{"entity": "researcher", "timestamp": "2026-08-20T20:48:58.727Z", "family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "affiliations": ["Department of Medicine Solna, Science for Life Laboratory, Karolinska Institute Solna, Solna, Sweden."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815"}}, "publications": [{"entity": "publication", "iuid": "2108b46955d444a39235fed52f4243dc", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/2108b46955d444a39235fed52f4243dc.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/2108b46955d444a39235fed52f4243dc"}}, "title": "Mutational insights into human kynurenine aminotransferase 1: modulation of transamination and \u03b2-elimination activities across diverse substrates.", "authors": [{"family": "Selvam", "given": "Arun Kumar", "initials": "AK", "orcid": "0000-0002-9854-2048", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/8e7a8d1d439a4ed0aebad8389a7253e2.json"}}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Razaghi", "given": "Ali", "initials": "A", "orcid": "0000-0001-8771-998X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b978f17f56764dfb8fbef3fd06d10214.json"}}, {"family": "Salter", "given": "Hugh", "initials": "H", "orcid": "0000-0001-5705-2950", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c405a1c865d34a769095ada5edc8d04b.json"}}, {"family": "Sandalova", "given": "Tatiana", "initials": "T", "orcid": "0000-0002-7694-6420", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d2ea3d2ec9e94fe3876f88bd0786c24b.json"}}, {"family": "Bj\u00f6rnstedt", "given": "Mikael", "initials": "M", "orcid": "0000-0003-2831-3837", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/08e79d991fab47c18b7390c7ddc12963.json"}}, {"family": "Achour", "given": "Adnane", "initials": "A", "orcid": "0000-0003-0432-710X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/65fba324156a4fcbafbe636e642587a9.json"}}], "type": "journal article", "published": "2025-08-18", "journal": {"title": "Biochem. J.", "issn": "1470-8728", "volume": "482", "issue": "16", "pages": "1163-1180", "issn-l": "0264-6021"}, "abstract": "Human kynurenine aminotransferase 1 (hKYAT1) plays a crucial role in the transamination of aromatic amino acids and kynurenine. This promiscuous homodimeric enzyme transaminates various amino acids into their corresponding \u03b1-keto acids. Additionally, hKYAT1 is known to catalyze the \u03b2-elimination of cysteine-S conjugates and cysteine-Se conjugates. In this study, we performed mutational analyses of hKYAT1, targeting its catalytic, ligand-binding, and substrate-binding sites. The transamination activity of 13 mutant variants was systematically evaluated against sixteen different amino acid substrates, including kynurenine, selenomethionine (SeMet), and Se-methylselenocysteine (MSC), as well as for the \u03b2-elimination of SeMet and MSC. Our results demonstrate that mutations of residues E27 in the catalytic site and H279 in the substratestabilizing site significantly enhanced the transamination of several amino acids, including phenylalanine, tryptophan, histidine, and MSC. The H279F mutation increased transamination and \u03b2-elimination of MSC by 2- and 1.5-fold, respectively. Furthermore, mutation at the ligand-binding residues R398, F125, and N185 substantially reduced MSC transamination activity of hKYAT1. Interestingly, none of the tested mutations affected the transamination of l-kynurenine, a natural substrate of hKYAT1. Altogether, these findings support future investigation into hKYAT1 as a modifiable target in selenium-mediated anticancer approaches.", "doi": "10.1042/BCJ20253178", "pmid": "40785633", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC12493182"}, {"db": "pii", "key": "236366"}], "notes": [], "created": "2026-08-20T09:28:22.125Z", "modified": "2026-08-20T09:28:22.422Z"}, {"entity": "publication", "iuid": "5003f858767a4018b4b72e7a83ccc4bf", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/5003f858767a4018b4b72e7a83ccc4bf.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/5003f858767a4018b4b72e7a83ccc4bf"}}, "title": "Solution architecture of G3BP1 reveals pH-dependent conformational switching underlying liquid-liquid phase separation", "authors": [{"family": "Han", "given": "Xiao", "initials": "X", "orcid": "0000-0003-0879-4119", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed.json"}}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Graewert", "given": "Melissa A", "initials": "MA"}, {"family": "Zhou", "given": "Qianyu", "initials": "Q"}, {"family": "Resink", "given": "Tom", "initials": "T", "orcid": "0000-0002-2851-1684", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0c147e9bc8e1457489364f54d61983a0.json"}}, {"family": "Blanchet", "given": "Clement E", "initials": "CE"}, {"family": "McInerney", "given": "Gerald", "initials": "G"}, {"family": "Alici", "given": "Evren", "initials": "E", "orcid": "0000-0001-5307-6648", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1b15e3ead7914feb86af38946f373dfb.json"}}, {"family": "Ljunggren", "given": "Hans Gustaf", "initials": "HG"}, {"family": "Farnebo", "given": "Marianne", "initials": "M"}, {"family": "Svergun", "given": "Dmitri", "initials": "D"}, {"family": "Achour", "given": "Adnane", "initials": "A"}], "type": "posted-content", "published": "2025-03-29", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2025.03.27.645651", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:01:50.979Z", "modified": "2026-08-20T11:01:51.108Z"}, {"entity": "publication", "iuid": "f84542e7ea5746209e3f0e441627ad69", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/f84542e7ea5746209e3f0e441627ad69.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/f84542e7ea5746209e3f0e441627ad69"}}, "title": "SARS-CoV-2 N protein recruits G3BP to double membrane vesicles to promote translation of viral mRNAs.", "authors": [{"family": "Long", "given": "Siwen", "initials": "S"}, {"family": "Guzyk", "given": "Mykhailo", "initials": "M"}, {"family": "Perez Vidakovics", "given": "Laura", "initials": "L", "orcid": "0000-0003-4283-812X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/309ffd38d0f54f26bbe038eb242d7e2d.json"}}, {"family": "Han", "given": "Xiao", "initials": "X"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Wang", "given": "Megan", "initials": "M", "orcid": "0000-0003-3000-3539", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/6c266ec5cfae49faa110c5b3f34b27ad.json"}}, {"family": "Panas", "given": "Marc D", "initials": "MD", "orcid": "0000-0002-7373-0341", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/de0aacc7004d4b179d37401c8636ac8f.json"}}, {"family": "Urgard", "given": "Egon", "initials": "E"}, {"family": "Coquet", "given": "Jonathan M", "initials": "JM", "orcid": "0000-0002-5967-4857", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5d8f18ddaf044bdb80d800630d137993.json"}}, {"family": "Merits", "given": "Andres", "initials": "A"}, {"family": "Achour", "given": "Adnane", "initials": "A", "orcid": "0000-0003-0432-710X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/65fba324156a4fcbafbe636e642587a9.json"}}, {"family": "McInerney", "given": "Gerald M", "initials": "GM", "orcid": "0000-0003-2257-7241", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/012d1aaf306b43dc89309b45ccc6b649.json"}}], "type": "journal article", "published": "2024-12-05", "journal": {"title": "Nat Commun", "issn": "2041-1723", "volume": "15", "issue": "1", "pages": "10607", "issn-l": "2041-1723"}, "abstract": "Ras-GTPase-activating protein SH3-domain-binding proteins (G3BP) are critical for the formation of stress granules (SGs) through their RNA- and ribosome-binding properties. SARS-CoV-2 nucleocapsid (N) protein exhibits strong binding affinity for G3BP and inhibits infection-induced SG formation soon after infection. To study the impact of the G3BP-N interaction on viral replication and pathogenesis in detail, we generated a mutant SARS-CoV-2 (RATA) that specifically lacks the G3BP-binding motif in the N protein. RATA triggers a stronger and more persistent SG response in infected cells, showing reduced replication across various cell lines, and greatly reduced pathogenesis in K18-hACE2 transgenic mice. At early times of infection, G3BP and WT N protein strongly colocalise with dsRNA and with non-structural protein 3 (nsp3), a component of the pore complex in double membrane vesicles (DMVs) from which nascent viral RNA emerges. Furthermore, G3BP-N complexes promote highly localized translation of viral mRNAs in the immediate vicinity of the DMVs and thus contribute to efficient viral gene expression and replication. In contrast, G3BP is absent from the DMVs in cells infected with RATA and translation of viral mRNAs is less efficient. This work provides a fuller understanding of the multifunctional roles of G3BP in SARS-CoV-2 infection.", "doi": "10.1038/s41467-024-54996-3", "pmid": "39638802", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11621422"}, {"db": "pii", "key": "10.1038/s41467-024-54996-3"}], "notes": [], "created": "2026-08-20T08:53:44.334Z", "modified": "2026-08-20T08:53:44.554Z"}, {"entity": "publication", "iuid": "93555e317ef54e44bd5030caa6749aa4", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/93555e317ef54e44bd5030caa6749aa4.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/93555e317ef54e44bd5030caa6749aa4"}}, "title": "High Resolution Crystal Structure of the Pyruvate Kinase Tetramer in Complex with the Allosteric Activator Mitapivat/AG-348", "authors": [{"family": "Han", "given": "Xiao", "initials": "X", "orcid": "0000-0003-0879-4119", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Zhang", "given": "Cheng", "initials": "C", "orcid": "0000-0002-3721-8586", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f46e4161be08458994efddb75ed75874.json"}}, {"family": "Mardinoglu", "given": "Adil", "initials": "A", "orcid": "0000-0002-4254-6090", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/ca58bf2d214047e0ae5e38a42a0f2808.json"}}, {"family": "Achour", "given": "Adnane", "initials": "A", "orcid": "0000-0003-0432-710X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/65fba324156a4fcbafbe636e642587a9.json"}}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}], "type": "journal-article", "published": "2024-05-05", "journal": {"title": "Crystals", "issn": "2073-4352", "volume": "14", "issue": "5", "pages": "441", "issn-l": null}, "abstract": null, "doi": "10.3390/cryst14050441", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T13:40:24.382Z", "modified": "2026-08-20T13:40:24.520Z"}, {"entity": "publication", "iuid": "8979c7df59254dd9822b926c7a0cb26a", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/8979c7df59254dd9822b926c7a0cb26a.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/8979c7df59254dd9822b926c7a0cb26a"}}, "title": "Towards understanding of allostery in MALT1: a possible role of interdomain motions as revealed by NMR and AlphaFold", "authors": [{"family": "Wallerstein", "given": "Johan", "initials": "J", "orcid": "0009-0005-9832-5210", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d318a6953cbe4263a46c9712c43bc477.json"}}, {"family": "Han", "given": "Xiao", "initials": "X"}, {"family": "Levkovets", "given": "Maria", "initials": "M", "orcid": "0000-0002-1805-9057", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5db1b8e1e0f94daba38a0b5836322f49.json"}}, {"family": "Lesovoy", "given": "Dmitry", "initials": "D", "orcid": "0000-0002-9130-715X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/706f3a39328e4e17823901ccc52b27c1.json"}}, {"family": "Malmodin", "given": "Daniel", "initials": "D", "orcid": "0000-0001-8528-0141", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/679de38a489d47c9a9225481c83624ef.json"}}, {"family": "Mirabello", "given": "Claudio", "initials": "C", "orcid": "0000-0001-7868-034X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/f4ca88bb3cf24e2591c447ec929502e6.json"}}, {"family": "Wallner", "given": "Bj\u00f6rn", "initials": "B", "orcid": "0000-0002-3772-8279", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/330342e0d01d4a0683bd6bda49064c21.json"}}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T", "orcid": "0000-0002-7694-6420", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d2ea3d2ec9e94fe3876f88bd0786c24b.json"}}, {"family": "Agback", "given": "Peter", "initials": "P"}, {"family": "Karlsson", "given": "G\u00f6ran", "initials": "G", "orcid": "0000-0002-1821-4715", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c237ffc07068465286d7b903683ed3ab.json"}}, {"family": "Achour", "given": "Adnane", "initials": "A", "orcid": "0000-0003-0432-710X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/65fba324156a4fcbafbe636e642587a9.json"}}, {"family": "Agback", "given": "Tatiana", "initials": "T", "orcid": "0000-0003-1325-6024", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/45cf38c8b15946cda75b81cde94bbdfe.json"}}, {"family": "Orekhov", "given": "Vladislav", "initials": "V", "orcid": "0000-0002-7892-6896", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/a2bf27272cbc40e7b01f24b4324f0fb2.json"}}], "type": "posted-content", "published": "2024-02-01", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/2024.02.01.578365", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T10:51:57.455Z", "modified": "2026-08-20T10:51:57.825Z"}, {"entity": "publication", "iuid": "49529f6dfbd942869ba0f99c6123c7a9", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/49529f6dfbd942869ba0f99c6123c7a9.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/49529f6dfbd942869ba0f99c6123c7a9"}}, "title": "Novel conformational filter allows unambiguous identification of specific conformational ensembles for the large NS3pro/NS2B Dengue-associated protease; Implications for the appropriate choice of protein conformations in drug discovery", "authors": [{"family": "Agback", "given": "Tatiana", "initials": "T"}, {"family": "Lesovoy", "given": "Dmitry", "initials": "D"}, {"family": "Han", "given": "Xiao", "initials": "X"}, {"family": "Lomzov", "given": "Alexander", "initials": "A"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T", "orcid": "0000-0002-7694-6420", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d2ea3d2ec9e94fe3876f88bd0786c24b.json"}}, {"family": "Orekhov", "given": "Vladislav", "initials": "V"}, {"family": "Achour", "given": "Adnane", "initials": "A"}, {"family": "Agback", "given": "Peter", "initials": "P"}], "type": "posted-content", "published": "2023-06-30", "journal": {"issn-l": null}, "abstract": null, "doi": "10.21203/rs.3.rs-3014908/v1", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T12:59:10.456Z", "modified": "2026-08-20T12:59:10.480Z"}, {"entity": "publication", "iuid": "b9199c74ab13436cb33b162ed38990cb", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/b9199c74ab13436cb33b162ed38990cb.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/b9199c74ab13436cb33b162ed38990cb"}}, "title": "Tuning antiviral CD8 T-cell response via proline-altered peptide ligand vaccination.", "authors": [{"family": "Duru", "given": "Adil Doganay", "initials": "AD"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Allerbring", "given": "Eva B", "initials": "EB", "orcid": "0000-0002-9575-0466", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4e1d21522744419bb23561be759c76b5.json"}}, {"family": "Chadderton", "given": "Jesseka", "initials": "J", "orcid": "0000-0002-2784-3556", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/0eb3a07ef04c4ef0b79629452bbd0bd9.json"}}, {"family": "Kadri", "given": "Nadir", "initials": "N"}, {"family": "Han", "given": "Xiao", "initials": "X"}, {"family": "Peqini", "given": "Kaliroi", "initials": "K"}, {"family": "Uchtenhagen", "given": "Hannes", "initials": "H", "orcid": "0000-0002-4342-1919", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/86b1228a42d4486c983058d76828cfd1.json"}}, {"family": "Madhurantakam", "given": "Chaithanya", "initials": "C"}, {"family": "Pellegrino", "given": "Sara", "initials": "S", "orcid": "0000-0002-2325-3583", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c0d6ed24c4914ce4b6cd0f699f121b52.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Nygren", "given": "Per-\u00c5ke", "initials": "P\u00c5", "orcid": "0000-0003-4214-6991", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/db3f3b9b876c486e9c8acaa5efcfff18.json"}}, {"family": "Turner", "given": "Stephen J", "initials": "SJ", "orcid": "0000-0002-1002-0000", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d6098f38a6784bf1ace7e09d718a70ec.json"}}, {"family": "Achour", "given": "Adnane", "initials": "A", "orcid": "0000-0003-0432-710X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/65fba324156a4fcbafbe636e642587a9.json"}}], "type": "journal article", "published": "2020-05-00", "journal": {"title": "PLoS Pathog", "issn": "1553-7374", "volume": "16", "issue": "5", "pages": "e1008244", "issn-l": "1553-7366"}, "abstract": "Viral escape from CD8+ cytotoxic T lymphocyte responses correlates with disease progression and represents a significant challenge for vaccination. Here, we demonstrate that CD8+ T cell recognition of the naturally occurring MHC-I-restricted LCMV-associated immune escape variant Y4F is restored following vaccination with a proline-altered peptide ligand (APL). The APL increases MHC/peptide (pMHC) complex stability, rigidifies the peptide and facilitates T cell receptor (TCR) recognition through reduced entropy costs. Structural analyses of pMHC complexes before and after TCR binding, combined with biophysical analyses, revealed that although the TCR binds similarly to all complexes, the p3P modification alters the conformations of a very limited amount of specific MHC and peptide residues, facilitating efficient TCR recognition. This approach can be easily introduced in peptides restricted to other MHC alleles, and can be combined with currently available and future vaccination protocols in order to prevent viral immune escape.", "doi": "10.1371/journal.ppat.1008244", "pmid": "32365082", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC7224568"}, {"db": "pii", "key": "PPATHOGENS-D-19-02081"}], "notes": [], "created": "2026-08-20T12:44:43.219Z", "modified": "2026-08-20T12:44:43.362Z"}, {"entity": "publication", "iuid": "050fbe86e588405eaa7d3cf8729266bf", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/050fbe86e588405eaa7d3cf8729266bf.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/050fbe86e588405eaa7d3cf8729266bf"}}, "title": "Biochemical and biophysical comparison of human and mouse beta-2 microglobulin reveals the molecular determinants of low amyloid propensity.", "authors": [{"family": "Achour", "given": "Adnane", "initials": "A"}, {"family": "Broggini", "given": "Luca", "initials": "L"}, {"family": "Han", "given": "Xiao", "initials": "X"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Santambrogio", "given": "Carlo", "initials": "C"}, {"family": "Buratto", "given": "Jeremie", "initials": "J"}, {"family": "Visentin", "given": "Cristina", "initials": "C"}, {"family": "Barbiroli", "given": "Alberto", "initials": "A"}, {"family": "De Luca", "given": "Chiara Maria Giulia", "initials": "CMG"}, {"family": "Sormanni", "given": "Pietro", "initials": "P"}, {"family": "Moda", "given": "Fabio", "initials": "F"}, {"family": "De Simone", "given": "Alfonso", "initials": "A"}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Grandori", "given": "Rita", "initials": "R"}, {"family": "Camilloni", "given": "Carlo", "initials": "C"}, {"family": "Ricagno", "given": "Stefano", "initials": "S", "orcid": "0000-0001-6678-5873", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/98daac35c7914d1584403a45a81bd8c4.json"}}], "type": "journal article", "published": "2020-02-00", "journal": {"title": "FEBS J.", "issn": "1742-4658", "volume": "287", "issue": "3", "pages": "546-560", "issn-l": "1742-464X"}, "abstract": "The molecular bases of amyloid aggregation propensity are still poorly understood, especially for proteins that display a stable folded native structure. A prototypic example is human beta-2 microglobulin (\u03b22m), which, when accumulated in patients, gives rise to dialysis-related amyloidosis. Interestingly, although the physiologic concentration of \u03b22m in mice is five times higher than that found in human patients, no amyloid deposits are observed in mice. Moreover, murine \u03b22m (m\u03b22m) not only displays a lower amyloid propensity both in vivo and in vitro but also inhibits the aggregation of human \u03b22m in vitro. Here, we compared human and m\u03b22m for their aggregation propensity, ability to form soluble oligomers, stability, three-dimensional structure and dynamics. Our results indicate that m\u03b22m low-aggregation propensity is due to two concomitant aspects: the low-aggregation propensity of its primary sequence combined with the absence of high-energy amyloid-competent conformations under native conditions. The identification of the specific properties determining the low-aggregation propensity of mouse \u03b22m will help delineate the molecular risk factors which cause a folded protein to aggregate.", "doi": "10.1111/febs.15046", "pmid": "31420997", "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:17:54.399Z", "modified": "2026-08-20T11:17:54.477Z"}, {"entity": "publication", "iuid": "1055a6a0b35b492e97418386361864f9", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1055a6a0b35b492e97418386361864f9.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1055a6a0b35b492e97418386361864f9"}}, "title": "Tuning antiviral CD8 T-cell response via proline-altered peptide ligand vaccination", "authors": [{"family": "Duru", "given": "Adil Doganay", "initials": "AD"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Allerbring", "given": "Eva B", "initials": "EB", "orcid": "0000-0002-9575-0466", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4e1d21522744419bb23561be759c76b5.json"}}, {"family": "Chadderton", "given": "Jesseka", "initials": "J"}, {"family": "Kadri", "given": "Nadir", "initials": "N"}, {"family": "Han", "given": "Xiao", "initials": "X"}, {"family": "Uchtenhagen", "given": "Hannes", "initials": "H", "orcid": "0000-0002-4342-1919", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/86b1228a42d4486c983058d76828cfd1.json"}}, {"family": "Madhurantakam", "given": "Chaithanya", "initials": "C"}, {"family": "Pellegrino", "given": "Sara", "initials": "S", "orcid": "0000-0002-2325-3583", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/c0d6ed24c4914ce4b6cd0f699f121b52.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Nygren", "given": "Per \u00c5ke", "initials": "P\u00c5", "orcid": "0000-0003-4214-6991", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/db3f3b9b876c486e9c8acaa5efcfff18.json"}}, {"family": "Turner", "given": "Stephen J", "initials": "SJ", "orcid": "0000-0002-1002-0000", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d6098f38a6784bf1ace7e09d718a70ec.json"}}, {"family": "Achour", "given": "Adnane", "initials": "A", "orcid": "0000-0003-0432-710X", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/65fba324156a4fcbafbe636e642587a9.json"}}], "type": "posted-content", "published": "2019-12-02", "journal": {"issn-l": null}, "abstract": null, "doi": "10.1101/862144", "pmid": null, "labels": [], "xrefs": [], "notes": [], "created": "2026-08-20T11:15:31.089Z", "modified": "2026-08-20T11:15:31.236Z"}, {"entity": "publication", "iuid": "e00b7b7acc294b5fb8c84f0631bba0b9", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/e00b7b7acc294b5fb8c84f0631bba0b9.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/e00b7b7acc294b5fb8c84f0631bba0b9"}}, "title": "14-3-3 scaffold proteins mediate the inactivation of trim25 and inhibition of the type I interferon response by herpesvirus deconjugases.", "authors": [{"family": "Gupta", "given": "Soham", "initials": "S", "orcid": "0000-0003-1136-3010", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/1d5cddb6da03462189049a2ca72f0e66.json"}}, {"family": "Yl\u00e4-Anttila", "given": "P\u00e4ivi", "initials": "P", "orcid": "0000-0002-5794-5094", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/60ff8f7881314618a9d400699d5e329f.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Achour", "given": "Adnane", "initials": "A"}, {"family": "Masucci", "given": "Maria G", "initials": "MG", "orcid": "0000-0002-5541-2809", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/9ac1411f252f403485d658f2c74204f0.json"}}], "type": "journal article", "published": "2019-11-00", "journal": {"title": "PLoS Pathog", "issn": "1553-7374", "volume": "15", "issue": "11", "pages": "e1008146", "issn-l": "1553-7366"}, "abstract": "The 14-3-3 molecular scaffolds promote type I interferon (IFN) responses by stabilizing the interaction of RIG-I with the TRIM25 ligase. Viruses have evolved unique strategies to halt this cellular response to support their replication and spread. Here, we report that the ubiquitin deconjugase (DUB) encoded in the N-terminus of the Epstein-Barr virus (EBV) large tegument protein BPLF1 harnesses 14-3-3 molecules to promote TRIM25 autoubiquitination and sequestration of the ligase into inactive protein aggregates. Catalytically inactive BPLF1 induced K48-linked autoubiquitination and degradation of TRIM25 while the ligase was mono- or di-ubiquitinated in the presence of the active viral enzyme and formed cytosolic aggregates decorated by the autophagy receptor p62/SQSTM1. Aggregate formation and the inhibition of IFN response were abolished by mutations of solvent exposed residues in helix-2 of BPLF1 that prevented binding to 14-3-3 while preserving both catalytic activity and binding to TRIM25. 14-3-3 interacted with the Coiled-Coil (CC) domain of TRIM25 in in vitro pulldown, while BPLF1 interacted with both the CC and B-box domains, suggesting that 14-3-3 positions BPLF1 at the ends of the CC dimer, close to known autoubiquitination sites. Our findings provide a molecular understanding of the mechanism by which a viral deubiquitinase inhibits the IFN response and emphasize the role of 14-3-3 proteins in modulating antiviral defenses.", "doi": "10.1371/journal.ppat.1008146", "pmid": "31710640", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6874091"}, {"db": "pii", "key": "PPATHOGENS-D-19-01153"}], "notes": [], "created": "2026-08-20T12:44:41.459Z", "modified": "2026-08-20T12:44:41.524Z"}, {"entity": "publication", "iuid": "c84f34304d684326a7455384401c79b6", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/c84f34304d684326a7455384401c79b6.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/c84f34304d684326a7455384401c79b6"}}, "title": "Successive crystal structure snapshots suggest the basis for MHC class I peptide loading and editing by tapasin.", "authors": [{"family": "Hafstrand", "given": "Ida", "initials": "I", "orcid": "0000-0002-1012-9532", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/30b0065eee584566a6d75a1df61c0836.json"}}, {"family": "Sayitoglu", "given": "Ece Canan", "initials": "EC"}, {"family": "Apavaloaei", "given": "Anca", "initials": "A", "orcid": "0000-0001-6896-1199", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/456edb69e56f47b4b9992e5d07994c6e.json"}}, {"family": "Josey", "given": "Benjamin John", "initials": "BJ"}, {"family": "Sun", "given": "Renhua", "initials": "R", "orcid": "0000-0002-8203-4946", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/29b44e08db3a4482a6a40bbda52fe815.json"}}, {"family": "Han", "given": "Xiao", "initials": "X", "orcid": "0000-0003-0879-4119", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/84f84bbd0b5a4d86b5512581773446ed.json"}}, {"family": "Pellegrino", "given": "Sara", "initials": "S"}, {"family": "Ozkazanc", "given": "Didem", "initials": "D"}, {"family": "Potens", "given": "Ren\u00e9e", "initials": "R"}, {"family": "Janssen", "given": "Linda", "initials": "L"}, {"family": "Nilvebrant", "given": "Johan", "initials": "J", "orcid": "0000-0002-6104-6446", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/5cd15a9b2af64e4b977d064bacad0330.json"}}, {"family": "Nygren", "given": "Per-\u00c5ke", "initials": "P\u00c5", "orcid": "0000-0003-4214-6991", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/db3f3b9b876c486e9c8acaa5efcfff18.json"}}, {"family": "Sandalova", "given": "Tatyana", "initials": "T"}, {"family": "Springer", "given": "Sebastian", "initials": "S", "orcid": "0000-0002-5527-6149", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/4b53dfef715d45569df53ba2bae9cc84.json"}}, {"family": "Georgoudaki", "given": "Anna-Maria", "initials": "AM"}, {"family": "Duru", "given": "Adil Doganay", "initials": "AD"}, {"family": "Achour", "given": "Adnane", "initials": "A"}], "type": "journal article", "published": "2019-03-12", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "116", "issue": "11", "pages": "5055-5060", "issn-l": "0027-8424"}, "abstract": "MHC-I epitope presentation to CD8+ T cells is directly dependent on peptide loading and selection during antigen processing. However, the exact molecular bases underlying peptide selection and binding by MHC-I remain largely unknown. Within the peptide-loading complex, the peptide editor tapasin is key to the selection of MHC-I-bound peptides. Here, we have determined an ensemble of crystal structures of MHC-I in complex with the peptide exchange-associated dipeptide GL, as well as the tapasin-associated scoop loop, alone or in combination with candidate epitopes. These results combined with mutation analyses allow us to propose a molecular model underlying MHC-I peptide selection by tapasin. The N termini of bound peptides most probably bind first in the N-terminal and middle region of the MHC-I peptide binding cleft, upon which the peptide C termini are tested for their capacity to dislodge the tapasin scoop loop from the F pocket of the MHC-I cleft. Our results also indicate important differences in peptide selection between different MHC-I alleles.", "doi": "10.1073/pnas.1807656116", "pmid": "30808808", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC6421438"}, {"db": "pii", "key": "1807656116"}, {"db": "PDB", "key": "6GB7"}, {"db": "PDB", "key": "6GB5"}, {"db": "PDB", "key": "6GB6"}], "notes": [], "created": "2026-08-20T09:29:48.827Z", "modified": "2026-08-20T09:29:49.027Z"}]}