Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Short-interfering-RNA-mediated gene silencing in mammalian cells requires Dicer and eIF2C translation initiation factors.
Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs.
Identification of novel argonaute-associated proteins.
Translation repression in human cells by microRNA-induced gene silencing requires RCK/p54.
A conserved motif in Argonaute-interacting proteins mediates functional interactions through the Argonaute PIWI domain.
Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells.
Protein microarray analysis identifies human cellular prion protein interactors.
Importance of translation and nonnucleolytic ago proteins for on-target RNA interference.
Importin 8 is a gene silencing factor that targets argonaute proteins to distinct mRNAs.
The C-terminal half of human Ago2 binds to multiple GW-rich regions of GW182 and requires GW182 to mediate silencing.
The C-terminal domains of human TNRC6A, TNRC6B, and TNRC6C silence bound transcripts independently of Argonaute proteins.
Mammalian miRNA RISC recruits CAF1 and PABP to affect PABP-dependent deadenylation.
ATP-dependent human RISC assembly pathways.
Mouse ZAR1-like (XM_359149) colocalizes with mRNA processing components and its dominant-negative mutant caused two-cell-stage embryonic arrest.
LIM-domain proteins, LIMD1, Ajuba, and WTIP are required for microRNA-mediated gene silencing.
Human prion protein binds Argonaute and promotes accumulation of microRNA effector complexes.
The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.
Slicing-independent RISC activation requires the argonaute PAZ domain.
HIV-1 replication and APOBEC3 antiviral activity are not regulated by P bodies.
Hypoxia-responsive miRNAs target argonaute 1 to promote angiogenesis.
Eukaryote-specific insertion elements control human ARGONAUTE slicer activity.
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.
Cellular microRNAs up-regulate transcription via interaction with promoter TATA-box motifs.
Systematic Analysis of Human Protein Phosphatase Interactions and Dynamics.
Argonaute Utilization for miRNA Silencing Is Determined by Phosphorylation-Dependent Recruitment of LIM-Domain-Containing Proteins.
Multivalent Recruitment of Human Argonaute by GW182.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Spatial centrosome proteome of human neural cells uncovers disease-relevant heterogeneity.
Multimodal cell maps as a foundation for structural and functional genomics.
MIR449 microRNAs bind 3'UTR of NOTCH1 mRNA
MIR34 microRNAs bind 3'UTR of NOTCH1 mRNA
MIR150 microRNA binds 3'UTR of NOTCH3 mRNA
MIR200B/C microRNAs bind NOTCH1 mRNA
MIR181C microRNA binds 3'UTR of NOTCH4 mRNA
MIR206 microRNA binds 3'UTR of NOTCH3 mRNA
MIR34 microRNAs bind 3'UTR of NOTCH2 mRNA
MIR302A microRNA binds 3'UTR of NOTCH4 mRNA
p53 positively regulates transcription of MIR34 microRNAs
miR-26A microRNAs bind PTEN mRNA
miR-24 binds p16INK4A and p14ARF mRNAs
RISC binds inexactly matching target RNAs
Nonendonucleolytic RISC binds exactly matching target RNAs
miR-92b binds 3'UTR of NLK mRNA
AGO1,2:small RNA complexes interact with chromatin
FOXO3 regulates MIR34B,C expression
MIR27A gene transcription is stimulated by the complex containing RUNX1, PRMT1 and GATA1 and inhibited by the complex of RUNX1, SIN3A and PRMT6
miR-106a binds RUNX1 mRNA
miR-214 microRNA binds PTEN mRNA
miR-205 microRNA binds PTEN mRNA
miR-21 nonendonucleolytic RISC binds PTEN mRNA
miR-26A and B bind to the 3'UTR of the GREB1 mRNA
miR-26A and B bind to the 3'UTR of the CHD11 mRNA
miR-26A and B bind to the 3'UTR of the KPNA2 mRNA
miR-613 binds to the 3'UTR of the NR1H3 mRNA
miR-26 binds to the 3'UTR of the ARL4C mRNA
miR-26 binds to the 3'UTR of the ABCA1 mRNA
miR-33 binds to the 3'UTR of the ABCA1 mRNA
miR-144 binds to the 3'UTR of the ABCA1 mRNA
MITF-M-dependent miR-211 expression
miR-211 RISC binds POU3F2 mRNA
CD274 mRNA binds miR-34 RISC
CD274 mRNA binds miR-340 RISC
CD274 mRNA binds miR-152 RISC
CD274 mRNA binds miR-140 RISC
CD274 mRNA binds miR-200B/C RISC
UniProt text export for AGO1
Falcon deep research report for AGO1
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Falcon research supports the reviewed core function of AGO1.
"Human **AGO1 (EIF2C1; UniProt Q9UL18)** is a **non-slicer Argonaute** that functions as a core miRISC effector mediating **miRNA-guided repression and mRNA decay** through recruitment of **TNRC6/GW182** and downstream **deadenylation/decapping** pathways."
Let-7a-regulated translational readthrough of mammalian AGO1 generates a microRNA pathway inhibitor.
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Original report of AGO1x - a C-terminally extended AGO1 proteoform said to arise from let-7a-promoted stop codon readthrough, to load miRNAs without silencing them because it cannot bind GW182, and thus to act as a competitive inhibitor of the miRNA pathway.
"Ago1x can load miRNAs on target mRNAs without causing post-transcriptional gene silencing, due to its inability to interact with GW182"
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Evidence beyond the contested reporter assay: ribosome profiling, mass spectrometry and a proteoform-specific antibody.
"Analysis of ribosome profiling data and mass spectrometry data provided additional evidence for translational readthrough of AGO1."
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Endogenous detection of the readthrough product is claimed with a specific antibody.
"The endogenous readthrough product, Ago1x, could be detected by a specific antibody both in vitro and in vivo."
Prevention of dsRNA-induced interferon signaling by AGO1x is linked to breast cancer cell proliferation.
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Independent laboratory (Zavolan) reporting AGO1x in breast cancer cells, with a function distinct from canonical AGO1 - limiting dsRNA accumulation and interferon induction - and a nuclear, perinucleolar localization unlike cytoplasmic AGO1.
"AGO1x, an evolutionarily conserved translational readthrough isoform of Argonaute 1, is generated in highly proliferative breast cancer cells"
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The reported AGO1x localization is nuclear, which matters because generic nuclear annotations on AGO1 should not be quietly justified by a disputed proteoform.
"AGO1x exhibits nuclear localization in the vicinity of nucleoli"
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Specificity of the AGO1x-detecting antibody was tested against FLAG-AGO1 and FLAG-AGO1x stable lines - evidence for the proteoform that does not depend on a luciferase reporter.
"These experiments again demonstrated that the AGO1x antibody is highly specific for AGO1x"
Transcript-specific induction of stop codon readthrough using a CRISPR-dCas13 system.
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Uses the AGO1 stop codon as a known natural readthrough site when demonstrating dCas13-induced readthrough; its AGO1 readthrough measurements are the second target of the 2025 critique.
"we target dCas13 to the region downstream of canonical stop codons of mammalian AGO1 and VEGFA mRNAs, known to exhibit natural SCR"
The dual luciferase assay does not support claims of stop codon readthrough on the AGO1 mRNA.
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Direct methodological challenge to the AGO1 readthrough claim: using an insulated StopGo/2A single-mRNA dual-luciferase system, no meaningful readthrough at the AGO1 stop codon was detected, while the positive control AQP4 behaved as expected.
"we could not detect readthrough activity above 0.1%"
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In the tested reporter designs, apparent readthrough fell after removing the AGO1 fusion; the authors interpret this as a reporter artefact. The design and interpretation are contested in PMID:40500329.
"when we tested the unfused AGO1-SG-F-luc constructs, apparent readthrough almost disappeared"
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The authors attribute the published ~20% figure to an impaired sense-codon control combined with reporter-independent background activity.
"resulted in an overestimation of AGO1 readthrough"
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The authors framed the reported efficiency as exceptionally high; their highest-known-human-readthrough statement is disputed by the response PMID:40500329 and is not adopted as an established fact.
"As far as we know, this is the highest reported readthrough efficiency observed for any human mRNA."
Response to Suresh et al.
Upregulation of Cyclin B1 by miRNA and its implications in cancer.
Argonaute proteins in cardiac tissue contribute to the heart injury during viral myocarditis.
Modeling neurodevelopmental disorder-associated hAGO1 mutations in C. elegans Argonaute ALG-1.
Modeling neurodevelopmental disorder-associated human AGO1 mutations in Caenorhabditis elegans Argonaute alg-1.
Novel de Novo Nonsense Variants in AGO3 and KHSRP: Insights into Global Developmental Delay and Autism Spectrum Disorders through Whole Genome Analysis.
MicroRNA and Rare Human Diseases.
Partners in Silencing: Decoding the Mammalian Argonaute Interactome.
The Life of MicroRNAs: Biogenesis, Function and Decay in Cancer.