[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"doc-seo-332498-105":3,"detail-sidebar-cat-0-en-105":81,"doc-detail-332498-en":130},{"code":4,"msg":5,"data":6},0,"ok",{"site_id":7,"language":8,"slug":9,"title":10,"keywords":11,"description":12,"schema_data":13,"social_meta":74,"head_meta":76,"extra_data":78,"updated_unix":80},105,"en","e3-ubiquitin-ligases-and-their-therapeutic-applications-in-cancers-e3-ubiquitin-ligases-and-their-therapeutic-applications-in-cancers","E3 Ubiquitin Ligases and Their Therapeutic Applications in Cancers - E3 Ubiquitin Ligases and Their Therapeutic Applications in Cancers","","E3 ubiquitin ligases are enzymes that maintain cellular equilibrium by attaching ubiquitin to substrates for destruction, operating through the ubiquitin-proteasome system. Because many cancer-associated proteins, including oncogenes and tumor suppressors, are regulated by this pathway, E3 ligases are attractive targets for anti-cancer drug development. E3 ligases act as substrate-selecting modules, enabling selective degradation of proteins linked to tumor biology. This review surveys the roles of E3 ligases in cancer and evaluates current bioactive substances designed to target distinct E3 ligases as potential candidates for cancer treatment.",{"@graph":14,"@context":73},[15,34,56],{"@type":16,"itemListElement":17},"BreadcrumbList",[18,23,27,31],{"item":19,"name":20,"@type":21,"position":22},"https://docshare.wps.com","Home","ListItem",1,{"item":24,"name":25,"@type":21,"position":26},"https://docshare.wps.com/document/","Document",2,{"item":28,"name":29,"@type":21,"position":30},"https://docshare.wps.com/document/research-report/","Research & Report",3,{"item":32,"name":10,"@type":21,"position":33},"https://docshare.wps.com/document/e3-ubiquitin-ligases-and-their-therapeutic-applications-in-cancers-e3-ubiquitin-ligases-and-their-therapeutic-applications-in-cancers/332498/",4,{"url":32,"name":10,"@type":35,"image":36,"author":41,"headline":10,"publisher":44,"fileFormat":47,"inLanguage":8,"description":12,"dateModified":48,"datePublished":49,"encodingFormat":47,"isAccessibleForFree":50,"interactionStatistic":51},"DigitalDocument",{"url":37,"@type":38,"width":39,"height":40},"https://docshare.wps.com/thumbnails/e3-ubiquitin-ligases-and-their-therapeutic-applications-in-cancers-e3-ubiquitin-ligases-and-their-therapeutic-applications-in-cancers/332498.png","ImageObject",300,407,{"name":42,"@type":43},"Miles","Person",{"url":19,"name":45,"@type":46},"DocShare","Organization","application/pdf","2026-11-03","2026-09-21",true,{"@type":52,"interactionType":53,"userInteractionCount":55},"InteractionCounter",{"@type":54},"ViewAction",9,{"@type":57,"mainEntity":58},"FAQPage",[59,65,69],{"name":60,"@type":61,"acceptedAnswer":62},"What is the main biological role of E3 ubiquitin ligases in cells?","Question",{"text":63,"@type":64},"E3 ubiquitin ligases bind ubiquitin molecules to specific substrates, marking them for destruction and thereby helping maintain cellular equilibrium through the ubiquitin-proteasome system.","Answer",{"name":66,"@type":61,"acceptedAnswer":67},"Why are E3 ligases considered promising targets for cancer therapy?",{"text":68,"@type":64},"Many cancer-related proteins are controlled by the ubiquitin-proteasome system. Inhibiting particular E3 ligases can change oncoprotein and tumor-suppressor levels, promoting apoptosis, altering the cell cycle, and helping overcome drug resistance.",{"name":70,"@type":61,"acceptedAnswer":71},"What does the review emphasize about bioactive substances targeting E3 ligases?",{"text":72,"@type":64},"It reviews the current bioactive substances created to target different E3 ligases and highlights their potential as candidates for treating cancers.","https://schema.org",{"og:url":32,"og:type":75,"og:title":10,"og:site_name":45,"og:description":12},"article",{"robots":77,"canonical":32},"index,follow",{"doc_id":79,"site_id":7},332498,1790646174,{"code":4,"msg":82,"data":83},"success",[84,88,92,96,101,106,111,115,119,122,126],{"id":22,"doc_module":4,"doc_module_name":25,"category_name":85,"show_sort_weight":86,"slug":87},"Story & Novel",90,"story-novel",{"id":26,"doc_module":4,"doc_module_name":25,"category_name":89,"show_sort_weight":90,"slug":91},"Literature",80,"literature",{"id":33,"doc_module":4,"doc_module_name":25,"category_name":93,"show_sort_weight":94,"slug":95},"Exam",70,"exam",{"id":97,"doc_module":4,"doc_module_name":25,"category_name":98,"show_sort_weight":99,"slug":100},5,"Comic",60,"comic",{"id":102,"doc_module":4,"doc_module_name":25,"category_name":103,"show_sort_weight":104,"slug":105},6,"Technology",50,"technology",{"id":107,"doc_module":4,"doc_module_name":25,"category_name":108,"show_sort_weight":109,"slug":110},7,"Healthcare",40,"healthcare",{"id":112,"doc_module":4,"doc_module_name":25,"category_name":29,"show_sort_weight":113,"slug":114},8,30,"research-report",{"id":55,"doc_module":4,"doc_module_name":25,"category_name":116,"show_sort_weight":117,"slug":118},"Religion & Spirituality",20,"religion-spirituality",{"id":117,"doc_module":4,"doc_module_name":25,"category_name":120,"show_sort_weight":117,"slug":121},"World Cup","world-cup",{"id":123,"doc_module":4,"doc_module_name":25,"category_name":124,"show_sort_weight":123,"slug":125},10,"Lifestyle","lifestyle",{"id":127,"doc_module":4,"doc_module_name":25,"category_name":128,"show_sort_weight":97,"slug":129},19,"General","general",{"code":4,"msg":82,"data":131},{"doc_id":79,"user_id":132,"nickname":42,"user_avatar":133,"doc_module":4,"category_id":112,"category_name":29,"doc_title":10,"doc_description":12,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":55,"is_deleted":4,"is_public":22,"is_downloadable":22,"audit_status":22,"page_count":30,"language":139,"language_code":8,"site_id":7,"html_lang":8,"table_of_contents":140,"faqs":141,"seo_title":142,"seo_description":12,"update_tm":143,"read_time":112,"preview_page_count":4},13056703019404,"https://ap-avatar.wpscdn.com/davatar_29158cc5080c5b710cf443261637dec0","Narrative Review  \nE3 Ubiquitin Ligases and Their Therapeutic Applications in Cancers: Narrative Review  \nAzfar Jamal1,2  \n1Department of Biology, College of Science, Al‑Zulfi‑, Majmaah University, Majmaah, Riyadh, Saudi Arabia, 2Health and Basic Science Research Centre, Majmaah University, Majmaah, Riyadh,  \nSaudi Arabia  \nSubmitted: 23‑Feb‑2024  \nRevised: 05‑Mar‑2024  \nAccepted: 12‑Mar‑2024  \nPublished: 07‑Jun‑2024  \nAbstract  \nE3 ubiquitin ligases are a class of enzymes, essential for maintaining the equilibrium of cells by binding ubiquitin molecules to substrates to mark them for destruction. Since many cancer‑related proteins, including both oncogenic and tumor‑suppressive ones, are controlled by the ubiquitin‑proteasome system, E3 ligases have drawn a great deal of interest as potential targets for the creation of anti‑cancer drugs. This is because E3 ligases function as modules that select the substrates that are intended for degradation, giving them the ability to particularly affect proteins that are connected to cancer. Their molecular properties and the ways in which they work serve as the basis for these distinctions. Investment in the creation of bioactive substances that can target E3 ligases is essential given the crucial roles they play in cancer. These substances have the potential to be powerful cancer‑fighting tools. In this review, we explore the crucial roles that E3 ligases play in the biology of cancer. We also examine the current bioactive substances that have been created to target different E3 ligases, emphasizing their potential as candidates for treating the cancers.  \nKeywords: E3 ligase, MDM2, NEDD4, RING (really interesting new genes), ubiquitin  \nIntroduction  \nThe ubiquitin‑proteasome  \nmechanism for breaking  \nsystem (UPS) is a down proteins in both  \nhealthy and pathological conditions through a series of enzymatic procedures including the enzymes (E1, E2, and E3). This is important for a diversity of cellular procedures, counting autophagy, signal transduction, deoxyribonucleic acid (DNA) repair, and more. The abnormalities in proteins delimited by the UPS are strongly related to several types of human malignancies.[1‑3] Prominently, a growing body of research has revealed that E3 ligases play a critical role in several malignancies by controlling the degradation of tumor organizers or suppressor genes.[4,5]  \nTargeting E3 ubiquitin ligases in cancer therapy holds significant promise due to their pivotal role in regulating protein degradation within cells through the UPS. By inhibiting specific E3 ligases, it becomes possible to modulate the levels of oncoproteins and tumor suppressors, inducing apoptosis, disrupting the cell cycle, and overcoming drug resistance.[6] This  \n\n| Access this article online |  |\n| --- | --- |\n| Quick Response Code:\u003Cbr>| Website: [https://journals.lww.com/jpbs](https://journals.lww.com/jpbs) |\n|  | DOI: 10.4103/jpbs.jpbs_134_24 |\n\napproach offers a precision medicine strategy, allowing for a more personalized treatment approach, and can be synergistically employed with existing cancer therapies. However, the complexity of the UPS necessitates thorough research to identify suitable E3 ligase targets and develop selective inhibitors to minimize potential off‑target effects, advancing the potential of E3 ligases as effective targets for cancer therapy.[6,7] This review investigates potential uses of E3 ligases as anti‑cancer therapies and explains their important roles in the setting of cancer.  \nAberrant Expression of E3 Ligases in Cancer  \nSome key cancer‑associated proteins, like p53, are under the strict supervision of several E3 ligases.[8] The first Nedd4 family member found to be widely expressed  \n\n| Address for correspondence: Dr. Azfar Jamal,\u003Cbr>Department of Biology, College of Science, Majmaah University, Majmaah 11952, Saudi Arabia.\u003Cbr>E‑mail: [azfarjamal@mu.edu.sa](azfarjamal@mu.edu.sa) |\n| --- |\n| This is an open access article distributed under the ","cbCaij4UX27esups","https://ap.wps.com/l/cbCaij4UX27esups","pdf",431643,"English","# Introduction\n## The ubiquitin-proteasome system (UPS)\n## Targeting E3 ubiquitin ligases in cancer therapy\n# Aberrant Expression of E3 Ligases in Cancer\n## NEDD4 and NEDD4L expression patterns","[{\"question\":\"What is the main biological role of E3 ubiquitin ligases in cells?\",\"answer\":\"E3 ubiquitin ligases bind ubiquitin molecules to specific substrates, marking them for destruction and thereby helping maintain cellular equilibrium through the ubiquitin-proteasome system.\"},{\"question\":\"Why are E3 ligases considered promising targets for cancer therapy?\",\"answer\":\"Many cancer-related proteins are controlled by the ubiquitin-proteasome system. Inhibiting particular E3 ligases can change oncoprotein and tumor-suppressor levels, promoting apoptosis, altering the cell cycle, and helping overcome drug resistance.\"},{\"question\":\"What does the review emphasize about bioactive substances targeting E3 ligases?\",\"answer\":\"It reviews the current bioactive substances created to target different E3 ligases and highlights their potential as candidates for treating cancers.\"}]","E3 Ubiquitin Ligases and Their Therapeutic Applications in Cancers - E3 Ubiquitin Ligases and Their Therapeutic Applications in Cancers | PDF",1789998492]