ArticleJournal of the American Chemical Society2009
Controlling peptide folding with repulsive interactions between phosphorylated amino acids and tryptophan.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- α-Alkylated α-amino acids reduce the aggregation of unfolded peptides.RSC advances · 2026Article
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- A structural machine learning approach for rapid prediction of thermodynamically destabilizing tyrosine phosphorylations.Cell reports methods · 2025Article
- Ultralong organic phosphorescence from isolated molecules with repulsive interactions for multifunctional applications.Nature communications · 2022Article
- Structural impact of thioamide incorporation into a β-hairpin.RSC chemical biology · 2022Article
- Article
- From supramolecular chemistry to the nucleosome: studies in biomolecular recognition.Beilstein journal of organic chemistry · 2016Review
- Towards the computational design of protein post-translational regulation.Bioorganic & medicinal chemistry · 2015Review
- Article
- OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.Journal of the American Chemical Society · 2014Article
- Phosphorylation variation during the cell cycle scales with structural propensities of proteins.PLoS computational biology · 2013Article
- Molecular dynamics of β-hairpin models of epigenetic recognition motifs.Journal of the American Chemical Society · 2012Article
- Structural role of RKS motifs in chromatin interactions: a molecular dynamics study of HP1 bound to a variably modified histone tail.Biophysical journal · 2012Article
- Parallel β-sheet secondary structure is stabilized and terminated by interstrand disulfide cross-linking.Journal of the American Chemical Society · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylated amino acids were incorporated into a designed beta-hairpin peptide to study the effect on beta-hairpin structure when the phosphate group is positioned to interact with a tryptophan residue on the neighboring strand. The three commonly phosphorylated residues in biological systems, serine, threonine, and tyrosine, were studied in the same beta-hairpin system. It was found that phosphorylation destabilizes the hairpin structure by approximately 1.0 kcal/mol, regardless of the type of phosphorylated residue. In contrast, destabilization due to glutamic acid was about 0.3 kcal/mol. Double mutant cycles and pH studies are consistent with a repulsive interaction as the source of destabilization. These findings demonstrate a novel mechanism by which phosphorylation may influence protein structure and function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.