{
  "abstract": "Inositol polyphosphates (InsPs) and inositol pyrophosphates (PP-InsPs) constitute a group of highly phosphorylated molecules that are involved in many cellular signaling processes. To characterize discrete signaling events of these structurally closely related molecules, a mass spectrometry approach was developed to derive apparent binding constants for these ligands on a proteome-wide scale. The method employed a series of chemically synthesized, biotinylated affinity reagents for inositol hexakisphosphate (InsP 6 ), and the inositol pyrophosphates 1PP-InsP 5 , 5PP-InsP 5 and 1,5(PP) 2 -InsP 4 (also termed InsP 8 ). Application of these affinity reagents at different concentrations, in combination with tandem mass tag (TMT) labeling, provided binding data for thousands of proteins from a mammalian cell lysate. Investigation of different enrichment conditions, where Mg 2+ ions were either available or not, showcased a strong influence of Mg 2+ on the protein binding capacities of PP-InsPs. Gene ontology analysis closely linked PP-InsP-interacting proteins to RNA processing in the nucleus and nucleolus. Subsequent data analysis enabled a targeted search for protein pyrophosphorylation among PP-InsP interactors, and identified four new pyrophosphorylated proteins. The data presented here constitute a valuable resource for the community, and application of the method reported here to other biological contexts will enable the exploration of PP-InsP dependent signaling pathways across species.",
  "abstract_shown": true,
  "affiliations": [
    "Institut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor-Straße 2, Berlin, Germany",
    "Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin, Germany",
    "Institut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor-Straße , 1489 Berlin, Germany",
    "Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 0, 325 Berlin, Germany",
    "Charité - Universitätsmedizin Berlin, Charitéplatz 1, 10117, Berlin, Germany",
    "Charité - Universitätsmedizin Berlin, Charitéplatz 1, Berlin, Germany",
    "Institut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor-Straße 2, Berlin, Germany. david.furkert@novartis.com",
    "Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin, Germany. david.furkert@novartis.com",
    "Institut für Chemie, Humboldt-Universität zu Berlin, Brook-Taylor-Straße 2, Berlin, Germany. fiedler@fmp-berlin.de",
    "Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, Berlin, Germany. fiedler@fmp-berlin.de"
  ],
  "article_type": null,
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "affs": [
        0,
        1,
        2,
        3
      ],
      "name": "Annika Richter"
    },
    {
      "affs": [
        1,
        3
      ],
      "name": "Jaime A. Isern",
      "orcid": "0009-0005-8004-6918"
    },
    {
      "affs": [
        1,
        2,
        3
      ],
      "name": "Max Ruwolt",
      "orcid": "0009-0000-7220-406X"
    },
    {
      "affs": [
        0,
        1,
        4,
        3
      ],
      "name": "Sarah Lampe",
      "orcid": "0009-0000-8828-640X"
    },
    {
      "affs": [
        0,
        1,
        2,
        3
      ],
      "name": "Abhirup Majumdar",
      "orcid": "0000-0002-8123-9771"
    },
    {
      "affs": [
        5,
        1,
        2,
        3
      ],
      "name": "Fan Liu",
      "orcid": "0000-0002-2358-549X"
    },
    {
      "affs": [
        6,
        7
      ],
      "name": "David Furkert",
      "orcid": "0000-0002-6145-5397"
    },
    {
      "affs": [
        8,
        9
      ],
      "name": "Dorothea Fiedler",
      "orcid": "0000-0002-0798-946X"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/1xqqqb0p4tz1p.bib",
  "cited_by": 6,
  "doi": "10.1038/s41467-026-73804-8",
  "fulltext_url": null,
  "id": "1xqqqb0p4tz1p",
  "issns": [
    "2041-1723"
  ],
  "landing_url": "https://doi.org/10.1038/s41467-026-73804-8",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1607|Advanced Proteomics Techniques and Applications"
    ]
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  "openalex": "W4401236524",
  "pdf_url": null,
  "pmcid": "PMC13237142",
  "pmid": "42243085",
  "published": "2026-06-04",
  "publisher": "Nature Portfolio",
  "ris": "https://research.draconitic.com/paper/1xqqqb0p4tz1p.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T13:26:44Z",
      "native_id": "W4401236524",
      "source": "openalex",
      "url": "https://doi.org/10.1038/s41467-026-73804-8"
    }
  ],
  "subjects": [
    {
      "field": "chemistry",
      "origin": "openalex:1607|Advanced Proteomics Techniques and Applications",
      "subfield": "physical"
    }
  ],
  "title": "Proteome-wide quantification of inositol pyrophosphate-protein interactions",
  "title_text": "Proteome-wide quantification of inositol pyrophosphate-protein interactions",
  "type": "peer-reviewed",
  "updated_at": "2026-11-09T13:21:04Z",
  "url": "https://research.draconitic.com/paper/1xqqqb0p4tz1p",
  "venue": "Nature Communications",
  "versions": []
}