{"entity": "journal", "iuid": "0e396be588864bbbb749e45a45bc7fcf", "timestamp": "2026-08-23T09:28:08.403Z", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/journal/J%20Enzyme%20Inhib%20Med%20Chem.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/journal/J%20Enzyme%20Inhib%20Med%20Chem"}}, "title": "J Enzyme Inhib Med Chem", "issn": "1475-6374", "issn-l": null, "publications_count": 3, "publications": [{"entity": "publication", "iuid": "7766365baea04bbfbcaaf4f86d0e9b0d", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/7766365baea04bbfbcaaf4f86d0e9b0d.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/7766365baea04bbfbcaaf4f86d0e9b0d"}}, "title": "Selisistat, a SIRT1 inhibitor, enhances paclitaxel activity in luminal and triple-negative breast cancer: in silico, in vitro, and in vivo studies.", "authors": [{"family": "Wawruszak", "given": "Anna", "initials": "A"}, {"family": "Luszczki", "given": "Jarogniew", "initials": "J"}, {"family": "Bartuzi", "given": "Damian", "initials": "D"}, {"family": "Kalafut", "given": "Joanna", "initials": "J"}, {"family": "Okon", "given": "Estera", "initials": "E"}, {"family": "Czerwonka", "given": "Arkadiusz", "initials": "A"}, {"family": "Stepulak", "given": "Andrzej", "initials": "A"}], "type": "journal article", "published": "2025-12-00", "journal": {"title": "J Enzyme Inhib Med Chem", "issn": "1475-6374", "volume": "40", "issue": "1", "pages": "2458554", "issn-l": null}, "abstract": "Sirtuins (SIRTs) are NAD+-dependent histone deacetylases, which play a key role in cancer progression; however, their prognostic values in breast cancer (BC) remain a subject of debate and controversy. Accumulative evidence suggests that each sirtuin possesses individual character, implicating its role in the regulation of multifaceted biological functions leading to BC initiation, progression and metastasis. Selisistat (EX527) is a potent, cell permeable, highly selective SIRT1 inhibitor. In the study, the tumour-suppressive effects of the SIRT1 inhibitor EX527 (selisistat) alone and in combination with paclitaxel (PAX) in different breast cancer cell lines and zebrafish xenograft models were investigated. The type of pharmacological drug-drug interaction between EX527 and PAX was determined using the isobolographic method. EX527 and PAX used individually inhibited proliferation, induced apoptosis and caused cell cycle arrest in G1 and subG1/G2 phases. Interestingly, the combination of these compounds used in the 1:1 dose-ratio augmented all these effects (IC50add 29.52 \u00b1 3.29 - 38.45 \u00b1 5.26). The co-treatment of EX527 with PAX generated desirable additive drug-drug interaction. The simultaneous application of EX527 and PAX induced a stronger inhibition of tumour growth compared to individual treatments in zebrafish xenografts. In silico analysis revealed a protein-protein interaction pathway (SIRT1-AKT-S1PR1-GNAI1/GNAO1-Tubulin) connecting molecular targets of both ligands. To summarise, the combination of EX527 and PAX more effectively impairs breast cancer cell growth compared to individual treatments. However, further investigations are required to clarify the specific targets and molecular mechanisms underlying the activity of EX527:PAX in other preclinical models.", "doi": "10.1080/14756366.2025.2458554", "pmid": "39935420", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11823383"}], "notes": [], "created": "2026-08-21T12:04:57.802Z", "modified": "2026-08-21T12:04:57.830Z"}, {"entity": "publication", "iuid": "a578ef9689824079ac99266c5b38d096", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/a578ef9689824079ac99266c5b38d096.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/a578ef9689824079ac99266c5b38d096"}}, "title": "Novel tetrahydronaphthalen-1-yl-phenethyl ureas: synthesis and dual antibacterial-anticancer activities.", "authors": [{"family": "Akbaba", "given": "Yusuf", "initials": "Y"}, {"family": "Kac\u0131", "given": "Fatma Necmiye", "initials": "FN"}, {"family": "Arslan", "given": "Mehmet Enes", "initials": "ME"}, {"family": "G\u00f6ks\u00fc", "given": "S\u00fcleyman", "initials": "S"}, {"family": "Mardino\u011flu", "given": "Adil", "initials": "A"}, {"family": "T\u00fcrkez", "given": "Hasan", "initials": "H"}], "type": "journal article", "published": "2024-12-00", "journal": {"title": "J Enzyme Inhib Med Chem", "issn": "1475-6374", "volume": "39", "issue": "1", "pages": "2286925", "issn-l": null}, "abstract": "Cancer and antibiotic-resistant bacterial infections are significant global health challenges. The resistance developed in cancer treatments intensifies therapeutic difficulties. In addressing these challenges, this study synthesised a series of N,N'-dialkyl urea derivatives containing methoxy substituents on phenethylamines. Using isocyanate for the efficient synthesis yielded target products 14-18 in 73-76% returns. Subsequently, their antibacterial and anticancer potentials were assessed. Cytotoxicity tests on cancer cell lines, bacterial strains, and a healthy fibroblast line revealed promising outcomes. All derivatives demonstrated robust antibacterial activity, with MIC values ranging from 0.97 to 15.82 \u00b5M. Notably, compounds 14 and 16 were particularly effective against the HeLa cell line, while compounds 14, 15, and 17 showed significant activity against the SH-SY5Y cell line. Importantly, these compounds had reduced toxicity to healthy fibroblast cells than to cancer cells, suggesting their potential as dual-functioning agents targeting both cancer and bacterial infections.", "doi": "10.1080/14756366.2023.2286925", "pmid": "38062550", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC11721939"}], "notes": [], "created": "2026-08-20T09:36:38.833Z", "modified": "2026-08-20T09:36:38.898Z"}, {"entity": "publication", "iuid": "1634cde677374aa7be15d67256b9b8c2", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/1634cde677374aa7be15d67256b9b8c2.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/1634cde677374aa7be15d67256b9b8c2"}}, "title": "Identification of histone deacetylase inhibitors with (arylidene)aminoxy scaffold active in uveal melanoma cell lines.", "authors": [{"family": "Nencetti", "given": "Susanna", "initials": "S"}, {"family": "Cuffaro", "given": "Doretta", "initials": "D"}, {"family": "Nuti", "given": "Elisa", "initials": "E", "orcid": "0000-0003-2669-5376", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/03e09baf8fc24cb5a474944ad47713f9.json"}}, {"family": "Ciccone", "given": "Lidia", "initials": "L", "orcid": "0000-0002-2762-1929", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/d242bab0e6c14f42b2bd6e7ab2d3108b.json"}}, {"family": "Rossello", "given": "Armando", "initials": "A", "orcid": "0000-0002-6795-8091", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/99958795e59648d286da609ce36c3955.json"}}, {"family": "Fabbi", "given": "Marina", "initials": "M"}, {"family": "Ballante", "given": "Flavio", "initials": "F"}, {"family": "Ortore", "given": "Gabriella", "initials": "G"}, {"family": "Carbotti", "given": "Grazia", "initials": "G"}, {"family": "Campelli", "given": "Francesco", "initials": "F"}, {"family": "Banti", "given": "Irene", "initials": "I"}, {"family": "Gangemi", "given": "Rosaria", "initials": "R"}, {"family": "Marshall", "given": "Garland R", "initials": "GR"}, {"family": "Orlandini", "given": "Elisabetta", "initials": "E"}], "type": "journal article", "published": "2021-12-00", "journal": {"title": "J Enzyme Inhib Med Chem", "issn": "1475-6374", "volume": "36", "issue": "1", "pages": "34-47", "issn-l": null}, "abstract": "Uveal melanoma (UM) represents an aggressive type of cancer and currently, there is no effective treatment for this metastatic disease. In the last years, histone deacetylase inhibitors (HDACIs) have been studied as a possible therapeutic treatment for UM, alone or in association with other chemotherapeutic agents. Here we synthesised a series of new HDACIs based on the SAHA scaffold bearing an (arylidene)aminoxy moiety. Their HDAC inhibitory activity was evaluated on isolated human HDAC1, 3, 6, and 8 by fluorometric assay and their binding mode in the catalytic site of HDACs was studied by molecular docking. The most promising hit was the quinoline derivative VS13, a nanomolar inhibitor of HDAC6, which exhibited a good antiproliferative effect on UM cell lines at micromolar concentration and a capability to modify the mRNA levels of HDAC target genes similar to that of SAHA.", "doi": "10.1080/14756366.2020.1835883", "pmid": "33100043", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC7594840"}], "notes": [], "created": "2026-08-21T12:04:55.519Z", "modified": "2026-08-21T12:04:55.702Z"}], "created": "2026-08-20T09:36:38.863Z", "modified": "2026-08-20T09:36:38.863Z"}