Defining the RGG/RG motif.
By Palaniraja Thandapani, Timothy R. O'Connor, Timothy L. Bailey, S. Richard. Molecules and Cells, 2013
617 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/482346c1518646529a4215dd67c1008682ef8812
How researchers see this paper
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In Molecular Biology
- C. Brangwynne
- S. Richard
- Thomas Tuschl
- Matthias W. Hentze
- M. Hafner
- S. Gerstberger
- Roméo S. Blanc
- Jeroen Krijgsveld
Citations in the corpus
- A census of human RNA-binding proteins (2014, background): “heteronuclear RBPs (hnRNPs) [reviewed in (Thandapani et al., 2013)].”
- Arginine Methylation: The Coming of Age. (2017, background): “PRMT1 is the main enzyme responsible for the generation of aDMA in proteins, and it has a preference for RGG/RG motifs (Thandapani et al., 2013); however, there are numerous exceptions.”
- Comprehensive Identification of RNA-Binding Domains in Human Cells (2016, background): “The superset of RNA-binding RGG boxes can be subclassified by the lengths of the glycine linkers (Thandapani et al., 2013).”
- The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics (2015, background): “The disordered N terminus is rich in arginines (R) and glycines (G) and is similar to the well-known RGG/RG motif RNAbinding domain (43).”