The RNA recognition motif, a plastic RNA‐binding platform to regulate post‐transcriptional gene expression
By C. Maris, C. Dominguez, F. Allain. The FEBS Journal, 2005
1,126 citations recorded by the source corpus.
Subfields: Molecular Biology
View Paper: https://www.semanticscholar.org/paper/c0483c731af06166b9b2cca004ef2c7230a259d7
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In Molecular Biology
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Citations in the corpus
- RNA-binding proteins: modular design for efficient function (2007, background): “The reader is referred to several excellent reviews that discuss in greater detail the molecular mechanisms that are used by individual domains to recognize specific RNA”
- Sampling native-like structures of RNA-protein complexes through Rosetta folding and docking (2018, background): “…we assumed the positions of the 5’ and 3’ nucleotides relative to the protein because for many single-stranded RNA binding proteins, RNA-protein contacts around these positions are highly conserved (Maris et al., 2005), therefore allowing these nucleotides to serve as anchor points during modeling.”
- Molecular Mechanisms of TDP-43 Misfolding and Pathology in Amyotrophic Lateral Sclerosis (2019, background): “Some RBPs, such as TDP-43, are also implicated in neurodegenerative diseases which therefore hints of disturbances in the RNA metabolism as a causative factor (Maris et al., 2005; Lunde et al., 2007; Clery et al., 2008).”
- Deep mutational scanning of an RRM domain of the Saccharomyces cerevisiae poly(A)-binding protein (2013, background): “N132 is part of the RNP2 motif (Maris et al. 2005) and is highly conserved.”
- RNA controls PolyQ protein phase transitions (2015, background): “To further probe the role of the RRM domain in droplet assembly, we introduced point mutations (Y610A or F653A) predicted to be directly involved in RNA binding (Maris et al., 2005; Nash et al., 2001).”