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  1. No Access

    Article

    Functional groups matter: metabolomics analysis of Escherichia coli exposed to trans-cinnamic acid and its derivatives unveils common and unique targets

    Phenolic acids are derivatives of benzoic and cinnamic acids, which possess important biological activities at certain concentrations. Trans-cinnamic acid (t-CA) and its derivatives, such as p-coumaric acid (p...

    Kadriye Aslıhan Onat-Taşdelen… in World Journal of Microbiology and Biotechn… (2023)

  2. Article

    Open Access

    A simple and sensitive detection of the binding ligands by using the receptor aggregation and NMR spectroscopy: a test case of the maltose binding protein

    Protein-ligand interaction is one of the highlights of molecular recognition. The most popular application of this type of interaction is drug development which requires a high throughput screening of a ligand...

    Young Kee Chae, Yoon** Um, Hakbeom Kim in Journal of Biomolecular NMR (2021)

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  3. No Access

    Article

    Discovery of novel human phenylethanolamine N-methyltransferase (hPNMT) inhibitors using 3D pharmacophore-Based in silico, biophysical screening and enzymatic activity assays

    With the aid of receptor-oriented pharmacophore-based in silico screening, we established three pharmacophore maps explaining the binding model of hPNMT and a known inhibitor, SK&F 29661 (Martin et al., 2001). Th...

    Dong-Il Kang, Jee-Young Lee, Woonghee Kim, Ki-Woong Jeong… in Molecules and Cells (2010)

  4. No Access

    Article

    1H, 15N and 13C Resonance Assignments of a Protein Involved in the Autophagy Process, At4g21980.1 from Arabidopsis thaliana

    Young Kee Chae, Kyunghee Lee, John L. Markley in Journal of Biomolecular NMR (2005)

  5. No Access

    Article

    Letter to the Editor: Assignment of 1H, 13C and 15N NMR signals in the toluene 4-monooxygenase effector protein

    Hikaru Hemmi, Joey M. Studts, Young Kee Chae… in Journal of Biomolecular NMR (2000)

  6. No Access

    Chapter

    NMR Approaches to the Study of Structure-Function Relationships in Iron-Sulfur Proteins

    Newer NMR methods, particularly in conjunction with stable isotope labeling (with 2H, 13C, and 15N), offer powerful approaches to the elucidation of structure-function relationships in paramagnetic proteins such ...

    John L. Markley, Bin **a, Young Kee Chae… in Protein Structure — Function Relationship (1996)

  7. No Access

    Chapter

    Iron-Sulfur Proteins: Investigations of Hyperfine-Shifted Hydrogen, Carbon, and Nitrogen Resonances

    Iron-sulfur proteins are present in almost all living organisms. They are characterized by one or more iron ions ligated to inorganic sulfur and/or cysteine sulfur. Rubredoxin-type clusters contain a single ir...

    Bin **a, Hong Cheng, Young Kee Chae… in NMR as a Structural Tool for Macromolecules (1996)

  8. No Access

    Chapter

    Multinuclear Magnetic Resonance and Mutagenesis Studies of Structure-Function Relationships in [2Fe-2S] Ferredoxins

    Iron-sulfur proteins are present in virtually all living organisms. Their function is to transfer electrons to various partners. They have iron and sulfur in their chromophore and rather low molecular weights ...

    Young Kee Chae, Bin **a, Hong Cheng… in Nuclear Magnetic Resonance of Paramagnetic… (1995)

  9. No Access

    Article

    Structure-function studies of [2Fe-2S] ferredoxins

    The ability to overexpress [2Fe-2S] ferredoxins inEscherichia coli has opened up exciting research opportunities. High-resolution x-ray structures have been determined for the wild-type ferredoxins produced by th...

    Hazel M. Holden, Bruce L. Jacobson… in Journal of Bioenergetics and Biomembranes (1994)