ArticleThe Journal of biological chemistry2018
Structure-based stabilization of insulin as a therapeutic protein assembly via enhanced aromatic-aromatic interactions.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
The trial behind it
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Who cites it
10 citing papers in PubMed.
- Effects of acetylation on human insulin structure, and dynamics at different temperatures: A molecular dynamics simulation study.Journal of biosciences · 2026Article
- Stabilization of a protein by a single halogen-based aromatic amplifier.Protein science : a publication of the Protein Society · 2025Article
- Synthesis of a highly thermostable insulin by phenylalanine conjugation at B29 Lysine.Communications chemistry · 2024Article
- In Vitro Affinity Maturation of Nanobodies against Mpox Virus A29 Protein Based on Computer-Aided Design.Molecules (Basel, Switzerland) · 2023Article
- An Investigation into the Acidity-Induced Insulin Agglomeration: Implications for Drug Delivery and Translation.ACS omega · 2023Article
- Progress in Simulation Studies of Insulin Structure and Function.Frontiers in endocrinology · 2022Review
- The conserved aromatic residue WMolecular plant pathology · 2021Article
- Modulating Insulin Fibrillation Using Engineered B-Chains with Mutated C-Termini.Biophysical journal · 2019Article
- Homology Modeling-Based in Silico Affinity Maturation Improves the Affinity of a Nanobody.International journal of molecular sciences · 2019Article
- Human αB-crystallin as fusion protein and molecular chaperone increases the expression and folding efficiency of recombinant insulin.PloS one · 2018Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Key contributions to protein structure and stability are provided by weakly polar interactions, which arise from asymmetric electronic distributions within amino acids and peptide bonds. Of particular interest are aromatic side chains whose directional π-systems commonly stabilize protein interiors and interfaces. Here, we consider aromatic-aromatic interactions within a model protein assembly: the dimer interface of insulin. Semi-classical simulations of aromatic-aromatic interactions at this interface suggested that substitution of residue Tyr
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Registered trials
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