Search Results - "Booth, Jonathan J"

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  1. 1

    Mechanism of Hydrophobic Drug Solubilization by Small Molecule Hydrotropes by Booth, Jonathan J, Abbott, Steven, Shimizu, Seishi

    Published in The journal of physical chemistry. B (27-12-2012)
    “…Drugs that are poorly soluble in water can be solubilized by the addition of hydrotropes. Albeit known for almost a century, how they work at a molecular basis…”
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    Journal Article
  2. 2

    Hydrotrope accumulation around the drug: the driving force for solubilization and minimum hydrotrope concentration for nicotinamide and urea by Booth, Jonathan J, Omar, Muhiadin, Abbott, Steven, Shimizu, Seishi

    Published in Physical chemistry chemical physics : PCCP (01-01-2015)
    “…Nicotinamide is an effective non-micellar hydrotrope (solubilizer) for drugs with low aqueous solubility. To clarify the molecular basis of nicotinamide's…”
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    Journal Article
  3. 3

    Hydrotropy: binding models vs. statistical thermodynamics by Shimizu, Seishi, Booth, Jonathan J, Abbott, Steven

    Published in Physical chemistry chemical physics : PCCP (21-12-2013)
    “…Hydrophobic drugs can often be solubilized by the addition of hydrotropes. We have previously shown that preferential drug-hydrotrope association is one of the…”
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    Journal Article
  4. 4

    Fully Atomistic Simulations of Protein Unfolding in Low Speed Atomic Force Microscope and Force Clamp Experiments with the Help of Boxed Molecular Dynamics by Booth, Jonathan J, Shalashilin, Dmitrii V

    Published in The journal of physical chemistry. B (04-02-2016)
    “…The results of boxed dynamics (BXD) fully atomistic simulations of protein unfolding by atomic force microscopy (AFM) in both force clamp (FC) and velocity…”
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    Journal Article
  5. 5

    Mechanical Unfolding of Proteins—A Comparative Nonequilibrium Molecular Dynamics Study by Mykuliak, Vasyl V., Sikora, Mateusz, Booth, Jonathan J., Cieplak, Marek, Shalashilin, Dmitrii V., Hytönen, Vesa P.

    Published in Biophysical journal (01-09-2020)
    “…Mechanical signals regulate functions of mechanosensitive proteins by inducing structural changes that are determinant for force-dependent interactions. Talin…”
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  6. 6