{"entity": "researcher", "timestamp": "2026-09-23T16:41:10.951Z", "family": "Sch\u00fcler", "given": "Herwig", "initials": "H", "orcid": "0000-0003-4059-3501", "affiliations": ["Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/6a66d04210ea41c2bbb0a5ee187c7b76.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/6a66d04210ea41c2bbb0a5ee187c7b76"}}, "publications": [{"entity": "publication", "iuid": "c28fb876d1334187af97136f2fff26d0", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/c28fb876d1334187af97136f2fff26d0.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/c28fb876d1334187af97136f2fff26d0"}}, "title": "System-wide identification and prioritization of enzyme substrates by thermal analysis.", "authors": [{"family": "Saei", "given": "Amir Ata", "initials": "AA", "orcid": "0000-0002-2639-6328", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ebf703f0f2d44b14846ea1d9811b6e0d.json"}}, {"family": "Beusch", "given": "Christian M", "initials": "CM", "orcid": "0000-0001-9100-8283", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/fbb4771768354080ab5292c96fee0812.json"}}, {"family": "Sabatier", "given": "Pierre", "initials": "P", "orcid": "0000-0002-2734-1791", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c4cf83f2cf534d7eb308dab89d6460e2.json"}}, {"family": "Wells", "given": "Juan Astorga", "initials": "JA", "orcid": "0000-0003-1017-8841", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/855ef6e5db6f4791a52eeae9ffb95a30.json"}}, {"family": "Gharibi", "given": "Hassan", "initials": "H", "orcid": "0000-0002-3072-4929", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5825ec93851a42618425b67a5bbfbf3f.json"}}, {"family": "Meng", "given": "Zhaowei", "initials": "Z"}, {"family": "Chernobrovkin", "given": "Alexey", "initials": "A", "orcid": "0000-0001-7709-0161", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/011675da8d7a4fd68fbe5ce03227978d.json"}}, {"family": "Rodin", "given": "Sergey", "initials": "S"}, {"family": "N\u00e4reoja", "given": "Katja", "initials": "K"}, {"family": "Thorsell", "given": "Ann-Gerd", "initials": "AG"}, {"family": "Karlberg", "given": "Tobias", "initials": "T"}, {"family": "Cheng", "given": "Qing", "initials": "Q"}, {"family": "Lundstr\u00f6m", "given": "Susanna L", "initials": "SL"}, {"family": "Gaetani", "given": "Massimiliano", "initials": "M", "orcid": "0000-0001-5610-0797", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a402c63fbe4f478daa286177f031b923.json"}}, {"family": "V\u00e9gv\u00e1ri", "given": "\u00c1kos", "initials": "\u00c1", "orcid": "0000-0002-1287-0906", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/724d65ef088147c4988093b2b6b5f318.json"}}, {"family": "Arn\u00e9r", "given": "Elias S J", "initials": "ESJ", "orcid": "0000-0002-4807-6114", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/3502128dcae54dfcb6808356694bf4dc.json"}}, {"family": "Sch\u00fcler", "given": "Herwig", "initials": "H", "orcid": "0000-0003-4059-3501", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6a66d04210ea41c2bbb0a5ee187c7b76.json"}}, {"family": "Zubarev", "given": "Roman A", "initials": "RA", "orcid": "0000-0001-9839-2089", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5e3f9910c1ff434c8056bdecf537e9ef.json"}}], "type": "journal article", "published": "2021-02-26", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "12", "issue": "1", "pages": "1296", "issn-l": "2041-1723"}, "abstract": "Despite the immense importance of enzyme-substrate reactions, there is a lack of general and unbiased tools for identifying and prioritizing substrate proteins that are modified by the enzyme on the structural level. Here we describe a high-throughput unbiased proteomics method called System-wide Identification and prioritization of Enzyme Substrates by Thermal Analysis (SIESTA). The approach assumes that the enzymatic post-translational modification of substrate proteins is likely to change their thermal stability. In our proof-of-concept studies, SIESTA successfully identifies several known and novel substrate candidates for selenoprotein thioredoxin reductase 1, protein kinase B (AKT1) and poly-(ADP-ribose) polymerase-10 systems. Wider application of SIESTA can enhance our understanding of the role of enzymes in homeostasis and disease, opening opportunities to investigate the effect of post-translational modifications on signal transduction and facilitate drug discovery.", "doi": "10.1038/s41467-021-21540-6", "pmid": "33637753", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC7910609"}, {"db": "pii", "key": "10.1038/s41467-021-21540-6"}], "notes": [], "created": "2026-09-23T08:34:01.574Z", "modified": "2026-09-23T08:34:01.919Z"}]}