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This review examines how HSP90 regulates pathways through its partnership with heat shock factor 1 (HSF-1) and evaluates PU-H71, a selective HSP90 inhibitor, as a cancer therapeutic candidate. PU-H71 promotes degradation of multiple client proteins, disrupting major oncogenic signaling routes and showing activity across triple-negative breast cancer, myeloma, B-cell lymphomas, hepatocellular carcinoma strategies, neuroinflammatory targets, and JAK2-dependent myeloproliferative neoplasms.",{"@graph":69,"@context":122},[70,84,105],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":40,"@type":76,"position":81},"https://docshare.wps.com/document/research-report/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/pu-h71-nsc-750424-a-molecular-masterpiece-that-targets-hsp90-in-cancer-and-beyond/331532/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/pu-h71-nsc-750424-a-molecular-masterpiece-that-targets-hsp90-in-cancer-and-beyond/331532.png","ImageObject",300,407,{"name":92,"@type":93},"Quinn","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-10-28","2026-09-21",true,{"@type":102,"interactionType":103,"userInteractionCount":29},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"What role does HSP90 play in cellular health and disease according to the review?","Question",{"text":112,"@type":113},"HSP90 is described as a pivotal molecular chaperone with multifaceted roles in cellular stress responses. It is also positioned as a key regulator connected to disease processes through its partnership with HSF-1.","Answer",{"name":115,"@type":110,"acceptedAnswer":116},"How does PU-H71 exert anticancer effects in the reported studies?",{"text":117,"@type":113},"PU-H71 is presented as a selective HSP90 inhibitor that induces degradation of multiple client proteins. This disruption affects several survival and signaling pathways, including MAPK, PI3K/Akt, JAK/STAT, EGFR, and mTOR.",{"name":119,"@type":110,"acceptedAnswer":120},"Which cancer and disease areas are highlighted for PU-H71 in this review?",{"text":121,"@type":113},"The review highlights triplenegative breast cancer and combination with carbon-ion beam therapy, myeloma, B-cell lymphomas dependent on Bcl6, hepatocellular carcinoma treatment approaches, and potential suppression of glial cell activation for neuroinflammatory disorders. It also mentions relevance to JAK2-dependent myeloproliferative neoplasms.","https://schema.org",{"og:url":83,"og:type":124,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":126,"canonical":83},"index,follow",{"doc_id":128,"site_id":62},331532,1790689720,{"code":4,"msg":5,"data":131},{"doc_id":128,"user_id":132,"nickname":92,"user_avatar":133,"doc_module":4,"category_id":39,"category_name":40,"doc_title":65,"doc_description":67,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":29,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":139,"language":140,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":141,"faqs":142,"seo_title":143,"seo_description":67,"update_tm":144,"read_time":145,"preview_page_count":4},962075114765,"https://ap-avatar.wpscdn.com/davatar_a8503ba1806abce46bf441b54a3ca4cd","TYPE Review  \nPUBLISHED 05 November 2024 DOI 10.3389/fphar.2024.1475998  \nOPEN ACCESS  \nEDITED BY  \nViviana di Giacomo,  \nUniversity of Studies G. d’Annunzio Chieti and Pescara, Italy  \nREVIEWED BY  \nGabriela Chiosis,  \nMemorial Sloan Kettering Cancer Center, United States  \nErnest Duah,  \nSumitomo Dainippon Pharma Oncology, United States  \n*CORRESPONDENCE  \nSameh Saber,  \n [sampharm81@gmail.co](sampharm81@gmail.co)[ ](sampharm81@gmail.co)Mai A. Elhemely,  \n [mai.ali@manchester.ac.uk](mai.ali@manchester.ac.uk)[ ](mai.ali@manchester.ac.uk)Elsayed A. Elmorsy,  \n [a.almarsa@qu.edu.sa](a.almarsa@qu.edu.sa)[ ](a.almarsa@qu.edu.sa)Rabab S. Hamad,  \n [rhamad@kfu.edu.sa](rhamad@kfu.edu.sa)[ ](rhamad@kfu.edu.sa)Mustafa Ahmed Abdel-Reheim,  \n [m.ahmed@su.edu.sa](m.ahmed@su.edu.sa)  \nRECEIVED 04 August 2024  \nACCEPTED 22 October 2024  \nPUBLISHED 05 November 2024  \nCITATION  \nSaber S, Abdelhady R, Elhemely MA, Elmorsy EA, Hamad RS, Abdel-Reheim MA, El-kott AF, AlShehri MA, Morsy K, AlSheri AS and Youssef ME (2024) PU-H71 (NSC 750424): a molecular masterpiece that targets HSP90 in cancer and beyond.  \nFront. Pharmacol. 15:1475998 .  \ndoi: 10.3389/fphar.2024.1475998  \nCOPYRIGHT  \n© 2024 Saber, Abdelhady, Elhemely, Elmorsy, Hamad, Abdel-Reheim, El-kott, AlShehri, Morsy, AlSheri and Youssef. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY) . The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.  \nPU-H71 (NSC 750424): a molecular masterpiece that targets HSP90 in cancer and beyond  \nSameh Saber 1*, Rasha Abdelhady 2,3, Mai A. Elhemely 4*, Elsayed A. Elmorsy 5,6*, Rabab S. Hamad 7, 8*,  \nMustafa Ahmed Abdel-Reheim 9,10*, Attalla F. El-kott 11,12, Mohammed A. AlShehri 11, Kareem Morsy 11,13, Ali S. AlSheri 11 and Mahmoud E. Youssef 1  \n1Department of Pharmacology, Faculty of Pharmacy, Delta University for Science and Technology, Gamasa, Egypt, 2Pharmacology and Toxicology Department, Faculty of Pharmacy, Fayoum University, Fayoum, Egypt, 3Pharmacology and Toxicology Department, Faculty of Pharmacy, Egyptian Chinese University, Cairo, Egypt, 4School of Medical Sciences, Faculty of Biology, Medicine and Health, The University of Manchester, Manchester, United Kingdom, 5Department of Pharmacology and Therapeutics, College of Medicine, Qassim University, Buraidah, Saudi Arabia, 6Department of Clinical Pharmacology, Faculty of Medicine, Mansoura University, Mansoura, Egypt, 7 Biological Sciences Department, College of Science, King Faisal University, Al Ahsa, Saudi Arabia, 8Central Laboratory, Theodor Bilharz Research Institute, Giza, Egypt, 9Department of Pharmaceutical Sciences, College of Pharmacy, Shaqra University, Shaqra, Saudi Arabia, 10Department of Pharmacology and Toxicology, Faculty of Pharmacy, Beni-Suef University, Beni Suef, Egypt, 11Department of Biology, College of Science, King Khalid University, Abha, Saudi Arabia, 12 Department of Zoology, Faculty of Science, Damanhour University, Damanhour, Egypt, 13Department of Zoology, Faculty of Science, Cairo University, Cairo, Egypt  \nHeat shock protein 90 (HSP90) is a pivotal molecular chaperone with multifaceted roles in cellular health and disease. Herein, we explore how HSP90 orchestrates cellular stress responses, particularly through its partnership with heat shock factor 1 (HSF-1) . PU-H71, a selective inhibitor of HSP90, demonstrates significant potential in cancer therapy by targeting a wide array of oncogenic pathways. By inducing the degradation of multiple client proteins, PU-H71 disrupts critical signaling pathways such as MAPK, PI3K/Akt, JAK/STAT, EGFR, and mTOR, which are essential for cancer cell survival, proliferation, and metastasis. W","cbCaiib08gS6R4EQ","https://ap.wps.com/l/cbCaiib08gS6R4EQ","pdf",1877223,27,"English","# Introduction\n## Heat shock proteins and HSP90 context\n## PU-H71 as a selective HSP90 inhibitor","[{\"question\":\"What role does HSP90 play in cellular health and disease according to the review?\",\"answer\":\"HSP90 is described as a pivotal molecular chaperone with multifaceted roles in cellular stress responses. It is also positioned as a key regulator connected to disease processes through its partnership with HSF-1.\"},{\"question\":\"How does PU-H71 exert anticancer effects in the reported studies?\",\"answer\":\"PU-H71 is presented as a selective HSP90 inhibitor that induces degradation of multiple client proteins. This disruption affects several survival and signaling pathways, including MAPK, PI3K/Akt, JAK/STAT, EGFR, and mTOR.\"},{\"question\":\"Which cancer and disease areas are highlighted for PU-H71 in this review?\",\"answer\":\"The review highlights triplenegative breast cancer and combination with carbon-ion beam therapy, myeloma, B-cell lymphomas dependent on Bcl6, hepatocellular carcinoma treatment approaches, and potential suppression of glial cell activation for neuroinflammatory disorders. It also mentions relevance to JAK2-dependent myeloproliferative neoplasms.\"}]","PU-H71 (NSC 750424) - a molecular masterpiece that targets HSP90 in cancer and beyond | PDF",1789993775,68]