{"entity": "journal", "iuid": "480b347f02ff4392b74a9aa1cbefa176", "timestamp": "2026-08-17T17:05:17.615Z", "links": {"self": {"href": "https://publications.scilifelab.se/journal/Biochimie.json"}, "display": {"href": "https://publications.scilifelab.se/journal/Biochimie"}}, "title": "Biochimie", "issn": "1638-6183", "issn-l": "0300-9084", "publications_count": 2, "publications": [{"entity": "publication", "iuid": "adf91460a7004b998f82c1bc861fb29e", "links": {"self": {"href": "https://publications.scilifelab.se/publication/adf91460a7004b998f82c1bc861fb29e.json"}, "display": {"href": "https://publications.scilifelab.se/publication/adf91460a7004b998f82c1bc861fb29e"}}, "title": "Robust approach for production of the human oncology target Aurora kinase B in complex with its binding partner INCENP.", "authors": [{"family": "Mattsson", "given": "Jonna", "initials": "J"}, {"family": "Rogne", "given": "Per", "initials": "P"}, {"family": "Landstr\u00f6m", "given": "Mar\u00e9ne", "initials": "M"}, {"family": "Wolf-Watz", "given": "Magnus", "initials": "M"}], "type": "journal article", "published": "2025-02-00", "journal": {"title": "Biochimie", "issn": "1638-6183", "volume": "229", "pages": "129-140", "issn-l": "0300-9084"}, "abstract": "Protein kinases are key players in many eukaryotic signal transduction cascades and are as a result often linked to human disease. In humans, the mitotic protein kinase family of Aurora kinases consist of three members: Aurora A, B and C. All three members are involved in cell division with proposed implications in various human cancers. The human Aurora kinase B has in particular proven challenging to study with structural biology approaches, and this is mainly due to difficulties in producing the large quantities of active enzyme required for such studies. Here, we present a novel and E. coli-based production system that allows for production of milligram quantities of well-folded and active human Aurora B in complex with its binding partner INCENP. The complex is produced as a continuous polypeptide chain and the resulting fusion protein is cleaved with TEV protease to generate a stable and native heterodimer of the Aurora B:INCENP complex. The activity, stability and degree of phosphorylation of the protein complex was quantified by using a coupled ATPase assay, 31P NMR spectroscopy and mass spectrometry. The developed production system enables isotope labeling and we here report the first 1H-15N-HSQC of the human Aurora B:INCENP complex. Our developed production strategy paves the way for future structural and functional studies of Aurora B and can as such assist the development of novel anticancer drugs targeting this important mitotic protein kinase.", "doi": "10.1016/j.biochi.2024.10.011", "pmid": "39424257", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pii", "key": "S0300-9084(24)00237-2"}], "notes": [], "created": "2024-11-13T19:36:45.131Z", "modified": "2025-10-17T13:03:52.415Z"}, {"entity": "publication", "iuid": "8f1f5f83cc66414e91e2a2c85d583587", "links": {"self": {"href": "https://publications.scilifelab.se/publication/8f1f5f83cc66414e91e2a2c85d583587.json"}, "display": {"href": "https://publications.scilifelab.se/publication/8f1f5f83cc66414e91e2a2c85d583587"}}, "title": "Probing the folding pathways of four-stranded intercalated cytosine-rich motifs at single base-pair resolution.", "authors": [{"family": "Jamroskovic", "given": "Jan", "initials": "J"}, {"family": "Deiana", "given": "Marco", "initials": "M"}, {"family": "Sabouri", "given": "Nasim", "initials": "N"}], "type": "journal article", "published": "2022-08-00", "journal": {"title": "Biochimie", "issn": "1638-6183", "volume": "199", "pages": "81-91", "issn-l": "0300-9084"}, "abstract": "Cytosine-rich DNA can fold into four-stranded intercalated structures called i-motifs (iMs) under acidic conditions through the formation of hemi-protonated C:C+ base pairs. However, the folding and stability of iMs rely on many other factors that are not yet fully understood. Here, we combined biochemical and biophysical approaches to determine the factors influencing iM stability under a wide range of experimental conditions. By using high-resolution primer extension assays, circular dichroism, and absorption spectroscopies, we demonstrate that the stabilities of three different biologically relevant iMs are not dependent on molecular crowding agents. Instead, some of the crowding agents affected overall DNA synthesis. We also tested a range of small molecules to determine their effect on iM stabilization at physiological temperature and demonstrated that the G-quadruplex-specific molecule CX-5461 is also a promising candidate for selective iM stabilization. This work provides important insights into the requirements needed for different assays to accurately study iM stabilization, which will serve as important tools for understanding the contribution of iMs in cell regulation and their potential as therapeutic targets.", "doi": "10.1016/j.biochi.2022.04.007", "pmid": "35452743", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pii", "key": "S0300-9084(22)00102-X"}], "notes": [], "created": "2022-08-31T14:03:19.955Z", "modified": "2025-10-17T13:03:54.697Z"}], "created": "2020-01-23T13:01:00.237Z", "modified": "2020-11-27T13:14:06.237Z"}