Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs.
By Gunter Meister, Markus Landthaler, Agnieszka Patkaniowska, Yair Dorsett, G. Teng, Thomas Tuschl. Molecules and Cells, 2004
2,092 citations recorded by the source corpus.
Subfields: Cancer Research, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e51a044e7a6915d570c748d206b213b482bd0dda
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In Cancer Research
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In Molecular Biology
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Citations in the corpus
- Human RISC couples microRNA biogenesis and posttranscriptional gene silencing. (2005, background): “However, Argonaute2 (Ago2) was recently found to be the catalytic endonuclease of human RISC, and, accordingly, structural studies identified the PIWI domain as the catalytic center that resembles that of RNase H (Liu et al., 2004, Meister et al., 2004, Song et al., 2004; Ma et al., 2005).”
- Analysis of the C. elegans Argonaute family reveals that distinct Argonautes act sequentially during RNAi. (2006, neutral): “The secondary AGO proteins lack key metal-coordinating residues in their RNase H-related PIWI domains, perhaps explaining why siRISC-mediated cleavage activity has not been detected to date in C. elegans.”
- Genome-wide identification and analysis of drought-responsive microRNAs in Oryza sativa. (2010, background): “Micro RNAs (miRNAs) are a class of non-protein-coding, single-strand molecules of 20–27 nucleotides in length, that have been reported to regulate gene expression at the posttranscriptional level in plants, animals, nematodes, and fungi (Bartel, 2004; Denli et al., 2004; Dugas and Bartel, 2004; Meis”
- Metazoan MicroRNAs (2018, background): “If pairing between the miRNA and the target site is sufficiently extensive, and if the miRNA is associated with an Argonaute protein that has retained its ancestral ability to catalyze the endonucleolytic cleavage characteristic of RNA interference (RNAi) (Liu et al., 2004; Meister et al., 2004), th”
- microRNAs in action: biogenesis, function and regulation (2023, background): “All four mammalian Ago proteins regulate seed-matched targets, but Ago2 uniquely exhibits the ability to use endogenous miRNAs and synthetic small RNA guides to cleave extensively paired targets 21,22 , an activity that does not require cofactors and mediates experimental RNA interference (RNAi).”
- Mechanisms of gene silencing by double-stranded RNA (2004, background): “Moreover, two recent studies in human systems showed that AGO1–AGO4 all associate with miRNAs and siRNAs, but that only the AGO2-containing RNPs exhibit RISC activit”
- Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies (2005, background): “To determine whether the localization of Ago2 was typical of other Argonaute proteins that are able to bind siRNAs and mRNAs, we set out to determine whether Ago1 and Ago2 colocaliz”
- Normal microRNA Maturation and Germ-Line Stem Cell Maintenance Requires Loquacious, a Double-Stranded RNA-Binding Domain Protein (2005, neutral): “of RISC [29,31,34,35,36].”
- Perspective: machines for RNAi. (2005, background): “Moreover, experiments using tagged, over-expressed human Argonaute proteins in cultured mammalian cells suggest that at least four human Argonaute proteins bind indiscriminately to miRNAs and siRNAs (Liu et al. 2004a; Meister et al. 2004).”
- Regulation by let-7 and lin-4 miRNAs results in target mRNA degradation. (2005, background): “Recent studies in Drosophila and mammalian systems have identified Argonaute 2 (AGO2) as the enzyme responsible for the RNA-guided slicing activity (Liu et al., 2004; Meister et al., 2004 ).”
- MicroRNA regulation by RNA-binding proteins and its implications for cancer (2011, background): “After cleavage of the ∼22-nt RNA duplex, now consisting of two 5′ phosphorylated sequence strands with 3′ overhangs, the functional strand, referred to as the guide strand, is loaded into an Argonaute (AGO) protei”
- Distinguishing protein-coding and noncoding genes in the human genome (2007, background): “Interestingly, the DDH motif, necessary for the endoribonuclease activity of EIF2C/Argonaute enzymes, was conserved in platypus EIF2C2 and all three PIWI proteins, as well as in EIF2C3, even though mouse and human orthologs of EIF2C3 appear to be noncatalytic (Liu et al. 2004; Meister et al. 2004).”
- Purified Argonaute2 and an siRNA form recombinant human RISC (2005, background): “Recent biochemical, genetic and structural studies have suggested a model in which the core activities of RISC could be contributed by these two factor”