ORIGINAL ARTICLEmRNA translation is not a prerequisite for small interfering RNA-mediated mRNA cleavage
References (20)
- et al.
Balancing acts: molecular control of mammalian iron metabolism
Cell
(2004) - et al.
IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F
Mol Cell
(1998) - et al.
A dicer-2-dependent 80s complex cleaves targeted mRNAs during RNAi in Drosophila
Cell
(2004) Mammalian RNAi for the masses
Trends Genet
(2003)- et al.
RNAi: double-stranded RNA directs the ATP-dependent cleavage of mRNA at 21 to 23 nucleotide intervals
Cell
(2000) - et al.
Depletion of intracellular Ca2+ stores, phosphorylation of eIF2alpha, and sustained inhibition of translation initiation mediate the anticancer effects of clotrimazole
Proc Natl Acad Sci USA
(1998) - et al.
Antibiotics and compounds affecting tanslation by eukaryotic ribosomes. Specific enhancement of aminoacyl-tRNA binding by methylaxnthines
Mol Cell Biochem
(1976) - et al.
Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
Nature
(1998) - et al.
Uncoupling of RNAi from active translation in mammalian cells
RNA
(2005) - et al.
Translational repression by a complex between the iron-responsive element of ferritin mRNA and its specific cytoplasmic binding protein is position-dependent in vivo
EMBO J
(1990)
There are more references available in the full text version of this article.
Cited by (20)
Preferential cleavage of upstream targets in concatenated miRNA/siRNA target sites support a 5′-3′ scanning model for RISC target recognition
2024, Biochemical and Biophysical Research CommunicationsNanotechnology for DNA and RNA delivery
2023, Nanomedicine: Technologies and ApplicationsRNA interference technology
2019, Comprehensive BiotechnologyNanotechnology for DNA and RNA delivery
2012, Nanomedicine: Technologies and ApplicationsRNA interference in Trypanosoma brucei: Role of the N-terminal RGG domain and the polyribosome association of argonaute
2009, Journal of Biological ChemistryCitation Excerpt :Thus, our previous studies suggested a potential interaction between TbAGO1 and ribosomes. Although studies in vitro and in vivo have shown that RNAi can be uncoupled from translation (19–21), a link between the RNAi machinery and the translational apparatus has been suggested by several lines of investigations. Early studies indicated that in S2 cells RISC components pellet with ribosomes and other large complexes after high speed centrifugation (5, 22, 23) and later experiments suggested that RISC is loaded into an 80 S complex, possibly the ribosome (24).
RISC-target interaction: Cleavage and translational suppression
2008, Biochimica et Biophysica Acta - Gene Regulatory Mechanisms
Copyright © 2005 International Society of Differentiation. Published by Elsevier Inc. All rights reserved.