ArticleFEBS open bio2014
Contribution of protein phosphorylation to binding-induced folding of the SLBP-histone mRNA complex probed by phosphorus-31 NMR.
Article in FEBS open bio, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 8 citations in OpenAlex.
- Stem-loop binding protein and metal carcinogenesis.Seminars in cancer biology · 2021Review
- Protein-assisted RNA fragment docking (RnaX) for modeling RNA-protein interactions using ModelX.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Structure-specific nucleic acid recognition by L-motifs and their diverse roles in expression and regulation of the genome.Biochimica et biophysica acta · 2015Review
- Structural basis for regulation of RNA-binding proteins by phosphorylation.ACS chemical biology · 2015Review
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1 author at 1 institution in 1 country.
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Abstract
Phosphorus-31 ((31)P) NMR can be used to characterize the structure and dynamics of phosphorylated proteins. Here, I use (31)P NMR to report on the chemical nature of a phosphothreonine that lies in the RNA binding domain of SLBP (stem-loop binding protein). SLBP is an intrinsically disordered protein and phosphorylation at this threonine promotes the assembly of the SLBP-RNA complex. The data show that the (31)P chemical shift can be a good spectroscopic probe for phosphate-coupled folding and binding processes in intrinsically disordered proteins, particularly where the phosphate exhibits torsional strain and is involved in a network of hydrogen-bonding interactions.
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