.2013.10.017openalex-snapshot
Phosphorylation of DGCR8 Increases Its Intracellular Stability and Induces a Progrowth miRNA Profile
inferredcites →https://doi.org/10.1016/j.gpb.2012.07.005openalex-snapshot
MicroRNAs in Common Human Diseases
inferredcites →https://doi.org/10.1016/j.jmb.2018.06.014openalex-snapshot
RGG/RG Motif Regions in RNA Binding and Phase Separation
inferredcites →https://doi.org/10.1016/j.molcel.2005.04.003openalex-snapshot
Arginine Methylation
inferredcites →https://doi.org/10.1016/j.molcel.2008.12.013openalex-snapshot
Protein Arginine Methylation in Mammals: Who, What, and Why
inferredcites →https://doi.org/10.1016/j.molcel.2010.03.013openalex-snapshot
Posttranscriptional Regulation of MicroRNA Biogenesis in Animals
inferredcites →https://doi.org/10.1016/j.molcel.2013.05.021openalex-snapshot
Defining the RGG/RG Motif
inferredcites →https://doi.org/10.1016/j.molcel.2015.01.004openalex-snapshot
Stress Induces p38 MAPK-Mediated Phosphorylation and Inhibition of Drosha-Dependent Cell Survival
inferredcites →https://doi.org/10.1016/j.molcel.2018.02.012openalex-snapshot
Systematic Discovery of RNA Binding Proteins that Regulate MicroRNA Levels
inferredcites →https://doi.org/10.1016/j.tibs.2015.08.012openalex-snapshot
Emerging Roles of Disordered Sequences in RNA-Binding Proteins
inferredcites →https://doi.org/10.1016/j.yexcr.2007.07.020openalex-snapshot
Nucleolar localization of DGCR8 and identification of eleven DGCR8-associated proteins
inferredcites →https://doi.org/10.1016/j.yexcr.2008.12.008openalex-snapshot
PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function
inferredcites →https://doi.org/10.1016/s0167-4889(02)00202-1openalex-snapshot
Identification of methylated proteins by protein arginine N-methyltransferase 1, PRMT1, with a new expression cloning strategy
inferredcites →https://doi.org/10.1016/s0960-9822(01)00294-9openalex-snapshot
Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1
inferredcites →https://doi.org/10.1016/s0969-2126(01)00685-2openalex-snapshot
Crystallographic and Modeling Studies of RNase III Suggest a Mechanism for Double-Stranded RNA Cleavage
inferredcites →https://doi.org/10.1016/s1097-2765(03)00101-1openalex-snapshot
Methylation of SPT5 Regulates Its Interaction with RNA Polymerase II and Transcriptional Elongation Properties
inferredcites →https://doi.org/10.1021/acschembio.5b00839openalex-snapshot
A Potent, Selective, and Cell-Active Inhibitor of Human Type I Protein Arginine Methyltransferases
inferredcites →https://doi.org/10.1021/pr101065jopenalex-snapshot
Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
inferredcites →https://doi.org/10.1038/cdd.2014.87openalex-snapshot
Role of miR-15/16 in CLL
inferredcites →https://doi.org/10.1038/leu.2013.246openalex-snapshot
Defective DROSHA processing contributes to downregulation of MiR-15/-16 in chronic lymphocytic leukemia
inferredcites →https://doi.org/10.1038/nature02871openalex-snapshot
The functions of animal microRNAs
inferredcites →https://doi.org/10.1038/nature03049openalex-snapshot
Processing of primary microRNAs by the Microprocessor complex
inferredcites →https://doi.org/10.1038/nature03120openalex-snapshot
The Microprocessor complex mediates the genesis of microRNAs
inferredcites →https://doi.org/10.1038/nature03702openalex-snapshot
MicroRNA expression profiles classify human cancers
inferredcites →https://doi.org/10.1038/nature03868openalex-snapshot
TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing
inferredcites →https://doi.org/10.1038/nature10198openalex-snapshot
Dicer recognizes the 5′ end of RNA for efficient and accurate processing
inferredcites →https://doi.org/10.1038/nbt.1511openalex-snapshot
MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
inferredcites →https://doi.org/10.1038/ncb1577openalex-snapshot
DEAD-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-snapshot
Comprehensive identification of arginine methylation in primary T cells reveals regulatory roles in cell signalling
inferredcites →https://doi.org/10.1038/nmeth715openalex-snapshot
Identifying and quantifying in vivo methylation sites by heavy methyl SILAC
inferredcites →https://doi.org/10.1038/nprot.2006.468openalex-snapshot
In-gel digestion for mass spectrometric characterization of proteins and proteomes
inferredcites →https://doi.org/10.1038/nprot.2007.261openalex-snapshot
Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
inferredcites →https://doi.org/10.1038/nrc3409openalex-snapshot
Protein arginine methyltransferases and cancer
inferredcites →https://doi.org/10.1038/nrc3932openalex-snapshot
MicroRNA biogenesis pathways in cancer
inferredcites →https://doi.org/10.1038/nsmb1250openalex-snapshot
The multifunctional RNA-binding protein hnRNP A1 is required for processing of miR-18a
inferredcites →https://doi.org/10.1038/sj.emboj.7600491openalex-snapshot
Recognition and cleavage of primary microRNA precursors by the nuclear processing enzyme Drosha
inferredcites →https://doi.org/10.1038/srep01311openalex-snapshot
Loss of the major Type I arginine methyltransferase PRMT1 causes substrate scavenging by other PRMTs
inferredcites →https://doi.org/10.1039/c3mb00009eopenalex-snapshot
Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome
inferredcites →https://doi.org/10.1042/bj20130545openalex-snapshot
Promiscuity as a functional trait: intrinsically disordered regions as central players of interactomes
inferredcites →https://doi.org/10.1042/bj3040903openalex-snapshot
Effect of enzymic methylation of heterogeneous ribonucleoprotein particle A1 on its nucleic-acid binding and controlled proteolysis
inferredcites →https://doi.org/10.1056/nejmoa050995openalex-snapshot
A MicroRNA Signature Associated with Prognosis and Progression in Chronic Lymphocytic Leukemia
inferredcites →https://doi.org/10.1073/pnas.1112427109openalex-snapshot
TDP-43 promotes microRNA biogenesis as a component of the Drosha and Dicer complexes
inferredcites →https://doi.org/10.1073/pnas.1311639110openalex-snapshot
Lower and upper stem–single-stranded RNA junctions together determine the Drosha cleavage site
inferredcites →https://doi.org/10.1074/jbc.275.11.7723openalex-snapshot
PRMT1 Is the Predominant Type I Protein Arginine Methyltransferase in Mammalian Cells
inferredcites →https://doi.org/10.1074/jbc.m011446200openalex-snapshot
Exposure on Cell Surface and Extensive Arginine Methylation of Ewing Sarcoma (EWS) Protein
inferredcites →https://doi.org/10.1074/jbc.m105161200openalex-snapshot
Dual 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.m111.265439openalex-snapshot
Nucleolin Protein Interacts with Microprocessor Complex to Affect Biogenesis of MicroRNAs 15a and 16
inferredcites →https://doi.org/10.1074/jbc.m116.748210openalex-snapshot
Suppression 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.m111.011932openalex-snapshot
RNA Helicase DDX5 Regulates MicroRNA Expression and Contributes to Cytoskeletal Reorganization in Basal Breast Cancer Cells
inferredcites →https://doi.org/10.1074/mcp.m115.055384openalex-snapshot
Large Scale Mass Spectrometry-based Identifications of Enzyme-mediated Protein Methylation Are Subject to High False Discovery Rates
inferredcites →https://doi.org/10.1074/mcp.o113.027870openalex-snapshot
Immunoaffinity Enrichment and Mass Spectrometry Analysis of Protein Methylation
inferredcites →https://doi.org/10.1074/mcp.o113.032748openalex-snapshot
Proteomic Analysis of Arginine Methylation Sites in Human Cells Reveals Dynamic Regulation During Transcriptional Arrest
inferredcites →https://doi.org/10.1093/database/bau099openalex-snapshot
miRIAD—integrating microRNA inter- and intragenic data
inferredcites →https://doi.org/10.1093/hmg/ddi429openalex-snapshot
Identification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp
inferredcites →https://doi.org/10.1093/hmg/ddr448openalex-snapshot
Arginine methylation by PRMT1 regulates nuclear-cytoplasmic localization and toxicity of FUS/TLS harbouring ALS-linked mutations
inferredcites →https://doi.org/10.1093/nar/gkv1145openalex-snapshot
2016 update of the PRIDE database and its related tools
inferredcites →https://doi.org/10.1093/nar/gkw880openalex-snapshot
2016 update of the PRIDE database and its related tools
inferredcites →https://doi.org/10.1093/nar/gkx460openalex-snapshot
Intrinsically disordered RGG/RG domains mediate degenerate specificity in RNA binding
inferredcites →https://doi.org/10.1093/nar/gkx922openalex-snapshot
20 years of the SMART protein domain annotation resource
inferredcites →https://doi.org/10.1101/gad.1158803openalex-snapshot
Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs
inferredcites →https://doi.org/10.1101/gad.1201404openalex-snapshot
The action of ARGONAUTE1 in the miRNA pathway and its regulation by the miRNA pathway are crucial for plant development
inferredcites →https://doi.org/10.1101/gad.1262504openalex-snapshot
The Drosha-DGCR8 complex in primary microRNA processing
inferredcites →https://doi.org/10.1101/gad.1279805openalex-snapshot
Arginine methylation of MRE11 by PRMT1 is required for DNA damage checkpoint control
inferredcites →https://doi.org/10.1101/gad.1444406openalex-snapshot
Extensive post-transcriptional regulation of microRNAs and its implications for cancer
inferredcites →https://doi.org/10.1101/gad.1632608openalex-snapshot
Methylation of RUNX1 by PRMT1 abrogates SIN3A binding and potentiates its transcriptional activity
inferredcites →https://doi.org/10.1101/gad.1919710openalex-snapshot
Emerging paradigms of regulated microRNA processing
inferredcites →https://doi.org/10.1126/science.1060781openalex-snapshot
Methylation of Histone H4 at Arginine 3 Facilitating Transcriptional Activation by Nuclear Hormone Receptor
inferredcites →https://doi.org/10.1126/science.1090599openalex-snapshot
Nuclear Export of MicroRNA Precursors
inferredcites →https://doi.org/10.1126/scisignal.aaf7329openalex-snapshot
Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells
inferredcites →https://doi.org/10.1128/mcb.00042-09openalex-snapshot
A Mouse PRMT1 Null Allele Defines an Essential Role for Arginine Methylation in Genome Maintenance and Cell Proliferation
inferredcites →https://doi.org/10.1128/mcb.01836-08openalex-snapshot
The NF90-NF45 Complex Functions as a Negative Regulator in the MicroRNA Processing Pathway
inferredcites →https://doi.org/10.1128/mcb.02025-07openalex-snapshot
A Glycine-Arginine Domain in Control of the Human MRE11 DNA Repair Protein
inferredcites →https://doi.org/10.1155/jbb/2006/26818openalex-snapshot
Intronic MicroRNA (miRNA)
inferredcites →https://doi.org/10.1158/0008-5472.can-05-0298openalex-snapshot
MicroRNA Biogenesis and Cancer
inferredcites →https://doi.org/10.1158/0008-5472.can-18-1995openalex-snapshot
Mouse Models of Overexpression Reveal Distinct Oncogenic Roles for Different Type I Protein Arginine Methyltransferases
inferredcites →https://doi.org/10.1186/1478-811x-7-18openalex-snapshot
Regulation of MicroRNA Biogenesis: A miRiad of mechanisms
inferredcites →https://doi.org/10.1186/1756-8935-7-38openalex-snapshot
Genome-wide analysis of H3.3 dissociation reveals high nucleosome turnover at distal regulatory regions of embryonic stem cells
inferredcites →https://doi.org/10.1261/rna.5167604openalex-snapshot
Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs
inferredcites →https://doi.org/10.1371/journal.pone.0002518openalex-snapshot
Suppression of Tumor Growth and Angiogenesis by a Specific Antagonist of the Cell-Surface Expressed Nucleolin
inferredcites →https://doi.org/10.1371/journal.pone.0011379openalex-snapshot
Methylation of the Tumor Suppressor Protein, BRCA1, Influences Its Transcriptional Cofactor Function
inferredcites →https://doi.org/10.1371/journal.pone.0038658openalex-snapshot
Coaggregation 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/10.1371/journal.pone.0061576openalex-snapshot
Protein Arginine Methyltransferase 1 and 8 Interact with FUS to Modify Its Sub-Cellular Distribution and Toxicity In Vitro and In Vivo
inferredcites →https://doi.org/10.1371/journal.pone.0072503openalex-snapshot
Acetylation of Drosha on the N-Terminus Inhibits Its Degradation by Ubiquitination
inferredcites →https://doi.org/10.4161/cc.22871openalex-snapshot
Alternatively spliced protein arginine methyltransferase 1 isoform PRMT1v2 promotes the survival and invasiveness of breast cancer cells
inferredcites →https://doi.org/10.4161/cc.4.12.2250openalex-snapshot
The GAR Motif of 53BP1 is Arginine Methylated by PRMT1 and is Necessary for 53BP1 DNA Binding Activity
inferredcites →https://doi.org/10.7554/elife.00822openalex-snapshot
A component of the mir-17-92 polycistronic oncomir promotes oncogene-dependent apoptosis

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1080/15384101.2019.1629791openalex-snapshot
PRMTs and miRNAs: functional cooperation in cancer and beyond
inferred← citeshttps://doi.org/10.2174/0118715265304580240405064250openalex-snapshot
Vitamin D and Mitochondrial Activity Preservation in COVID-19
inferred← citeshttps://doi.org/10.7554/elife.74940openalex-snapshot
SAFB regulates hippocampal stem cell fate by targeting Drosha to destabilize Nfib mRNA
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.