{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,3]],"date-time":"2026-02-03T09:17:08Z","timestamp":1770110228444,"version":"3.49.0"},"reference-count":63,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,1,21]],"date-time":"2026-01-21T00:00:00Z","timestamp":1768953600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000001","name":"Alberta Cancer Foundation","doi-asserted-by":"publisher","award":["27364"],"award-info":[{"award-number":["27364"]}],"id":[{"id":"10.13039\/501100000001","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000196","name":"Canada Foundation for Innovation","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000196","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN-2019-04967"],"award-info":[{"award-number":["RGPIN-2019-04967"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN-2019-04504"],"award-info":[{"award-number":["RGPIN-2019-04504"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100000024","name":"Canadian Institutes of Health Research","doi-asserted-by":"publisher","award":["178282"],"award-info":[{"award-number":["178282"]}],"id":[{"id":"10.13039\/501100000024","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100019691","name":"Faculty of Medicine and Dentistry, University of Alberta","doi-asserted-by":"publisher","award":["SCR_019200"],"award-info":[{"award-number":["SCR_019200"]}],"id":[{"id":"10.13039\/501100019691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2026,3]]},"DOI":"10.1016\/j.bioorg.2026.109522","type":"journal-article","created":{"date-parts":[[2026,1,18]],"date-time":"2026-01-18T22:47:15Z","timestamp":1768776435000},"page":"109522","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Novel Hsp90 inhibitors as leads for the development of radiotheragnostics for Meitner-Auger electron therapy"],"prefix":"10.1016","volume":"170","author":[{"given":"Alexandra K.","family":"Kennedy","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Miguel Angel","family":"Herrera-Rueda","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reese","family":"Wilby","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Frank","family":"Wuest","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Paul","family":"LaPointe","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"2","key":"10.1016\/j.bioorg.2026.109522_bb0005","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1017\/S0033583510000314","article-title":"Conformational dynamics of the molecular chaperone Hsp90","volume":"44","author":"Krukenberg","year":"2011","journal-title":"Q. Rev. Biophys."},{"issue":"5","key":"10.1016\/j.bioorg.2026.109522_bb0010","doi-asserted-by":"crossref","first-page":"987","DOI":"10.1016\/j.cell.2012.06.047","article-title":"Quantitative analysis of HSP90-client interactions reveals principles of substrate recognition","volume":"150","author":"Taipale","year":"2012","journal-title":"Cell"},{"issue":"8","key":"10.1016\/j.bioorg.2026.109522_bb0015","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1038\/nrc2887","article-title":"Targeting the dynamic HSP90 complex in cancer","volume":"10","author":"Trepel","year":"2010","journal-title":"Nat. Rev. Cancer"},{"issue":"19","key":"10.1016\/j.bioorg.2026.109522_bb0020","doi-asserted-by":"crossref","DOI":"10.3390\/ijms221910317","article-title":"Role of HSP90 in Cancer","volume":"22","author":"Birbo","year":"2021","journal-title":"Int. J. Mol. Sci."},{"issue":"16","key":"10.1016\/j.bioorg.2026.109522_bb0025","doi-asserted-by":"crossref","first-page":"4383","DOI":"10.1093\/emboj\/19.16.4383","article-title":"The ATPase cycle of Hsp90 drives a molecular \u2018clamp\u2019 via transient dimerization of the N-terminal domains","volume":"19","author":"Prodromou","year":"2000","journal-title":"EMBO J."},{"issue":"1","key":"10.1016\/j.bioorg.2026.109522_bb0030","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/S0092-8674(00)80314-1","article-title":"Identification and structural characterization of the ATP\/ADP-binding site in the Hsp90 molecular chaperone","volume":"90","author":"Prodromou","year":"1997","journal-title":"Cell"},{"issue":"6","key":"10.1016\/j.bioorg.2026.109522_bb0035","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1038\/nsb0697-477","article-title":"A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone","volume":"4","author":"Prodromou","year":"1997","journal-title":"Nat. Struct. Biol."},{"issue":"36","key":"10.1016\/j.bioorg.2026.109522_bb0040","doi-asserted-by":"crossref","first-page":"33689","DOI":"10.1074\/jbc.M103832200","article-title":"Coordinated ATP hydrolysis by the Hsp90 dimer","volume":"276","author":"Richter","year":"2001","journal-title":"J. Biol. Chem."},{"issue":"26","key":"10.1016\/j.bioorg.2026.109522_bb0045","doi-asserted-by":"crossref","first-page":"17757","DOI":"10.1074\/jbc.M800540200","article-title":"Conserved conformational changes in the ATPase cycle of human Hsp90","volume":"283","author":"Richter","year":"2008","journal-title":"J. Biol. Chem."},{"issue":"6","key":"10.1016\/j.bioorg.2026.109522_bb0050","first-page":"670","article-title":"Binding of p23 and hsp90 during assembly with the progesterone receptor","volume":"9","author":"Johnson","year":"1995","journal-title":"Mol. Endocrinol."},{"issue":"5","key":"10.1016\/j.bioorg.2026.109522_bb0055","doi-asserted-by":"crossref","first-page":"3748","DOI":"10.1128\/MCB.19.5.3748","article-title":"Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction","volume":"19","author":"Knoblauch","year":"1999","journal-title":"Mol. Cell. Biol."},{"issue":"7893","key":"10.1016\/j.bioorg.2026.109522_bb0060","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1038\/s41586-021-04236-1","article-title":"Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism","volume":"601","author":"Noddings","year":"2022","journal-title":"Nature"},{"issue":"15","key":"10.1016\/j.bioorg.2026.109522_bb0065","doi-asserted-by":"crossref","first-page":"2303","DOI":"10.1091\/mbc.e12-12-0892","article-title":"Hsp90 cochaperones p23 and FKBP4 physically interact with hAgo2 and activate RNA interference-mediated silencing in mammalian cells","volume":"24","author":"Pare","year":"2013","journal-title":"Mol. Biol. Cell"},{"issue":"7","key":"10.1016\/j.bioorg.2026.109522_bb0070","doi-asserted-by":"crossref","first-page":"1894","DOI":"10.1016\/j.celrep.2019.07.045","article-title":"Co-chaperones TIMP2 and AHA1 competitively regulate extracellular HSP90:Client MMP2 Activity and Matrix Proteolysis","volume":"28","author":"Baker-Williams","year":"2019","journal-title":"Cell Rep."},{"issue":"6","key":"10.1016\/j.bioorg.2026.109522_bb0075","doi-asserted-by":"crossref","first-page":"1402","DOI":"10.1038\/sj.emboj.7600141","article-title":"Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery","volume":"23","author":"Meyer","year":"2004","journal-title":"EMBO J."},{"issue":"6","key":"10.1016\/j.bioorg.2026.109522_bb0080","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/S1097-2765(02)00785-2","article-title":"Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1","volume":"10","author":"Panaretou","year":"2002","journal-title":"Mol. Cell"},{"issue":"36","key":"10.1016\/j.bioorg.2026.109522_bb0085","doi-asserted-by":"crossref","first-page":"9707","DOI":"10.1073\/pnas.1707039114","article-title":"Hsp90 activator Aha1 drives production of pathological tau aggregates","volume":"114","author":"Shelton","year":"2017","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"8","key":"10.1016\/j.bioorg.2026.109522_bb0090","doi-asserted-by":"crossref","first-page":"3532","DOI":"10.1038\/s44319-024-00193-8","article-title":"Recruitment of Ahsa1 to Hsp90 is regulated by a conserved peptide that inhibits ATPase stimulation","volume":"25","author":"Hussein","year":"2024","journal-title":"EMBO Rep."},{"issue":"6","key":"10.1016\/j.bioorg.2026.109522_bb0095","doi-asserted-by":"crossref","first-page":"3679","DOI":"10.1074\/jbc.273.6.3679","article-title":"Hop modulates Hsp70\/Hsp90 interactions in protein folding","volume":"273","author":"Johnson","year":"1998","journal-title":"J. Biol. Chem."},{"issue":"7893","key":"10.1016\/j.bioorg.2026.109522_bb0100","doi-asserted-by":"crossref","first-page":"460","DOI":"10.1038\/s41586-021-04252-1","article-title":"Structure of Hsp90-Hsp70-hop-GR reveals the Hsp90 client-loading mechanism","volume":"601","author":"Wang","year":"2022","journal-title":"Nature"},{"issue":"6","key":"10.1016\/j.bioorg.2026.109522_bb0105","doi-asserted-by":"crossref","first-page":"886","DOI":"10.1016\/j.molcel.2008.07.021","article-title":"Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37","volume":"31","author":"Vaughan","year":"2008","journal-title":"Mol. Cell"},{"issue":"7","key":"10.1016\/j.bioorg.2026.109522_bb0110","doi-asserted-by":"crossref","first-page":"1685","DOI":"10.1016\/j.cell.2014.04.038","article-title":"Glucocorticoid receptor function regulated by coordinated action of the Hsp90 and Hsp70 chaperone cycles","volume":"157","author":"Kirschke","year":"2014","journal-title":"Cell"},{"issue":"12","key":"10.1016\/j.bioorg.2026.109522_bb0115","doi-asserted-by":"crossref","first-page":"10328","DOI":"10.1074\/jbc.M213094200","article-title":"Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle","volume":"278","author":"Richter","year":"2003","journal-title":"J. Biol. Chem."},{"issue":"19","key":"10.1016\/j.bioorg.2026.109522_bb0120","doi-asserted-by":"crossref","first-page":"17228","DOI":"10.1074\/jbc.M212761200","article-title":"Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone","volume":"278","author":"Lotz","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bioorg.2026.109522_bb0125","doi-asserted-by":"crossref","first-page":"33179","DOI":"10.1038\/srep33179","article-title":"The mechanism of Hsp90 ATPase stimulation by Aha1","volume":"6","author":"Wolmarans","year":"2016","journal-title":"Sci. Rep."},{"issue":"5","key":"10.1016\/j.bioorg.2026.109522_bb0130","doi-asserted-by":"crossref","first-page":"601","DOI":"10.1016\/j.molcel.2005.04.021","article-title":"HDAC6 regulates Hsp90 acetylation and chaperone-dependent activation of glucocorticoid receptor","volume":"18","author":"Kovacs","year":"2005","journal-title":"Mol. Cell"},{"issue":"3","key":"10.1016\/j.bioorg.2026.109522_bb0135","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1016\/j.jmb.2009.11.017","article-title":"Identification of residues on Hsp70 and Hsp90 ubiquitinated by the cochaperone CHIP","volume":"395","author":"Kundrat","year":"2010","journal-title":"J. Mol. Biol."},{"issue":"24","key":"10.1016\/j.bioorg.2026.109522_bb0140","doi-asserted-by":"crossref","first-page":"8525","DOI":"10.1073\/pnas.0407294102","article-title":"S-nitrosylation of Hsp90 promotes the inhibition of its ATPase and endothelial nitric oxide synthase regulatory activities","volume":"102","author":"Martinez-Ruiz","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"issue":"2","key":"10.1016\/j.bioorg.2026.109522_bb0145","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.molcel.2013.12.007","article-title":"Asymmetric Hsp90 N domain SUMOylation recruits Aha1 and ATP-competitive inhibitors","volume":"53","author":"Mollapour","year":"2014","journal-title":"Mol. Cell"},{"issue":"3","key":"10.1016\/j.bioorg.2026.109522_bb0150","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/j.molcel.2010.01.005","article-title":"Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function","volume":"37","author":"Mollapour","year":"2010","journal-title":"Mol. Cell"},{"issue":"6","key":"10.1016\/j.bioorg.2026.109522_bb0155","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/j.molcel.2011.02.011","article-title":"Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity","volume":"41","author":"Mollapour","year":"2011","journal-title":"Mol. Cell"},{"issue":"1","key":"10.1016\/j.bioorg.2026.109522_bb0160","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.molcel.2006.12.008","article-title":"An acetylation site in the middle domain of Hsp90 regulates chaperone function","volume":"25","author":"Scroggins","year":"2007","journal-title":"Mol. Cell"},{"issue":"3","key":"10.1016\/j.bioorg.2026.109522_bb0165","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.molcel.2012.05.015","article-title":"Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine","volume":"47","author":"Xu","year":"2012","journal-title":"Mol. Cell"},{"issue":"1","key":"10.1016\/j.bioorg.2026.109522_bb0170","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/S0968-0004(99)01503-0","article-title":"GHKL, an emergent ATPase\/kinase superfamily","volume":"25","author":"Dutta","year":"2000","journal-title":"Trends Biochem. Sci."},{"issue":"1","key":"10.1016\/j.bioorg.2026.109522_bb0175","doi-asserted-by":"crossref","DOI":"10.3892\/or.2022.8443","article-title":"HSP90 inhibitors and cancer: prospects for use in targeted therapies (review)","volume":"49","author":"Li","year":"2023","journal-title":"Oncol. Rep."},{"issue":"9","key":"10.1016\/j.bioorg.2026.109522_bb0180","doi-asserted-by":"crossref","first-page":"507","DOI":"10.2217\/fon-2022-1172","article-title":"Pimitespib for the treatment of advanced gastrointestinal stromal tumors and other tumors","volume":"20","author":"Doi","year":"2024","journal-title":"Future Oncol."},{"issue":"13","key":"10.1016\/j.bioorg.2026.109522_bb0185","doi-asserted-by":"crossref","first-page":"1413","DOI":"10.1007\/s40265-022-01764-6","article-title":"Pimitespib: first approval","volume":"82","author":"Hoy","year":"2022","journal-title":"Drugs"},{"issue":"1","key":"10.1016\/j.bioorg.2026.109522_bb0190","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1186\/s40792-023-01637-4","article-title":"Long-term response to pimitespib in postoperative recurrent gastrointestinal stromal tumors with PDGFRA D842V mutation: a case report","volume":"9","author":"Teranishi","year":"2023","journal-title":"Surg Case Rep"},{"issue":"12","key":"10.1016\/j.bioorg.2026.109522_bb0195","doi-asserted-by":"crossref","first-page":"2580","DOI":"10.1002\/ijc.34461","article-title":"Combination of pimitespib (TAS-116) with sunitinib is an effective therapy for imatinib-resistant gastrointestinal stromal tumors","volume":"152","author":"Teranishi","year":"2023","journal-title":"Int. J. Cancer"},{"issue":"4","key":"10.1016\/j.bioorg.2026.109522_bb0200","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.cstres.2024.05.005","article-title":"An update on the status of HSP90 inhibitors in cancer clinical trials","volume":"29","author":"Rastogi","year":"2024","journal-title":"Cell Stress Chaperones"},{"issue":"5","key":"10.1016\/j.bioorg.2026.109522_bb0205","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1517\/13543784.2014.902442","article-title":"Heat shock protein 90 inhibitors in the treatment of cancer: current status and future directions","volume":"23","author":"Jhaveri","year":"2014","journal-title":"Expert Opin. Investig. Drugs"},{"issue":"2","key":"10.1016\/j.bioorg.2026.109522_bb0210","doi-asserted-by":"crossref","first-page":"R33","DOI":"10.1186\/bcr1996","article-title":"NVP-AUY922: a small molecule HSP90 inhibitor with potent antitumor activity in preclinical breast cancer models","volume":"10","author":"Jensen","year":"2008","journal-title":"Breast Cancer Res."},{"issue":"5","key":"10.1016\/j.bioorg.2026.109522_bb0215","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/j.ccell.2019.09.007","article-title":"Paradigms for Precision Medicine in Epichaperome Cancer Therapy","volume":"36","author":"Pillarsetty","year":"2019","journal-title":"Cancer Cell"},{"issue":"7625","key":"10.1016\/j.bioorg.2026.109522_bb0220","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1038\/nature19807","article-title":"The epichaperome is an integrated chaperome network that facilitates tumour survival","volume":"538","author":"Rodina","year":"2016","journal-title":"Nature"},{"issue":"1","key":"10.1016\/j.bioorg.2026.109522_bb0225","doi-asserted-by":"crossref","first-page":"8912","DOI":"10.1038\/s41467-024-53178-5","article-title":"Phosphorylation-driven epichaperome assembly is a regulator of cellular adaptability and proliferation","volume":"15","author":"Roychowdhury","year":"2024","journal-title":"Nat. Commun."},{"issue":"6956","key":"10.1016\/j.bioorg.2026.109522_bb0230","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/nature01913","article-title":"A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors","volume":"425","author":"Kamal","year":"2003","journal-title":"Nature"},{"issue":"14","key":"10.1016\/j.bioorg.2026.109522_bb0235","doi-asserted-by":"crossref","first-page":"5205","DOI":"10.1128\/MCB.00009-06","article-title":"The cochaperone p23 differentially regulates estrogen receptor target genes and promotes tumor cell adhesion and invasion","volume":"26","author":"Oxelmark","year":"2006","journal-title":"Mol. Cell. Biol."},{"issue":"16","key":"10.1016\/j.bioorg.2026.109522_bb0240","doi-asserted-by":"crossref","first-page":"5956","DOI":"10.1021\/jm100060b","article-title":"Discovery of (2,4-dihydroxy-5-isopropylphenyl)-[5-(4-methylpiperazin-1-ylmethyl)-1,3-dihydroisoindol-2-yl]methanone (AT13387), a novel inhibitor of the molecular chaperone Hsp90 by fragment based drug design","volume":"53","author":"Woodhead","year":"2010","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/j.bioorg.2026.109522_bb0245","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1080\/09553007514550991","article-title":"Rdiotoxicity of intracellular 67Ga, 125I and 3H. Nuclear versus cytoplasmic radiation effects in murine L1210 leukaemia","volume":"28","author":"Hofer","year":"1975","journal-title":"Int. J. Radiat. Biol. Relat. Stud. Phys. Chem. Med."},{"issue":"25","key":"10.1016\/j.bioorg.2026.109522_bb0250","doi-asserted-by":"crossref","first-page":"17525","DOI":"10.1074\/jbc.274.25.17525","article-title":"The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes","volume":"274","author":"Grenert","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"17","key":"10.1016\/j.bioorg.2026.109522_bb0255","doi-asserted-by":"crossref","first-page":"10035","DOI":"10.1074\/jbc.271.17.10035","article-title":"Assessment of the ATP binding properties of Hsp90","volume":"271","author":"Jakob","year":"1996","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.bioorg.2026.109522_bb0260","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1177\/1087057104265995","article-title":"Development of a fluorescence polarization assay for the molecular chaperone Hsp90","volume":"9","author":"Kim","year":"2004","journal-title":"J. Biomol. Screen."},{"issue":"20","key":"10.1016\/j.bioorg.2026.109522_bb0265","doi-asserted-by":"crossref","first-page":"6215","DOI":"10.1158\/1078-0432.CCR-16-3151","article-title":"Efficacy of Onalespib, a long-acting second-generation HSP90 inhibitor, as a single agent and in combination with temozolomide against malignant gliomas","volume":"23","author":"Canella","year":"2017","journal-title":"Clin. Cancer Res."},{"issue":"4","key":"10.1016\/j.bioorg.2026.109522_bb0270","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1080\/152165499306829","article-title":"Geldanamycin induces heat shock protein expression through activation of HSF1 in K562 erythroleukemic cells","volume":"48","author":"Kim","year":"1999","journal-title":"IUBMB Life"},{"issue":"8","key":"10.1016\/j.bioorg.2026.109522_bb0275","first-page":"3312","article-title":"Induction of a heat shock factor 1-dependent stress response alters the cytotoxic activity of hsp90-binding agents","volume":"6","author":"Bagatell","year":"2000","journal-title":"Clin. Cancer Res."},{"issue":"1","key":"10.1016\/j.bioorg.2026.109522_bb0280","doi-asserted-by":"crossref","first-page":"18","DOI":"10.3892\/ijo.2014.2399","article-title":"HSP27, 70 and 90, anti-apoptotic proteins, in clinical cancer therapy (review)","volume":"45","author":"Wang","year":"2014","journal-title":"Int. J. Oncol."},{"issue":"7","key":"10.1016\/j.bioorg.2026.109522_bb0285","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1021\/ml500114p","article-title":"Chemically accessible hsp90 inhibitor that does not induce a heat shock response","volume":"5","author":"Koay","year":"2014","journal-title":"ACS Med. Chem. Lett."},{"issue":"1","key":"10.1016\/j.bioorg.2026.109522_bb0290","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/j.bbamcr.2010.09.012","article-title":"HSP90 modulates actin dynamics: inhibition of HSP90 leads to decreased cell motility and impairs invasion","volume":"1813","author":"Taiyab","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"issue":"13_Supplement","key":"10.1016\/j.bioorg.2026.109522_bb0295","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1158\/1538-7445.AM2021-971","article-title":"Abstract 971: chaperone-mediated protein degradation (CHAMP): a novel technology for tumor-targeted protein degradation","volume":"81","author":"Foley","year":"2021","journal-title":"Cancer Res."},{"issue":"14","key":"10.1016\/j.bioorg.2026.109522_bb0300","doi-asserted-by":"crossref","first-page":"ar140","DOI":"10.1091\/mbc.E21-11-0554","article-title":"DNA damage-induced nuclear import of HSP90alpha is promoted by Aha1","volume":"33","author":"Fangaria","year":"2022","journal-title":"Mol. Biol. Cell"},{"issue":"5","key":"10.1016\/j.bioorg.2026.109522_bb0305","doi-asserted-by":"crossref","first-page":"658","DOI":"10.2165\/00003495-198938050-00002","article-title":"Octreotide. A review of its pharmacodynamic and pharmacokinetic properties, and therapeutic potential in conditions associated with excessive peptide secretion","volume":"38","author":"Battershill","year":"1989","journal-title":"Drugs"},{"issue":"14","key":"10.1016\/j.bioorg.2026.109522_bb0310","doi-asserted-by":"crossref","DOI":"10.3390\/cancers13143607","article-title":"Target heterogeneity in oncology: the best predictor for differential response to radioligand therapy in neuroendocrine Tumors and prostate Cancer","volume":"13","author":"Puranik","year":"2021","journal-title":"Cancers (Basel)"},{"issue":"13","key":"10.1016\/j.bioorg.2026.109522_bb0315","doi-asserted-by":"crossref","first-page":"2185","DOI":"10.1002\/cncr.29339","article-title":"Phase 1\/1B trial of the heat shock protein 90 inhibitor NVP-AUY922 as monotherapy or in combination with bortezomib in patients with relapsed or refractory multiple myeloma","volume":"121","author":"Seggewiss-Bernhardt","year":"2015","journal-title":"Cancer"}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206826000581?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206826000581?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,2,2]],"date-time":"2026-02-02T21:17:58Z","timestamp":1770067078000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206826000581"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,3]]},"references-count":63,"alternative-id":["S0045206826000581"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2026.109522","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2026,3]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Novel Hsp90 inhibitors as leads for the development of radiotheragnostics for Meitner-Auger electron therapy","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2026.109522","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}],"article-number":"109522"}}