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demonstrate that Pol V lncRNAs or the act of their transcription are required to lock Pol V holoenzyme into a stable DNA-bound state that allows AGO4 recruitment via redundant glycine-tryptophan/tryptophan-glycine AGO hook motifs present on both Pol V and its associated factor, SPT5L.
Findings reported here highlight an involvement of AGO4 during meiosis by ensuring accurate chromosome segregation at anaphase I.
Members of the AGO4 clade cooperatively participate in preventing the abnormal specification of multiple premeiotic gametophytic precursors during early ovule development.
Our results indicate that AtMBD6 is involved in RNA-mediated gene silencing and it binds to RNA binding proteins like AtRPS2C, AtAGO4 and AtNTF2. AtMBD6 also interacts with histone deacetylase AtHDA6 (show HDAC6 Proteins) that might have a role in chromatin condensation at the targets of RdDM
These findings suggest that the targets of AGO4-directed RNA-directed DNA methylation (show HELLS Proteins) are regulatory units responsible for controlling gene expression under specific environmental conditions.
AGO4 and AGO6 mainly act sequentially in mediating small RNA-directed DNA methylation (show HELLS Proteins).
Trans-acting small interfering RNAs are associated with AGO4 proteins to direct DNA methylation (show HELLS Proteins).
selective nuclear import of mature AGO4/siRNA complexes is a key regulatory point prior to the effector stage of RdDM.
DNA-dependent RNA polymerase IV-dependent smRNAs were mainly 24 nt and associated with AGO4.
our data suggest that AGO4 is guided to target loci through base-pairing of associated siRNAs with nascent RNA Pol V transcripts.
Chimeras with Ago4 N-terminal domains were defective in RISC activation & sometimes also in RNA loading. This highlights the pleiotropic role of the Ago N domain & emphasizes the unique position of human Ago4 within the Ago protein family.
EIF2C2 (show EIF2C2 Proteins)-4 and PIWIL4 (show PIWIL4 Proteins) appear increased in advanced tumors with distant metastasis, suggesting they may promote tumor invasion
The specificity of RNA interference depends on the concentration of Ago1 (show EIF2C1 Proteins), Ago3 (show EIF2C3 Proteins), and Ago4 relative to Ago2 (show EIF2C2 Proteins).
EIF2C4 protein is expressed in differentiating and terminally differentiated N-type cells more than in S- and I-type cells
up-regulated in murine macrophage RAW264.7 cells transfected by Echinococcus multilocularis miR (show MLXIP Proteins)-71
show that Ago4(-/-) spermatogonia initiate meiosis early, resulting from premature induction of retinoic acid-response genes
Data show that Ago4- Ago1 (show EIF2C1 Proteins)-Ago3 (show EIF2C3 Proteins) genes are linked together at the p12 (show SPRN Proteins) of the chromosome 6, while Ago2 (show EIF2C2 Proteins) is located at the p15 (show CDKN2B Proteins) of the chromosome 4.
This gene encodes a member of the Argonaute family of proteins which play a role in RNA interference. The encoded protein is highly basic containing PAZ and PIWI domains, and it may play a role in short-interfering-RNA-mediated gene silencing. This gene is located on chromosome 1 in a cluster of closely related family members including argonaute 3, and eukaryotic translation initiation factor 2C, 1.
eukaryotic translation initiation factor 2C, 4
, argonaute 4
, protein argonaute-4
, eIF-2C 4
, eIF2C 4
, Piwi/Argonaute family protein meIF2C4
, argonaute RISC catalytic component 4