Structural Basis for Double-Stranded RNA Processing by Dicer

By I. MacRae, Kaihong Zhou, Fei Li, Adrian Repic, Angela N. Brooks, W. Cande, Paul D. Adams, Jennifer A. Doudna. Science, 2006

1,007 citations recorded by the source corpus.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/2f3cda257860e2a220f5ba223ab51618605f22e2

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Citations in the corpus

Biogenesis, Turnover, and Mode of Action of Plant MicroRNAs[OPEN] (2013, background): “The intramolecular spacing of the RNase III active site and the 39 overhang binding pocket of the PAZ domain is thought to act as a molecular ruler determining the length of the dsRNA product helix generated by Dicer family enzymes (Macrae et al., 2006).”
siRNA vs. shRNA: similarities and differences. (2009, background): “Dicer preferentially binds to the 5′ phosphate of 2 nt 3′ overhang and cleaves dsRNAs into 21 to 22 nucleotide siRNAs [72,73].”
Molecular basis for the recognition of primary microRNAs by the Drosha-DGCR8 complex. (2006, background): “…domain of Dicer may interact with the 30 overhang at the terminus and determines the processing site in a ruler-like fashion that measures 22 nt segments away from the terminus (Lingel et al., 2004; Ma et al., 2004; Macrae et al., 2006; Song et al., 2003; Vermeulen et al., 2005; Yan et al., 2003).”
Origins and Mechanisms of miRNAs and siRNAs (2009, background): “Biochemical, genetic, and structural studies have converged on a model in which the PAZ and RNase III domains play central roles in excising siRNAs preferentially from ends of dsRNA molecules (Zhang et al., 2004;Macrae et al., 2006).”
Macromolecular crystal twinning, lattice disorders and multiple crystals (2008, methodology): “The enzyme ‘Dicer’ MacRae and Doudna (64) worked on the crystal structure of the enzyme ‘Dicer’ from Giardia intestinalis to 3.3 Å resolution by MAD using crystals belonging to space group P21212 (65).”
microRNAs in action: biogenesis, function and regulation (2023, background): “initial structures of Dicer and Argonaute homologues from protozoan ( Giardia intestinalis ) and archaeal ( Thermus thermophilus and Pyrococcus furiosus ) species 18,48,78–80 .”
Molecular mechanisms of RNA interference (2013, neutral): “Giardia intestinalis Dicer lacks a helicase domain (59), and the budding yeast Kluyveromyces polysporus equivalent is further pared down, lacking a PAZ domain and bearing an RNase III”