Structure of Human DROSHA.
Seoul, South Korea. In Cell, Feb 2016
MicroRNA maturation is initiated by RNase III DROSHA that cleaves the stem loop of primary microRNA.
Characterization of ribonuclease III from Brucella.
Wuhan, China. In Gene, Feb 2016
UNASSIGNED: Bacterial ribonuclease III (RNase III) is a highly conserved endonuclease, which plays pivotal roles in RNA maturation and decay pathways by cleaving double-stranded structure of RNAs.
Distinct E-cadherin-based complexes regulate cell behaviour through miRNA processing or Src and p120 catenin activity.
Jacksonville, United States. In Nat Cell Biol, Sep 2015
Here, we resolve this apparent paradox by identifying two spatially and functionally distinct junctional complexes in non-transformed polarized epithelial cells: one growth suppressing at the apical zonula adherens (ZA), defined by the p120 partner PLEKHA7 and a non-nuclear subset of the core microprocessor components DROSHA and DGCR8, and one growth promoting at basolateral areas of cell-cell contact containing tyrosine-phosphorylated p120 and active Src.
Functional Anatomy of the Human Microprocessor.
Seoul, South Korea. In Cell, Jul 2015
MicroRNA (miRNA) maturation is initiated by Microprocessor composed of RNase III DROSHA and its cofactor DGCR8, whose fidelity is critical for generation of functional miRNAs.
Signaling-mediated regulation of MicroRNA processing.
Houston, United States. In Cancer Res, Apr 2015
Canonical miRNA biogenesis consists of a two-step processing, from primary transcripts (pri-miRNA) to precursor miRNAs (pre-miRNA) mediated by Drosha in the nucleus and from pre-miRNAs to mature miRNAs mediated by Dicer in the cytoplasm.
TRAIL mediated signaling in pancreatic cancer.
Santa Maria, Brazil. In Asian Pac J Cancer Prev, 2013
It has been shown that DR5 interacts with the core microprocessor components Drosha and DGCR8, thus impairing processing of primary let-7.
DGCR8 HITS-CLIP reveals novel functions for the Microprocessor.
Edinburgh, United Kingdom. In Nat Struct Mol Biol, 2012
DGCR8-mediated cleavage of snoRNAs was independent of Drosha, suggesting the involvement of DGCR8 in cellular complexes with other endonucleases. Binding of DGCR8 to cassette exons is a new mechanism for regulation of alternatively spliced isoforms.