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RNA-Binding Proteins Chaperone Ribonucleoprotein Complex Assembly to Solve the RNA-Folding Problem
Author(s) -
Katherine E. Bohnsack,
Markus T. Bohnsack
Publication year - 2019
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2019.11.011
Subject(s) - ribonucleoprotein , biology , rna , ribosome , chaperone (clinical) , ribonucleoprotein particle , microbiology and biotechnology , cooperativity , rna binding protein , genetics , gene , medicine , pathology
The inherent tendency of RNAs to misfold is a major problem that can impede efficient assembly of essential ribonucleoprotein complexes (RNPs), such as ribosomes. In this issue of Cell, Duss et al., (2019) and Rodgers and Woodson (2019) reveal how transient RNA-protein interactions can chaperone RNA folding during RNP assembly.

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