ArticleScientific reports2019
Ligand entry in human ileal bile acid-binding protein is mediated by histidine protonation.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 4 citations in OpenAlex.
- Functionally related internal fluctuations in human ileal bile acid-binding protein by high pressure nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2026Article
- Multiple Timescale Dynamic Analysis of Functionally-Impairing Mutations in Human Ileal Bile Acid-Binding Protein.International journal of molecular sciences · 2022Article
- Structural and Dynamic Determinants of Molecular Recognition in Bile Acid-Binding Proteins.International journal of molecular sciences · 2022Review
- Mapping the electrostatic potential of the nucleosome acidic patch.Scientific reports · 2021Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human ileal bile acid-binding protein (hI-BABP) has a key role in the intracellular transport of bile salts. To explore the role of histidine protonation in the binding process, the pH-dependence of bile salt binding and internal dynamics in hI-BABP was investigated using NMR spectroscopy and biophysical tools. Thermodynamic and kinetic measurements show an increase in the overall binding affinity and the association rate constant of the first binding step below the pK
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Registered trials
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