ArticleFrontiers in endocrinology2011
Conformational dynamics of insulin.
Article in Frontiers in endocrinology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 40 citations in OpenAlex.
- Damping amyloid-associated conformational fluctuations in a protein by an engineered diselenide bridge.Protein science : a publication of the Protein Society · 2026Article
- Stabilization of a protein by a single halogen-based aromatic amplifier.Protein science : a publication of the Protein Society · 2025Article
- X-ray crystallographic and hydrogen deuterium exchange studies confirm alternate kinetic models for homolog insulin monomers.PloS one · 2025Article
- Exploring proinsulin proteostasis: insights into beta cell health and diabetes.Frontiers in molecular biosciences · 2025Review
- Synthetic studies of the mutant proinsulin syndrome demonstrate correlation between folding efficiency and age of diabetes onset.International journal of peptide research and therapeutics · 2025Article
- Analysis of the Dynamics of a Complex, Multipathway Reaction: Insulin Dimer Dissociation.The journal of physical chemistry. B · 2024Article
- Unraveling Light-Activated Insulin Action in Regulating Blood Glucose: New Photoactivatable Insight as a Novel Modality in Diabetes Management.Molecules (Basel, Switzerland) · 2024Article
- Peptide Model of the Mutant Proinsulin Syndrome. II. Nascent Structure and Biological Implications.Frontiers in endocrinology · 2022Article
- Structural Ensemble of the Insulin Monomer.Biochemistry · 2021Article
- Structural principles of insulin formulation and analog design: A century of innovation.Molecular metabolism · 2021Review
- Insertion of a synthetic switch into insulin provides metabolite-dependent regulation of hormone-receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural Lessons From the Mutant Proinsulin Syndrome.Frontiers in endocrinology · 2021Review
- Evolution of insulin at the edge of foldability and its medical implications.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Long-term glycemic control and prevention of diabetes complications in vivo using oleic acid-grafted-chitosan‑zinc-insulin complexes incorporated in thermosensitive copolymer.Journal of controlled release : official journal of the Controlled Release Society · 2020Article
- "Register-shift" insulin analogs uncover constraints of proteotoxicity in protein evolution.The Journal of biological chemistry · 2020Article
- Smart Thermosensitive Copolymer Incorporating Chitosan-Zinc-Insulin Electrostatic Complexes for Controlled Delivery of Insulin: Effect of Chitosan Chain Length.International journal of polymeric materials · 2020Article
- Probing the correlation between insulin activity and structural stability through introduction of the rigid A6-A11 bond.The Journal of biological chemistry · 2018Article
- Structure-based stabilization of insulin as a therapeutic protein assembly via enhanced aromatic-aromatic interactions.The Journal of biological chemistry · 2018Article
- Solution structure of an ultra-stable single-chain insulin analog connects protein dynamics to a novel mechanism of receptor binding.The Journal of biological chemistry · 2018Article
- Extending Halogen-based Medicinal Chemistry to Proteins: IODO-INSULIN AS A CASE STUDY.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
We have exploited a prandial insulin analog to elucidate the underlying structure and dynamics of insulin as a monomer in solution. A model was provided by insulin lispro (the active component of Humalog(®); Eli Lilly and Co.). Whereas NMR-based modeling recapitulated structural relationships of insulin crystals (T-state protomers), dynamic anomalies were revealed by amide-proton exchange kinetics in D(2)O. Surprisingly, the majority of hydrogen bonds observed in crystal structures are only transiently maintained in solution, including key T-state-specific inter-chain contacts. Long-lived hydrogen bonds (as defined by global exchange kinetics) exist only at a subset of four α-helical sites (two per chain) flanking an internal disulfide bridge (cystine A20-B19); these sites map within the proposed folding nucleus of proinsulin. The anomalous flexibility of insulin otherwise spans its active surface and may facilitate receptor binding. Because conformational fluctuations promote the degradation of pharmaceutical formulations, we envisage that "dynamic re-engineering" of insulin may enable design of ultra-stable formulations for humanitarian use in the developing world.
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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.