Intrinsically disordered regions as affinity tuners in protein–DNA interactions
By Yaakov Levy. 2012
133 citations recorded by the source corpus.
Subfields: Cell Biology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/7db0c2bd92440bfdb3347cb86d9711d618cd9007
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In Cell Biology
In Molecular Biology
Citations in the corpus
- Structural Mechanisms of Nucleosome Recognition by Linker Histones (2015, result): “These results are consistent with the view that linker histone tails are intrinsically disordered regions and likely to interact non-specifically with the linker DNA, which allows chromatin to fold by reducing electrostatic repulsion (Vuzman and Levy, 2012).”
- Conformations of intrinsically disordered proteins are influenced by linear sequence distributions of oppositely charged residues (2013, background): “Proc Natl Acad Sci USA 109(40):16155–16160.”
- Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. (2012, unknown): “Hypothetically, poly(K) patches could establish electrostatic interactions with the phosphate backbone of RNA in analogy with the basic tails in DNA-binding proteins (DBPs) (Vuzman and Levy, 2012).”