[19] Intra-RNA and RNA—protein cross-linking techniques in Escherichia coli ribosomes
References (38)
- et al.
J. Mol. Biol.
(1973) - et al.
J. Mol. Biol.
(1986) - et al.
J. Mol. Biol.
(1982) - et al.
J. Mol. Biol.
(1981) - et al.
Anal. Biochem.
(1977) - et al.
J. Mol. Biol.
(1978) - et al.
Anal. Biochem.
(1980) - et al.
J. Mol. Biol.
(1980) - et al.
J. Mol. Biol.
(1973) - et al.
Anal. Biochem.
(1970)
Anal. Biochem.
Anal. Biochem.
J. Immunol. Methods
Nucleic Acids Res.
Nucleic Acids Res.
Cited by (64)
Progress in genome-wide identification of RBPs and their role in mitigating stresses, and growth in plants
2023, South African Journal of BotanyNext-generation sequencing: A new avenue to understand viral RNA–protein interactions
2022, Journal of Biological ChemistryCitation Excerpt :This prevents HITS-CLIP’s application to complex tissues or organs. It is also important to note that during short wavelength UV radiation, protein-RNA crosslinks are not exclusive (61–63) and extensive RNA-RNA crosslinking can also occur (64, 65), which can interfere with the interpretation of true RNA–protein interactions. During downstream analysis, bioinformatic tools have been developed to maximize the specificity and sensitivity of HITS-CLIP data (reviewed in (66, 67)).
Advances in stem cell proteomics
2017, Current Opinion in Genetics and DevelopmentAnalysis of RNA-protein interactions in vertebrate embryos using UV crosslinking approaches
2017, MethodsCitation Excerpt :Over the past decade, UV crosslinking approaches have been extensively used to study RNA-protein interactions in tissue culture cells. UV light creates irreversible, covalent intra and intermolecular nucleic acid- and protein-nucleic acid linkages at 0 Å [2]. In vivo generation of crosslinks within the cell, followed by cell lysis allows purification of RNPs under stringent conditions without a risk of losing the association between RNA and protein of interest, simultaneously circumventing the isolation of proteins that do not directly interact with RNA.
mRNA interactome capture in mammalian cells
2017, MethodsCitation Excerpt :Similar to crosslinking and immunoprecipitation (CLIP) methods [20–23], covalent bond formation between proteins and RNA is achieved by UV crosslinking, a photo-crosslinking approach for which monochromatic UV light irradiation is used. It induces short-lived free radicals at nucleotide bases resulting in covalent bond formation with amino acids of proteins in direct vicinity (∼2 Å, “zero distance”) [24,25]. Two approaches are commonly used fur UV crosslinking: Conventional UV crosslinking (cCL) uses UV irradiation at 254 nm wavelength to induce covalent bond formation between nucleic acids and proteins.