ArticleJournal of biomolecular NMR2018
A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study.
Article in Journal of biomolecular NMR, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- SelectiveAngewandte Chemie (International ed. in English) · 2022Article
- NMR illuminates intrinsic disorder.Current opinion in structural biology · 2021Review
- Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues.Magnetic resonance (Gottingen, Germany) · 2021Article
- HACANCOi: a new HJournal of biomolecular NMR · 2020Article
- Multi-receiver solid-state NMR using polarization optimized experiments (POE) at ultrafast magic angle spinning.Journal of biomolecular NMR · 2020Article
- Dispersion from CJournal of biomolecular NMR · 2020Article
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Authors and funding
6 authors.
Funding
Abstract
The C-terminal domain of histone H1.0 (C-H1.0) is involved in DNA binding and is a main determinant of the chromatin condensing properties of histone H1.0. Phosphorylation at the (S/T)-P-X-(K/R) motifs affects DNA binding and is crucial for regulation of C-H1.0 function. Since C-H1.0 is an intrinsically disordered domain, solution NMR is an excellent approach to characterize the effect of phosphorylation on the structural and dynamic properties of C-H1.0. However, its very repetitive, low-amino acid-diverse and Pro-rich sequence, together with the low signal dispersion observed at the
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