{"entity": "researcher", "timestamp": "2026-10-05T21:00:36.367Z", "family": "Georgoulia", "given": "Panagiota S", "initials": "PS", "orcid": "0000-0003-4573-8052", "affiliations": ["Department of Chemistry and Molecular Biology University of Gothenburg  Box 465 40530 Gothenburg Sweden"], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/419e2b2c66404881b3e7a51dbd47fcdb.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/419e2b2c66404881b3e7a51dbd47fcdb"}}, "publications": [{"entity": "publication", "iuid": "77ec4343e81c4bb68aa465ead425bf05", "links": {"self": {"href": "https://publications.scilifelab.se/publication/77ec4343e81c4bb68aa465ead425bf05.json"}, "display": {"href": "https://publications.scilifelab.se/publication/77ec4343e81c4bb68aa465ead425bf05"}}, "title": "Unambiguous Tracking of Protein Phosphorylation by Fast High-Resolution FOSY NMR*.", "authors": [{"family": "Lesovoy", "given": "Dmitry M", "initials": "DM", "orcid": "0000-0002-9130-715X", "researcher": {"href": "https://publications.scilifelab.se/researcher/2e31406b34f542d9969a828f705fa6e6.json"}}, {"family": "Georgoulia", "given": "Panagiota S", "initials": "PS", "orcid": "0000-0003-4573-8052", "researcher": {"href": "https://publications.scilifelab.se/researcher/419e2b2c66404881b3e7a51dbd47fcdb.json"}}, {"family": "Diercks", "given": "Tammo", "initials": "T", "orcid": "0000-0002-5200-0905", "researcher": {"href": "https://publications.scilifelab.se/researcher/f393c6609cf54b048585e7e11599df84.json"}}, {"family": "Mate\u010dko-Burmann", "given": "Irena", "initials": "I", "orcid": "0000-0001-8873-8381", "researcher": {"href": "https://publications.scilifelab.se/researcher/b8f4fca92f6143aea4378e5e081339ca.json"}}, {"family": "Burmann", "given": "Bj\u00f6rn M", "initials": "BM", "orcid": "0000-0002-3135-7964", "researcher": {"href": "https://publications.scilifelab.se/researcher/b7a6d61fc1a64677874973c3247b1eb4.json"}}, {"family": "Bocharov", "given": "Eduard V", "initials": "EV", "orcid": "0000-0002-3635-1609", "researcher": {"href": "https://publications.scilifelab.se/researcher/8bd226b1e4f04add992f2791b1735202.json"}}, {"family": "Bermel", "given": "Wolfgang", "initials": "W"}, {"family": "Orekhov", "given": "Vladislav Y", "initials": "VY", "orcid": "0000-0002-7892-6896", "researcher": {"href": "https://publications.scilifelab.se/researcher/77382c412de04fa08ff7c3bc7087b77e.json"}}], "type": "journal article", "published": "2021-10-25", "journal": {"title": "Angew. Chem. Int. Ed. Engl.", "issn": "1521-3773", "volume": "60", "issue": "44", "pages": "23540-23544", "issn-l": "1433-7851"}, "abstract": "Dysregulation of post-translational modifications (PTMs) like phosphorylation is often involved in disease. NMR may elucidate exact loci and time courses of PTMs at atomic resolution and near-physiological conditions but requires signal assignment to individual atoms. Conventional NMR methods for this base on tedious global signal assignment that may often fail, as for large intrinsically disordered proteins (IDPs). We present a sensitive, robust alternative to rapidly obtain only the local assignment near affected signals, based on FOcused SpectroscopY (FOSY) experiments using selective polarisation transfer (SPT). We prove its efficiency by identifying two phosphorylation sites of glycogen synthase kinase 3 beta (GSK3\u03b2) in human Tau40, an IDP of 441 residues, where the extreme spectral dispersion in FOSY revealed unprimed phosphorylation also of Ser409. FOSY may broadly benefit NMR studies of PTMs and other hotspots in IDPs, including sites involved in molecular interactions.", "doi": "10.1002/anie.202102758", "pmid": "34143912", "labels": {"Swedish NMR Centre": "Collaborative"}, "xrefs": [], "notes": [], "created": "2021-07-02T14:10:53.289Z", "modified": "2025-10-17T13:03:55.426Z"}, {"entity": "publication", "iuid": "ed9dfb96ce7b4525960909d2a2186e16", "links": {"self": {"href": "https://publications.scilifelab.se/publication/ed9dfb96ce7b4525960909d2a2186e16.json"}, "display": {"href": "https://publications.scilifelab.se/publication/ed9dfb96ce7b4525960909d2a2186e16"}}, "title": "Resolution enhancement in NMR spectra by deconvolution with compressed sensing reconstruction.", "authors": [{"family": "Kazimierczuk", "given": "Krzysztof", "initials": "K", "orcid": "0000-0001-9585-1737", "researcher": {"href": "https://publications.scilifelab.se/researcher/ad35e5f050384e6c94bc2d06066a1cf6.json"}}, {"family": "Kasprzak", "given": "Pawe\u0142", "initials": "P", "orcid": "0000-0001-7387-4284", "researcher": {"href": "https://publications.scilifelab.se/researcher/aa6e68d3b1d442efb5418ee75f8f54d0.json"}}, {"family": "Georgoulia", "given": "Panagiota S", "initials": "PS", "orcid": "0000-0003-4573-8052", "researcher": {"href": "https://publications.scilifelab.se/researcher/419e2b2c66404881b3e7a51dbd47fcdb.json"}}, {"family": "Mate\u010dko-Burmann", "given": "Irena", "initials": "I", "orcid": "0000-0001-8873-8381", "researcher": {"href": "https://publications.scilifelab.se/researcher/b8f4fca92f6143aea4378e5e081339ca.json"}}, {"family": "Burmann", "given": "Bj\u00f6rn M", "initials": "BM", "orcid": "0000-0002-3135-7964", "researcher": {"href": "https://publications.scilifelab.se/researcher/b7a6d61fc1a64677874973c3247b1eb4.json"}}, {"family": "Isaksson", "given": "Linn\u00e9a", "initials": "L"}, {"family": "Gustavsson", "given": "Emil", "initials": "E", "orcid": "0000-0003-0166-1786", "researcher": {"href": "https://publications.scilifelab.se/researcher/474b967a7726414288142c12b7b9dc3f.json"}}, {"family": "Westenhoff", "given": "Sebastian", "initials": "S", "orcid": "0000-0002-6961-8015", "researcher": {"href": "https://publications.scilifelab.se/researcher/3f1519bb234b43c6a13833b04e6720b8.json"}}, {"family": "Orekhov", "given": "Vladislav Yu", "initials": "VY", "orcid": "0000-0002-7892-6896", "researcher": {"href": "https://publications.scilifelab.se/researcher/77382c412de04fa08ff7c3bc7087b77e.json"}}], "type": "journal article", "published": "2020-12-04", "journal": {"title": "Chem. Commun. (Camb.)", "issn": "1364-548X", "volume": "56", "issue": "93", "pages": "14585-14588", "issn-l": "1359-7345"}, "abstract": "NMR spectroscopy is one of the basic tools for molecular structure elucidation. Unfortunately, the resolution of the spectra is often limited by inter-nuclear couplings. The existing workarounds often alleviate the problem by trading it for another deficiency, such as spectral artefacts or difficult sample preparation and, thus, are rarely used. We suggest an approach using the coupling deconvolution in the framework of compressed sensing (CS) spectra processing that leads to a major increase in resolution, sensitivity, and overall quality of NUS reconstruction. A new mathematical description of the decoupling by deconvolution explains the effects of thermal noise and reveals a relation with the underlying assumption of the CS. The gain in resolution and sensitivity for challenging molecular systems is demonstrated for the key HNCA experiment used for protein backbone assignment applied to two large proteins: intrinsically disordered 441-residue Tau and a 509-residue globular bacteriophytochrome fragment. The approach will be valuable in a multitude of chemistry applications, where NMR experiments are compromised by the homonuclear scalar coupling.", "doi": "10.1039/d0cc06188c", "pmid": "33146166", "labels": {"Swedish NMR Centre": "Collaborative"}, "xrefs": [], "notes": [], "created": "2020-12-11T09:16:11.124Z", "modified": "2025-10-17T13:03:56.405Z"}]}