{
    "abstract": "Metallothioneins (MTs) are small cysteine-rich proteins that preferentially bind d",
    "authors": [
        {
            "affiliation": "Department of Chemistry, University of Zurich, Zurich, Switzerland.",
            "firstname": "Rukmal",
            "initials": "R",
            "lastname": "Karunaratne"
        },
        {
            "affiliation": "Department of Evolutionary Anthropology, University of Zurich, Zurich, Switzerland.",
            "firstname": "Erik P",
            "initials": "EP",
            "lastname": "Willems"
        },
        {
            "affiliation": "Department of Chemistry, University of Zurich, Zurich, Switzerland.",
            "firstname": "Oliver",
            "initials": "O",
            "lastname": "Zerbe"
        },
        {
            "affiliation": "Department of Chemistry, University of Zurich, Zurich, Switzerland. Electronic address: freisinger@chem.uzh.ch.",
            "firstname": "Eva",
            "initials": "E",
            "lastname": "Freisinger"
        }
    ],
    "conclusions": null,
    "copyrights": "Copyright \u00a9 2025 The Authors. Published by Elsevier Inc. All rights reserved.",
    "doi": "10.1016/j.jinorgbio.2025.112931",
    "journal": "Journal of inorganic biochemistry",
    "keywords": [
        "Histidine",
        "Metalation pathway",
        "Metallothionein",
        "NMR",
        "Wheat",
        "Zinc"
    ],
    "methods": null,
    "publication_date": "2025-04-27",
    "pubmed_id": "40286534",
    "results": null,
    "title": "Elucidating the metalation pathway of the E",
    "xml": "<Element 'PubmedArticle' at 0x78850356b560>"
}