ArticleiScience2025
Decoding elegant interplay among different stereo-electronic effects due to the ancient prolyl-4-hydroxylation stabilizing collagenous helicity.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Selective Hydroxylation of Collagen Model Peptides by Metal Catalysis.Chemistry & biodiversity · 2026Article
- Molecular foundations of collagen triple helical assembly: the central role of prolyl-4-hydroxylation.The Biochemical journal · 2026Review
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Authors and funding
3 authors.
Funding
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Abstract
Prolyl-4-hydroxylation is an ancient evolutionarily conserved post-translational modification (PTM) critical for both structural and regulatory functions in multicellular life forms. This PTM plays a pivotal role in stabilizing collagen's triple helix by influencing the puckering of the pyrrolidine ring. The elegant interplay between ring pucker, torsional angles, peptide bond isomerization, and charge-transfer interactions (O···C=O n→π∗ and σ→σ∗) attaining the helical stability remains underappreciated. Using density functional theory calibrated against gold standard
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Registered trials
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