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Lou, M., Garrett, T.P.J., McKern, N.M., Hoyne, P.A., Epa, V.C., Bentley, J.D., et al. (2006) The First Three Domains of the Insulin Receptor Differ Structurally from the Insulin-Like Growth Factor 1 Receptor in the Regions Governing Ligand Specificity. Proceedings of the National Academy of Sciences, 103, 12429-12434.
https://doi.org/10.1073/pnas.0605395103

has been cited by the following article:

• TITLE: Systematic Analysis of Post-Translational Modifications for Increased Longevity of Biotherapeutic Proteins

  AUTHORS: Justin Kim, Karanveer Sadiora

  KEYWORDS: Post-Translational Modification, Protein-Based Therapeutics, Therapeutic Half-Life, Protein Aggregation, Protein Reception

  JOURNAL NAME: Computational Molecular Bioscience, Vol.14 No.3, September 10, 2024

  ABSTRACT: Protein-based therapeutics (PPTs) are drugs used to treat a variety of different conditions in the human body by alleviating enzymatic deficiencies, augmenting other proteins and drugs, modulating signal pathways, and more. However, many PPTs struggle from a short half-life due to degradation caused by irreversible protein aggregation in the bloodstream. Currently, the most researched strategies for improving the efficiency and longevity of PPTs are post-translational modifications (PTMs). The goal of our research was to determine which type of PTM increases longevity the most for each of three commonly-used therapeutic proteins by comparing the docking scores (DS) and binding free energies (BFE) from protein aggregation and reception simulations. DS and BFE values were used to create a quantitative index that outputs a relative number from −1 to 1 to show reduced performance, no change, or increased performance. Results showed that methylation was the most beneficial for insulin (p