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Human EIF2C1 Protein expressed in Baculovirus infected Insect Cells - ABIN2004127
Koesters, Adams, Betts, Moos, Schmid, Siermann, Hassam, Weitz, Lichter, Heitz, von Knebel Doeberitz, Briner: Human eukaryotic initiation factor EIF2C1 gene: cDNA sequence, genomic organization, localization to chromosomal bands 1p34-p35, and expression. in Genomics 1999
Show all 3 Pubmed References
findings propose that Ago-1 acts as a key regulator in controlling cell death, tumor regression and stress response in metazoan providing a constructive bridge between RNAi machinery and cell death
Results suggest that Wisp (show SNX9 Proteins) interacts with Ago1 and induces miRNA adenylation and facilitates its downregulation.
Results have established a novel role of Ago-1 as a regulator of the cell cycle.
AGO1 protein level is reduced in the absence of miRNA biogenesis & accumulates on depletion of GW182. Ectopic transcription of miRNAs within in vivo clones & genetic interference with the ubiquitin (show UBA52 Proteins)-proteasome system induced accumulation of AGO1.
Smaug (show SAMD4A Proteins) directly recruits Ago1 to nanos mRNA in a miRNA-independent manner, thereby repressing translation.
analysis of regulation of Argonaute slicer activity by guide RNA 3' end interactions with the N-terminal lobe
The study provides a molecular explanation for the previously reported heterogeneity of miRNA 3' ends and proposes a model in which Nibbler converts miRNAs into isoforms that are compatible with the preferred length of Ago1-bound small RNAs.
propose Drosophila Ago-1 as a multifunctional RNAi component that interconnects at least two unrelated events, chromatin organization in the nucleus and microRNA processing in the cytoplasm, which may be extended to the other systems
these results suggest that Ago1 and its miRNA biogenesis partners play a role in oocyte determination and germline cell division in Drosophila.
Ago1-RISC induces silencing via two independent pathways: shortening of the poly(A) tail and pure repression of translation
Ago1,Ago2,Ago3 and Piwi are upregulated upon infection with nucleopolyhedrovirus.
Data show that Ago4 (show EIF2C4 Proteins)- Ago1-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.
In miRNA-mediated gene silencing, the physical interaction between human Argonaute (show EIF2C2 Proteins) (hAgo (show FBXW7 Proteins)) and GW182 (hGW182) is essential for facilitating the downstream silencing of the targeted mRNA. hGW182 can recruit up to three copies of hAgo (show FBXW7 Proteins) via its three GW motifs. This may explain the observed cooperativity in miRNA-mediated gene silencing.
We selected five single nucleotide polymorphisms (SNPs) (rs7813, rs2740349, rs2291778, rs910924, rs595961) in two key microRNA biosynthesis genes (GEMIN4 and AGO1) and systematically evaluated the association between these SNPs, the gene-environment interaction and lung cancer risk. This is the first study showing that rs7813 and rs595961 could be meaningful as genetic markers for lung cancer risk.
Low AGO1 expression is associated with melanoma.
Blocking AGO1, AGO2, or TRBP expression changes expression levels and nuclear distribution of RNAi factors Dicer, TNRC6A (GW182), and TRBP.
EIF2C2 (show EIF2C2 Proteins), Dicer (show DICER1 Proteins), and Drosha (show DROSHA Proteins) are more highly expressed in bladder carcinoma, promote the development of bladder cancer, and suggested a poor prognosis
Argonaute-1 binds transcriptional enhancers and controls constitutive and alternative splicing
Completion of the tetrad, combined with a mutation on a loop adjacent to the active site of hAgo1, results in slicer activity that is substantially enhanced by swapping in the N domain of hAgo2 (show EIF2C2 Proteins).
Evolutionary amino acid changes to hAGO1 were readily reversible, suggesting that loading of guide RNA and pairing of seed-based miRNA and target RNA constrain its sequence drift.
nuclear Ago1 directly interacts with RNA Polymerase II and is widely associated with chromosomal loci throughout the genome with preferential enrichment in promoters of transcriptionally active genes
Aberrant expression of argonaute-1/-2 in human renal cell carcinoma (show MOK Proteins) is possibly involved with tumorigenesis and prognosis.
up-regulated in murine macrophage RAW264.7 cells transfected by Echinococcus multilocularis miR (show MLXIP Proteins)-71
Results from the liver show that, siRNA targets 3'UTR and the coding sequence (CDs (show ABHD5 Proteins)) of endogenous genes in the presence Ago2 (show EIF2C2 Proteins) but in its absence, only 3'UTR-targeted siRNA-mediated knockdown are active with the help of Ago1 and Ago3 (show EIF2C3 Proteins).
enhanced flu susceptibility of Ago1/3 double-knockout mice arises from an intrinsic impairment in the ability of lung cells to tolerate flu-elicited inflammation.
Ago3 (show EIF2C3 Proteins) is able to load microRNAs efficiently in the absence of Ago1 and Ago2 (show EIF2C2 Proteins), despite a significant loss of global microRNA expression
describes cloning rat sequence and used RNA interference to show that the GERp95 (show EIF2C2 Proteins) orthologue in C. elegans is important for maturation of germ-line stem cells in the gonad.
Results indicate that TRN1 (show TNPO1 Proteins) positively regulates miRNA activity by promoting the association of miRNAs with AGO1, and they reveal opposing roles of two importin beta (show KPNB1 Proteins) family proteins in miRNA loading.
Sweet potato mild mottle virus P1 interacts with AGO1 and AGO2 (show EIF2C2 Proteins), but solely interferes with AGO1 function.
Results suggests that ARGONAUTE1 (AGO1) interacts with chromatin at microRNAs MIR161 and MIR173 loci and causes the disassembly of the transcriptional complex, releasing short and unpolyadenylated transcripts.
that AGO1 may have functions in gene regulation independent of small RNAs.
AGO1 is a major, largely HSP90 (show HSP90 Proteins)-independent, factor in providing environmental robustness to plants.
miR168 is a key miRNA because it regulates the expression of the slicer protein ARGONAUTE1 (AGO1), which catalyzes mRNA cleavage. Interestingly, plant miR168s are highly evolutionarily conserved; however, it is unclear whether MIR168 promoter elements and expression patterns are also conserved.
a total of 5,123 and 1,399 AGO1-enriched small RNAs, excluding miRNAs, were identified in Arabidopsis thaliana and rice (Oryza sativa), respectively.
Mungbean yellow mosaic Indian virus AC2 interacts with AGO1 and inhibits its transcript slicing activity in vitro.
AGO1, AGO2 and AGO10 promoted anti-TuMV defense in a modular way in various organs, with AGO2 providing a prominent antiviral role in leaves. AGO5, AGO7 and AGO10 had minor effects in leaves.
HOS1 regulates miR168a/b and AGO1 levels in Arabidopsis by maintaining proper transcription of MIR168b.
This gene encodes a member of the Argonaute family of proteins which play a role in RNA interference. The encoded protein is highly basic, and contains a PAZ domain and a PIWI domain. It may interact with dicer1 and 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 argonaute 4.
, argonaute 1
, argonaute protein 1
, mRNA-like ncRNA in embryogenesis 20
, eukaryotic translation initiation factor 2C, 1
, protein argonaute-1-like
, Golgi Endoplasmic Reticulum protein 95 kDa
, eIF-2C 1
, eIF2C 1
, protein argonaute-1
, putative RNA-binding protein Q99
, Piwi/Argonaute family protein meIF2C1
, argonaute RISC catalytic component 1