Please use this identifier to cite or link to this item: http://hdl.handle.net/11452/30992
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dc.contributor.authorKırmızıbayrak, Petek Ballar-
dc.contributor.authorGözen, Oğuz-
dc.contributor.authorErzurumlu, Yalçın-
dc.contributor.authorBarrio, R-
dc.contributor.authorSutherland, JD-
dc.contributor.authorRodriguez, MS-
dc.date.accessioned2023-02-13T09:01:47Z-
dc.date.available2023-02-13T09:01:47Z-
dc.date.issued2020-04-10-
dc.identifier.citationKırmızıbayrak, P. B. vd. (2020). "Divergent modulation of proteostasis in prostate cancer". ed. R. Barrio vd. Advances in Experimental Medicine and Biology, 1233, 117-151.en_US
dc.identifier.isbn978-3-030-38265-0-
dc.identifier.isbn978-3-030-38266-7-
dc.identifier.issn0065-2598-
dc.identifier.issn2214-8019-
dc.identifier.urihttps://doi.org/10.1007/978-3-030-38266-7_5-
dc.identifier.urihttps://link.springer.com/chapter/10.1007/978-3-030-38266-7_5-
dc.identifier.urihttp://hdl.handle.net/11452/30992-
dc.description.abstractProteostasis regulates key cellular processes such as cell proliferation, differentiation, transcription, and apoptosis. The mechanisms by which proteostasis is regulated are crucial and the deterioration of cellular proteostasis has been significantly associated with tumorigenesis since it specifically targets key oncoproteins and tumor suppressors. Prostate cancer (PCa) is the second most common cause of cancer death in men worldwide. Androgens mediate one of the most central signaling pathways in all stages of PCa via the androgen receptor (AR). In addition to their regulation by hormones, PCa cells are also known to be highly secretory and are particularly prone to ER stress as proper ER function is essential. Alterations in various complex signaling pathways and cellular processes including cell cycle control, transcription, DNA repair, apoptosis, cell adhesion, epithelial-mesenchymal transition (EMT), and angiogenesis are critical factors influencing PCa development through key molecular changes mainly by posttranslational modifications in PCa-related proteins, including AR, NKX3.1, PTEN, p53, cyclin D1, and p27. Several ubiquitin ligases like MDM2, Siah2, RNF6, CHIP, and substrate-binding adaptor SPOP; deubiquitinases such as USP7, USP10, USP26, and USP12 are just some of the modifiers involved in the regulation of these key proteins via ubiquitin-proteasome system (UPS). Some ubiquitin-like modifiers, especially SUMOs, have been also closely associated with PCa. On the other hand, the proteotoxicity resulting from misfolded proteins and failure of ER adaptive capacity induce unfolded protein response (UPR) that is an indispensable signaling mechanism for PCa development. Lastly, ER-associated degradation (ERAD) also plays a crucial role in prostate tumorigenesis. In this section, the relationship between prostate cancer and proteostasis will be discussed in terms of UPS, UPR, SUMOylation, ERAD, and autophagy.en_US
dc.description.sponsorshipEuropean Cooperation in Science and Technology (BM1307)en_US
dc.description.sponsorshipEge Üniversitesitr_TR
dc.description.sponsorshipBilim Akademisitr_TR
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectBiochemistry & molecular biologyen_US
dc.subjectPathologyen_US
dc.subjectResearch & experimental medicineen_US
dc.subjectProstate canceren_US
dc.subjectUbiquitinen_US
dc.subjectUbiquitin-likeen_US
dc.subjectDeubiquitinaseen_US
dc.subjectAutophagyen_US
dc.subjectUnfolded protein responseen_US
dc.subjectUnfolded protein responseen_US
dc.subjectAndrogen receptor-activtyen_US
dc.subjectTumor-suppressor geneen_US
dc.subjectDeubiquitinating enzyme USP12en_US
dc.subjectUbiquitin ligase SIAH2en_US
dc.subjectHeat-shock proteinsen_US
dc.subjectWild-type spopen_US
dc.subjectCell-proliferationen_US
dc.subjectHomeobox geneen_US
dc.subjectTranscriptional activityen_US
dc.subject.meshDeubiquitinating enzymesen_US
dc.subject.meshEndoplasmic reticulum-associated degradationen_US
dc.subject.meshHumansen_US
dc.subject.meshMaleen_US
dc.subject.meshProstatic neoplasmsen_US
dc.subject.meshProteasome endopeptidase complexen_US
dc.subject.meshProteostasisen_US
dc.subject.meshUbiquitinen_US
dc.subject.meshUnfolded protein responseen_US
dc.titleDivergent modulation of proteostasis in prostate canceren_US
dc.typeArticleen_US
dc.typeBook Chapteren_US
dc.identifier.wos000530838600006tr_TR
dc.identifier.scopus2-s2.0-85083257850tr_TR
dc.relation.tubitakSBAG-108S056/114S062tr_TR
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergitr_TR
dc.contributor.departmentBursa Uludağ Üniversitesi/Fen-Edebiyat Fakültesi/Moleküler Biyoloji ve Genetik Bölümü.tr_TR
dc.identifier.startpage117tr_TR
dc.identifier.endpage151tr_TR
dc.identifier.volume1233tr_TR
dc.relation.journalAdvances in Experimental Medicine and Biologyen_US
dc.contributor.buuauthorTepedelen, Burcu Erbaykent-
dc.contributor.researcheridCNH-6913-2022tr_TR
dc.relation.collaborationYurt içitr_TR
dc.identifier.pubmed32274755tr_TR
dc.subject.wosBiochemistry & molecular biologyen_US
dc.subject.wosPathologyen_US
dc.subject.wosMedicine, research & experimentalen_US
dc.indexed.wosSCIEen_US
dc.indexed.wosBKCISen_US
dc.indexed.scopusScopusen_US
dc.indexed.pubmedPubMeden_US
dc.wos.quartileQ2 (Biology)en_US
dc.wos.quartileQ3en_US
dc.contributor.scopusid47860936500tr_TR
dc.subject.scopusDeubiquitinase; Ubiquitin-Specific Proteases; Ubiquitinen_US
dc.subject.emtreeAndrogenen_US
dc.subject.emtreeAndrogen receptoren_US
dc.subject.emtreeCell nucleus receptoren_US
dc.subject.emtreeCullin RING ubiquitin ligaseen_US
dc.subject.emtreeCyclin D1en_US
dc.subject.emtreeCyclin dependent kinase inhibitor 1Ben_US
dc.subject.emtreeLigaseen_US
dc.subject.emtreeMyc proteinen_US
dc.subject.emtreePhosphatidylinositol 3 kinaseen_US
dc.subject.emtreePhosphatidylinositol 3,4,5 trisphosphate 3 phosphataseen_US
dc.subject.emtreeProstate specific antigenen_US
dc.subject.emtreeProtein kinase Ben_US
dc.subject.emtreeProtein NKX 3 1en_US
dc.subject.emtreeProtein p21en_US
dc.subject.emtreeProtein p27en_US
dc.subject.emtreeRegulator proteinen_US
dc.subject.emtreeRING finger E3 ubiquitin ligaseen_US
dc.subject.emtreeUbiquitinen_US
dc.subject.emtreeUbiquitin protein ligase E3en_US
dc.subject.emtreeUbiquitin protein ligase NEDD4en_US
dc.subject.emtreeUnclassified drugen_US
dc.subject.emtreeDeubiquitinaseen_US
dc.subject.emtreeProteasomeen_US
dc.subject.emtreeUbiquitinen_US
dc.subject.emtreeAmino acid sequenceen_US
dc.subject.emtreeAmino terminal sequenceen_US
dc.subject.emtreeAutophagy (cellular)en_US
dc.subject.emtreeCancer inhibitionen_US
dc.subject.emtreeCarboxy terminal sequenceen_US
dc.subject.emtreeCarcinogenesisen_US
dc.subject.emtreeDeubiquitinationen_US
dc.subject.emtreeDNA repairen_US
dc.subject.emtreeEndoplasmic reticulum associated degradationen_US
dc.subject.emtreeEpithelial mesenchymal transitionen_US
dc.subject.emtreeHumanen_US
dc.subject.emtreeNonhumanen_US
dc.subject.emtreeOncogene mycen_US
dc.subject.emtreePriority journalen_US
dc.subject.emtreeProstate canceren_US
dc.subject.emtreeProtein expressionen_US
dc.subject.emtreeProtein functionen_US
dc.subject.emtreeProtein homeostasisen_US
dc.subject.emtreeSumoylationen_US
dc.subject.emtreeUbiquitinationen_US
dc.subject.emtreeUnfolded protein responseen_US
dc.subject.emtreeEnzymologyen_US
dc.subject.emtreeMaleen_US
dc.subject.emtreeMetabolismen_US
dc.subject.emtreeProstate tumoren_US
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