https://m2.mtmt.hu/ hun 2026-09-22 05:43 JournalArticle 36833696 VALIDATED true Funding Agency and Grant Number: University of California; Semmelweis University Funding text: The APC was funded by Semmelweis University and University of California. 0 false 2026-05-22T22:33:07.512+0000 2026-02-10T10:06:35.536+0000 2026-01-02T11:45:40.290+0000 true 10000786 Csala Miklós /api/author/10000786 Author Csala Miklós (Biokémia) true 10000786 2026-05-22T22:32:02.419+0000 2026-01-12T14:00:23.814+0000 true 10062250 Molnár-Taga Márta /api/admin/10062250 Admin Molnár-Taga Márta (SE 4-es admin) true 10062250 2026-01-19T07:23:34.588+0000 true 10080205 Szalóky-Siki Ágnes /api/admin/10080205 Admin Szalóky-Siki Ágnes (SE_KK_Admin5_SZSA, admin) true true false true 24 24 /api/publicationtype/24 PublicationType Folyóiratcikk 1 true 24 JournalArticle true 1134514 Survey paper true 24 24 /api/publicationtype/24 PublicationType Folyóiratcikk 1 true 24 JournalArticle /api/subtype/1134514 Összefoglaló cikk SubType Összefoglaló cikk (Folyóiratcikk) 102 true 1134514 true 1 /api/category/1 Category Tudományos true 1 Wappler-Guzzetta, Edina Amalia true true /api/journal/10003252 REVIEWED INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 1661-6596 1422-0067 true false 10003252 false 10003252 true 1661-6596 1422-0067 Journal FOREIGN 27 1 342 342 45 2026 Epithelial ovarian cancer is one of the most lethal gynecological malignancies worldwide. Its development strongly depends on several genetic and environmental factors, with metabolic components and cellular redox homeostasis alterations playing a significant a role in its development and disease progression. In this review, we summarize the contribution of mitochondrial and endoplasmic reticulum (ER) stress in the pathogenesis of epithelial ovarian cancer along with their role as potential biomarkers and therapeutic targets, including proteins of glucose metabolism, mitochondrial fission and fusion, mitophagy, membrane-associated ring-CH-type finger 5 (MARCH5), A-kinase anchoring proteins (AKAPs), proteins regulating mitochondrial Ca2+ homeostasis, mitochondrial unfolded protein response (UPRmt) proteins, activating transcription factors (ATFs), CCAAT enhancer binding protein (C/EBP) homologous protein (CHOP), ‘mitokines’, GRP75, and GRP78. Although many of these potential targets are in preclinical phase, they have a high potential to become valuable alternative or additive treatments for epithelial ovarian cancers. Funding 2061592 /api/funding/2061592 (The APC was funded by Semmelweis University) false true true 2026 true true true false true false GOLD 2026-05-23 false http://www.mdpi.com/journal/ijms 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 0 5 5 D1 441941 false false false false 2026-01-11T14:00:23.291+0000 Belgyógyászati és Hematológiai Klinika (SE / AOK / K); Szülészeti és Nőgyógyászati Klinika (SE / AOK / K); Transzlációs Medicina Intézet (SE / AOK / I) 4 23 3 7 0 true Language 10002 /api/language/10002 Angol Angol English true 2 true PersonAuthorship 132491067 /api/authorship/132491067 Wappler-Guzzetta, Edina Amalia 1 0.14285715 true false false Wappler-Guzzetta Edina Amalia true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 132491068 /api/authorship/132491068 Margittai, Eva [Margittai, Éva (Molekuláris Bioló...), szerző] Transzlációs Medicina Intézet (SE / AOK / I) 2 0.143 false false false Author 10015704 /api/author/10015704 Margittai Éva (Molekuláris Biológiai) Margittai Éva true 10015704 true Margittai Eva true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 132491069 /api/authorship/132491069 Veszelyi, Krisztina [Veszelyi, Krisztina Nóra (molekuláris biológia), szerző] Transzlációs Medicina Intézet (SE / AOK / I) 3 0.143 false false false Author 10074867 /api/author/10074867 Veszelyi Krisztina Nóra (molekuláris biológia) Veszelyi Krisztina Nóra true true Veszelyi Krisztina true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 132491070 /api/authorship/132491070 Pickard, Shanel 4 0.14285715 false false false Pickard Shanel true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 132491071 /api/authorship/132491071 Merwin, Caroline 5 0.14285715 false false false Merwin Caroline true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 132491072 /api/authorship/132491072 Molvarec, Attila [Molvarec, Attila (Szülészet-nőgyógy...), szerző] Szülészeti és Nőgyógyászati Klinika (SE / AOK / K) 6 0.143 false false false Author 10003519 /api/author/10003519 Molvarec Attila (Szülészet-nőgyógyászat) Molvarec Attila true 10003519 true Molvarec Attila true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PersonAuthorship 132491073 /api/authorship/132491073 Czegle, Ibolya ✉ [Czegle, Ibolya (Onkológia, belgyó...), szerző] Belgyógyászati és Hematológiai Klinika (SE / AOK / K) 7 0.143 false true true Author 10023838 /api/author/10023838 Czegle Ibolya (Onkológia, belgyógyászat) Czegle Ibolya true 10023838 true Czegle Ibolya true false false AuthorshipType 1 /api/authorshiptype/1 Szerző 0 true 0 true false true PublicationIdentifier 31089356 /api/publicationidentifier/31089356 DOI: 10.3390/ijms27010342 PlainSource 6 /api/publicationsource/6 DOI PublicationSourceType 10001 /api/publicationsourcetype/10001 DOI true true true DOI DOI https://doi.org/@@@ true true 6 true IDENTICAL 10.3390/ijms27010342 https://doi.org/10.3390/ijms27010342 false true PublicationIdentifier 31201692 /api/publicationidentifier/31201692 WoS: 001657437600001 PlainSource 1 /api/publicationsource/1 WoS PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true WoS WoS https://www.webofscience.com/wos/woscc/full-record/@@@ true true 1 true IDENTICAL 001657437600001 https://www.webofscience.com/wos/woscc/full-record/001657437600001 true true PublicationIdentifier 31397017 /api/publicationidentifier/31397017 Scopus: 105026969813 PlainSource 3 /api/publicationsource/3 Scopus PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true Scopus Scopus http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-@@@ true true 3 true IDENTICAL 105026969813 http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-105026969813 false true PublicationIdentifier 31215458 /api/publicationidentifier/31215458 PubMed: 41516218 PlainSource 17 /api/publicationsource/17 PubMed PublicationSourceType 10003 /api/publicationsourcetype/10003 Indexelő adatbázis false true true PubMed PubMed http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=@@@&dopt=Abstract true true 17 true IDENTICAL 41516218 http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=41516218&dopt=Abstract true true PublicationIdentifier 31383746 /api/publicationidentifier/31383746 Egyéb URL: https://www.scopus.com/inward/record.uri?eid=2-s2.0-105026969813&doi=10.3390%2Fijms27010342&partnerID=40&md5=cd8be9409f0a2140c0b1cd2b2154408a PlainSource 40 /api/publicationsource/40 Egyéb URL PublicationSourceType 10006 /api/publicationsourcetype/10006 Link true true true Egyéb URL Other URL @@@ true true 40 true NONE IDENTICAL https://www.scopus.com/inward/record.uri?eid=2-s2.0-105026969813&doi=10.3390%2Fijms27010342&partnerID=40&md5=cd8be9409f0a2140c0b1cd2b2154408a https://www.scopus.com/inward/record.uri?eid=2-s2.0-105026969813&doi=10.3390%2Fijms27010342&partnerID=40&md5=cd8be9409f0a2140c0b1cd2b2154408a false true PredatorRating 11781719 /api/predatorrating/11781719 Norvég listás folyóirat:441941 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 1661-6596 1422-0067 RatingType 10033 /api/ratingtype/10033 Norvég listás folyóirat norveg true true 441941 true true SjrRating 11676124 /api/sjrrating/11676124 sjr:D1 (2026) Scopus - Inorganic Chemistry INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 1661-6596 1422-0067 5 0.1 journal RatingType 10002 /api/ratingtype/10002 sjr sjr true true ClassificationExternal 1604 /api/classificationexternal/1604 Scopus - Inorganic Chemistry true 1604 true D1 FROM_LAST_YEAR true true Reference 71118888 /api/reference/71118888 1. Sung 2021: Global Cancer Statistics 2020: GLOBOCAN Estimates of Incidence and Mortality Worldwide for 36 Cancers in 185 Countries., CA Cancer J. Clin., 71, p. 209 1 false true Reference 71118921 /api/reference/71118921 2. Blumberg 2014: Transcription Factors Bind Negatively Selected Sites within Human mtDNA Genes., Genome Biol. Evol., 6, p. 2634, DOI: 10.1093/gbe/evu210 2 10.1093/gbe/evu210 false true Reference 71118889 /api/reference/71118889 3. Wentzensen 2016: Ovarian Cancer Risk Factors by Histologic Subtype: An Analysis from the Ovarian Cancer Cohort Consortium., J. Clin. Oncol., 34, p. 2888, DOI: 10.1200/JCO.2016.66.8178 3 10.1200/JCO.2016.66.8178 false true Reference 71118890 /api/reference/71118890 4. Karlsson 2021: Time-Dependent Effects of Oral Contraceptive Use on Breast, Ovarian, and Endometrial Cancers., Cancer Res., 81, p. 1153, DOI: 10.1158/0008-5472.CAN-20-2476 4 10.1158/0008-5472.CAN-20-2476 false true Reference 71118891 /api/reference/71118891 5. Miller 2020: ESMO recommendations on predictive biomarker testing for homologous recombination deficiency and PARP inhibitor benefit in ovarian cancer., Ann. Oncol., 31, p. 1606, DOI: 10.1016/j.annonc.2020.08.2102 5 10.1016/j.annonc.2020.08.2102 false true Reference 71118892 /api/reference/71118892 6. Weidemann, S., Böhle, J.L., Contreras, H., Luebke, A.M., Kluth, M., Büscheck, F., Hube-Magg, C., Höflmayer, D., Möller, K., and Fraune, C. (2021). Napsin A Expression in Human Tumors and Normal Tissues. Pathol. Oncol. Res., 27., DOI: 10.3389/pore.2021.613099 6 10.3389/pore.2021.613099 false true Reference 71118893 /api/reference/71118893 7. Desouki 2014: Differential vimentin expression in ovarian and uterine corpus endometrioid adenocarcinomas: Diagnostic utility in distinguishing double primaries from metastatic tumors., Int. J. Gynecol. Pathol., 33, p. 274, DOI: 10.1097/PGP.0b013e31829040b5 7 10.1097/PGP.0b013e31829040b5 false true Reference 71118894 /api/reference/71118894 8. Iwamoto 2015: Napsin A is frequently expressed in clear cell carcinoma of the ovary and endometrium., Hum. Pathol., 46, p. 957, DOI: 10.1016/j.humpath.2015.03.008 8 10.1016/j.humpath.2015.03.008 false true Reference 71118895 /api/reference/71118895 9. Lim 2015: Immunohistochemical Comparison of Ovarian and Uterine Endometrioid Carcinoma, Endometrioid Carcinoma With Clear Cell Change, and Clear Cell Carcinoma., Am. J. Surg. Pathol., 39, p. 1061, DOI: 10.1097/PAS.0000000000000436 9 10.1097/PAS.0000000000000436 false true Reference 71118896 /api/reference/71118896 10. Bassiouny 2019: p53, Mismatch Repair Protein, and POLE Abnormalities in Ovarian Clear Cell Carcinoma: An Outcome-based Clinicopathologic Analysis., Am. J. Surg. Pathol., 43, p. 1591, DOI: 10.1097/PAS.0000000000001328 10 10.1097/PAS.0000000000001328 false true Reference 71118897 /api/reference/71118897 11. DeLair 2011: Morphologic spectrum of immunohistochemically characterized clear cell carcinoma of the ovary: A study of 155 cases., Am. J. Surg. Pathol., 35, p. 36, DOI: 10.1097/PAS.0b013e3181ff400e 11 10.1097/PAS.0b013e3181ff400e false true Reference 71118898 /api/reference/71118898 12. Kang 2021: Refined cut-off for TP53 immunohistochemistry improves prediction of TP53 mutation status in ovarian mucinous tumors: Implications for outcome analyses., Mod. Pathol., 34, p. 194, DOI: 10.1038/s41379-020-0618-9 12 10.1038/s41379-020-0618-9 false true Reference 71118899 /api/reference/71118899 13. Vang 2006: Immunohistochemical expression of CDX2 in primary ovarian mucinous tumors and metastatic mucinous carcinomas involving the ovary: Comparison with CK20 and correlation with coordinate expression of CK7., Mod. Pathol., 19, p. 1421, DOI: 10.1038/modpathol.3800698 13 10.1038/modpathol.3800698 false true Reference 71118900 /api/reference/71118900 14. Kim 2005: The usefulness of CDX-2 for differentiating primary and metastatic ovarian carcinoma: An immunohistochemical study using a tissue microarray., J. Korean Med. Sci., 20, p. 643, DOI: 10.3346/jkms.2005.20.4.643 14 10.3346/jkms.2005.20.4.643 false true Reference 71118901 /api/reference/71118901 15. Collinson 2014: Optimal treatment of early-stage ovarian cancer., Ann. Oncol., 25, p. 1165, DOI: 10.1093/annonc/mdu116 15 10.1093/annonc/mdu116 false true Reference 71118902 /api/reference/71118902 16. Lawrie, T.A., Winter-Roach, B.A., Heus, P., and Kitchener, H.C. (2015). Adjuvant (post-surgery) chemotherapy for early stage epithelial ovarian cancer. Cochrane Database Syst. Rev., DOI: 10.1002/14651858.CD004706.pub5 16 10.1002/14651858.CD004706.pub5 false true Reference 71118903 /api/reference/71118903 17. Rouzier 2017: Efficacy and safety of bevacizumab-containing neoadjuvant therapy followed by interval debulking surgery in advanced ovarian cancer: Results from the ANTHALYA trial., Eur. J. Cancer, 70, p. 133, DOI: 10.1016/j.ejca.2016.09.036 17 10.1016/j.ejca.2016.09.036 false true Reference 71118904 /api/reference/71118904 18. Mendiola 2019: Efficacy and safety results from GEICO 1205, a randomized phase II trial of neoadjuvant chemotherapy with or without bevacizumab for advanced epithelial ovarian cancer., Int. J. Gynecol. Cancer, 29, p. 1050, DOI: 10.1136/ijgc-2019-000256 18 10.1136/ijgc-2019-000256 false true Reference 71118905 /api/reference/71118905 19. Stuart 2011: 2010 Gynecologic Cancer InterGroup (GCIG) Consensus Statement on Clinical Trials in Ovarian Cancer., Int. J. Gynecol. Cancer, 21, p. 750, DOI: 10.1097/IGC.0b013e31821b2568 19 10.1097/IGC.0b013e31821b2568 false true Reference 71118906 /api/reference/71118906 20. Perren 2011: A Phase 3 Trial of Bevacizumab in Ovarian Cancer., N. Engl. J. Med., 365, p. 2484, DOI: 10.1056/NEJMoa1103799 20 10.1056/NEJMoa1103799 false true Reference 71118907 /api/reference/71118907 21. Farmer 2005: Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy., Nature, 434, p. 917, DOI: 10.1038/nature03445 21 10.1038/nature03445 false true Reference 71118908 /api/reference/71118908 22. Monk 2022: A Randomized, Phase III Trial to Evaluate Rucaparib Monotherapy as Maintenance Treatment in Patients with Newly Diagnosed Ovarian Cancer (ATHENA–MONO/GOG-3020/ENGOT-ov45)., J. Clin. Oncol., 40, p. 3952, DOI: 10.1200/JCO.22.01003 22 10.1200/JCO.22.01003 false true Reference 71118909 /api/reference/71118909 23. Harter 2023: Newly diagnosed and relapsed epithelial ovarian cancer: ESMO Clinical Practice Guideline for diagnosis, treatment and follow-up., Ann. Oncol., 34, p. 833, DOI: 10.1016/j.annonc.2023.07.011 23 10.1016/j.annonc.2023.07.011 false true Reference 71118910 /api/reference/71118910 24. DiSilvestro 2023: Overall Survival with Maintenance Olaparib at a 7-Year Follow-Up in Patients with Newly Diagnosed Advanced Ovarian Cancer and a BRCA Mutation: The SOLO1/GOG 3004 Trial., J. Clin. Oncol., 41, p. 609, DOI: 10.1200/JCO.22.01549 24 10.1200/JCO.22.01549 false true Reference 71118911 /api/reference/71118911 25. Moore 2018: Maintenance Olaparib in Patients with Newly Diagnosed Advanced Ovarian Cancer., N. Engl. J. Med., 379, p. 2495, DOI: 10.1056/NEJMoa1810858 25 10.1056/NEJMoa1810858 false true Reference 71118912 /api/reference/71118912 26. Aghajanian 2015: Final overall survival and safety analysis of OCEANS, a phase 3 trial of chemotherapy with or without bevacizumab in patients with platinum-sensitive recurrent ovarian cancer., Gynecol. Oncol., 139, p. 10, DOI: 10.1016/j.ygyno.2015.08.004 26 10.1016/j.ygyno.2015.08.004 false true Reference 71118913 /api/reference/71118913 27. Yoon 2023: Immune checkpoint inhibitors in ovarian cancer: Where do we go from here?., Cancer Drug Resist., 6, p. 358, DOI: 10.20517/cdr.2023.13 27 10.20517/cdr.2023.13 false true Reference 71118914 /api/reference/71118914 28. Czegle, I., Gray, A.L., Wang, M., Liu, Y., Wang, J., and Wappler-Guzzetta, E.A. (2021). Mitochondria and Their Relationship with Common Genetic Abnormalities in Hematologic Malignancies. Life, 11., DOI: 10.3390/life11121351 28 10.3390/life11121351 false true Reference 71118915 /api/reference/71118915 29. Yue, X., Qian, Y., Gim, B., and Lee, I. (2019). Acyl-CoA-Binding Domain-Containing 3 (ACBD3; PAP7; GCP60): A Multi-Functional Membrane Domain Organizer. Int. J. Mol. Sci., 20., DOI: 10.3390/ijms20082028 29 10.3390/ijms20082028 false true Reference 71118916 /api/reference/71118916 30. Osellame 2012: Cellular and molecular mechanisms of mitochondrial function., Best Pract. Res. Clin. Endocrinol. Metab., 26, p. 711, DOI: 10.1016/j.beem.2012.05.003 30 10.1016/j.beem.2012.05.003 false true Reference 71118917 /api/reference/71118917 31. Sun 2025: Structure of human mitochondrial pyruvate carrier MPC1 and MPC2 complex., Nat. Commun., 16, p. 6700, DOI: 10.1038/s41467-025-61939-z 31 10.1038/s41467-025-61939-z false true Reference 71118918 /api/reference/71118918 32. Gustafsson 2016: Maintenance and Expression of Mammalian Mitochondrial DNA., Annu. Rev. Biochem., 85, p. 133, DOI: 10.1146/annurev-biochem-060815-014402 32 10.1146/annurev-biochem-060815-014402 false true Reference 71118919 /api/reference/71118919 33. Hodel 2001: Dissection of a Nuclear Localization Signal., J. Biol. Chem., 276, p. 1317, DOI: 10.1074/jbc.M008522200 33 10.1074/jbc.M008522200 false true Reference 71118920 /api/reference/71118920 34. Falkenberg 2024: Replication and Transcription of Human Mitochondrial DNA., Annu. Rev. Biochem., 93, p. 47, DOI: 10.1146/annurev-biochem-052621-092014 34 10.1146/annurev-biochem-052621-092014 false true Reference 71118922 /api/reference/71118922 35. Liang 2006: PGC-1α: A key regulator of energy metabolism., Adv. Physiol. Educ., 30, p. 145, DOI: 10.1152/advan.00052.2006 35 10.1152/advan.00052.2006 false true Reference 71118923 /api/reference/71118923 36. Zhu 2022: Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization., Cell, 185, p. 2309, DOI: 10.1016/j.cell.2022.05.006 36 10.1016/j.cell.2022.05.006 false true Reference 71118924 /api/reference/71118924 37. Kim 2018: The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress., Cell Metab., 28, p. 516, DOI: 10.1016/j.cmet.2018.06.008 37 10.1016/j.cmet.2018.06.008 false true Reference 71118925 /api/reference/71118925 38. Miller 2020: Peptides derived from small mitochondrial open reading frames: Genomic, biological, and therapeutic implications., Exp. Cell Res., 393, p. 112056, DOI: 10.1016/j.yexcr.2020.112056 38 10.1016/j.yexcr.2020.112056 false true Reference 71118926 /api/reference/71118926 39. Yen 2025: Mitochondrial-derived microproteins: From discovery to function., Trends Genet., 41, p. 132, DOI: 10.1016/j.tig.2024.11.010 39 10.1016/j.tig.2024.11.010 false true Reference 71118927 /api/reference/71118927 40. Serasinghe 2017: Mitochondrial Fission in Human Diseases., Handb. Exp. Pharmacol., 240, p. 159, DOI: 10.1007/164_2016_38 40 10.1007/164_2016_38 false true Reference 71118928 /api/reference/71118928 41. Atkins 2016: The role of Drp1 adaptor proteins MiD49 and MiD51 in mitochondrial fission: Implications for human disease., Clin. Sci., 130, p. 1861, DOI: 10.1042/CS20160030 41 10.1042/CS20160030 false true Reference 71118929 /api/reference/71118929 42. Palmer 2013: Adaptor proteins MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission., J. Biol. Chem., 288, p. 27584, DOI: 10.1074/jbc.M113.479873 42 10.1074/jbc.M113.479873 false true Reference 71118930 /api/reference/71118930 43. Liu, Y., Merrill, R.A., and Strack, S. (2020). A-Kinase Anchoring Protein 1: Emerging Roles in Regulating Mitochondrial Form and Function in Health and Disease. Cells, 9., DOI: 10.3390/cells9020298 43 10.3390/cells9020298 false true Reference 71118931 /api/reference/71118931 44. Pokhrel 2025: A hidden cysteine in Fis1 targeted to prevent excessive mitochondrial fission and dysfunction under oxidative stress., Nat. Commun., 16, p. 4187, DOI: 10.1038/s41467-025-59434-6 44 10.1038/s41467-025-59434-6 false true Reference 71118932 /api/reference/71118932 45. Toyama 2016: Metabolism. AMP-activated protein kinase mediates mitochondrial fission in response to energy stress., Science, 351, p. 275, DOI: 10.1126/science.aab4138 45 10.1126/science.aab4138 false true Reference 71118933 /api/reference/71118933 46. Yu 2019: Human Fis1 regulates mitochondrial dynamics through inhibition of the fusion machinery., EMBO J., 38, p. e99748, DOI: 10.15252/embj.201899748 46 10.15252/embj.201899748 false true Reference 71118934 /api/reference/71118934 47. Elgass 2015: Analysis of ER-mitochondria contacts using correlative fluorescence microscopy and soft X-ray tomography of mammalian cells., J. Cell Sci., 128, p. 2795 47 false true Reference 71118935 /api/reference/71118935 48. Samangouei 2018: MiD49 and MiD51: New mediators of mitochondrial fission and novel targets for cardioprotection., Cond. Med., 1, p. 239 48 false true Reference 71118936 /api/reference/71118936 49. Meng 2015: Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1., Protein Sci., 24, p. 386, DOI: 10.1002/pro.2629 49 10.1002/pro.2629 false true Reference 71118937 /api/reference/71118937 50. Richter 2014: Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission., J. Cell Biol., 204, p. 477, DOI: 10.1083/jcb.201311014 50 10.1083/jcb.201311014 false true Reference 71118938 /api/reference/71118938 51. Liu 2013: The mitochondrial elongation factors MIEF1 and MIEF2 exert partially distinct functions in mitochondrial dynamics., Exp. Cell Res., 319, p. 2893, DOI: 10.1016/j.yexcr.2013.07.010 51 10.1016/j.yexcr.2013.07.010 false true Reference 71118939 /api/reference/71118939 52. Palmer 2011: MiD49 and MiD51, new components of the mitochondrial fission machinery., EMBO Rep., 12, p. 565, DOI: 10.1038/embor.2011.54 52 10.1038/embor.2011.54 false true Reference 71118940 /api/reference/71118940 53. Karbowski 2002: Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis., J. Cell Biol., 159, p. 931, DOI: 10.1083/jcb.200209124 53 10.1083/jcb.200209124 false true Reference 71118941 /api/reference/71118941 54. Osellame 2016: Cooperative and independent roles of the Drp1 adaptors Mff, MiD49 and MiD51 in mitochondrial fission., J. Cell Sci., 129, p. 2170, DOI: 10.1242/jcs.185165 54 10.1242/jcs.185165 false true Reference 71118942 /api/reference/71118942 55. Chandhok 2018: Structure, function, and regulation of mitofusin-2 in health and disease., Biol. Rev. Camb. Philos. Soc., 93, p. 933, DOI: 10.1111/brv.12378 55 10.1111/brv.12378 false true Reference 71118943 /api/reference/71118943 56. Chen 2004: Dysregulation of HSG triggers vascular proliferative disorders., Nat. Cell Biol., 6, p. 872, DOI: 10.1038/ncb1161 56 10.1038/ncb1161 false true Reference 71118944 /api/reference/71118944 57. Cheng 2022: Prognostic impact of mitofusin 2 expression in colon cancer., Transl. Cancer Res., 11, p. 3610, DOI: 10.21037/tcr-22-589 57 10.21037/tcr-22-589 false true Reference 71118945 /api/reference/71118945 58. Ishihara 2004: Mitofusin 1 and 2 play distinct roles in mitochondrial fusion reactions via GTPase activity., J. Cell Sci., 117, p. 6535, DOI: 10.1242/jcs.01565 58 10.1242/jcs.01565 false true Reference 71118946 /api/reference/71118946 59. Li 2019: Structural insights of human mitofusin-2 into mitochondrial fusion and CMT2A onset., Nat. Commun., 10, p. 4914, DOI: 10.1038/s41467-019-12912-0 59 10.1038/s41467-019-12912-0 false true Reference 71118947 /api/reference/71118947 60. Hoppins 2011: The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes., Mol. Cell, 41, p. 150, DOI: 10.1016/j.molcel.2010.11.030 60 10.1016/j.molcel.2010.11.030 false true Reference 71118948 /api/reference/71118948 61. Li 2019: ROR2 induces cell apoptosis via activating IRE1α/JNK/CHOP pathway in high-grade serous ovarian carcinoma in vitro and in vivo., J. Transl. Med., 17, p. 428, DOI: 10.1186/s12967-019-02178-x 61 10.1186/s12967-019-02178-x false true Reference 71118949 /api/reference/71118949 62. Guillery 2008: Metalloprotease-mediated OPA1 processing is modulated by the mitochondrial membrane potential., Biol. Cell, 100, p. 315, DOI: 10.1042/BC20070110 62 10.1042/BC20070110 false true Reference 71118950 /api/reference/71118950 63. Fogazza 2018: Eight human OPA1 isoforms, long and short: What are they for?., Biochim. Biophys. Acta BBA Bioenerg., 1859, p. 263, DOI: 10.1016/j.bbabio.2018.01.005 63 10.1016/j.bbabio.2018.01.005 false true Reference 71118951 /api/reference/71118951 64. Wang 2021: Identification of new OPA1 cleavage site reveals that short isoforms regulate mitochondrial fusion., Mol. Biol. Cell, 32, p. 157, DOI: 10.1091/mbc.E20-09-0605 64 10.1091/mbc.E20-09-0605 false true Reference 71118952 /api/reference/71118952 65. Ge 2020: Two forms of Opa1 cooperate to complete fusion of the mitochondrial inner-membrane., eLife, 9, p. e50973, DOI: 10.7554/eLife.50973 65 10.7554/eLife.50973 false true Reference 71118953 /api/reference/71118953 66. Frezza 2006: OPA1 Controls Apoptotic Cristae Remodeling Independently from Mitochondrial Fusion., Cell, 126, p. 177, DOI: 10.1016/j.cell.2006.06.025 66 10.1016/j.cell.2006.06.025 false true Reference 71118954 /api/reference/71118954 67. Liao 2017: Dysregulated mitophagy and mitochondrial organization in optic atrophy due to OPA1 mutations., Neurology, 88, p. 131, DOI: 10.1212/WNL.0000000000003491 67 10.1212/WNL.0000000000003491 false true Reference 71118955 /api/reference/71118955 68. Elachouri 2011: OPA1 links human mitochondrial genome maintenance to mtDNA replication and distribution., Genome Res., 21, p. 12, DOI: 10.1101/gr.108696.110 68 10.1101/gr.108696.110 false true Reference 71118956 /api/reference/71118956 69. Cartes-Saavedra, B., Macuada, J., Lagos, D., Arancibia, D., Andrés, M.E., Yu-Wai-Man, P., Hajnóczky, G., and Eisner, V. (2022). OPA1 Modulates Mitochondrial Ca2+ Uptake Through ER-Mitochondria Coupling. Front. Cell Dev. Biol., 9., DOI: 10.3389/fcell.2021.774108 69 10.3389/fcell.2021.774108 false true Reference 71118957 /api/reference/71118957 70. Schuler 2020: OPA1 and Angiogenesis: Beyond the Fusion Function., Cell Metab., 31, p. 886, DOI: 10.1016/j.cmet.2020.04.014 70 10.1016/j.cmet.2020.04.014 false true Reference 71118958 /api/reference/71118958 71. Lee 2017: The short variant of the mitochondrial dynamin OPA1 maintains mitochondrial energetics and cristae structure., J. Biol. Chem., 292, p. 7115, DOI: 10.1074/jbc.M116.762567 71 10.1074/jbc.M116.762567 false true Reference 71118959 /api/reference/71118959 72. Yang, L., Tang, H., Lin, X., Wu, Y., Zeng, S., Pan, Y., Li, Y., Xiang, G., Lin, Y.-F., and Zhuang, S.-M. (2020). OPA1-Exon4b Binds to mtDNA D-Loop for Transcriptional and Metabolic Modulation, Independent of Mitochondrial Fusion. Front. Cell Dev. Biol., 8., DOI: 10.3389/fcell.2020.00180 72 10.3389/fcell.2020.00180 false true Reference 71118960 /api/reference/71118960 73. Herkenne 2020: Developmental and Tumor Angiogenesis Requires the Mitochondria-Shaping Protein Opa1., Cell Metab., 31, p. 987, DOI: 10.1016/j.cmet.2020.04.007 73 10.1016/j.cmet.2020.04.007 false true Reference 71118961 /api/reference/71118961 74. Xia 2025: Mitophagy: A key regulator of radiotherapy resistance in the tumor immune microenvironment., Mol. Asp. Med., 105, p. 101385, DOI: 10.1016/j.mam.2025.101385 74 10.1016/j.mam.2025.101385 false true Reference 71118962 /api/reference/71118962 75. Yamano 2020: Critical role of mitochondrial ubiquitination and the OPTN–ATG9A axis in mitophagy., J. Cell Biol., 219, p. e201912144, DOI: 10.1083/jcb.201912144 75 10.1083/jcb.201912144 false true Reference 71118963 /api/reference/71118963 76. Fiesel 2014: A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently., J. Cell Sci., 127, p. 3488 76 false true Reference 71118964 /api/reference/71118964 77. Geisler 2014: UBE2N, UBE2L3 and UBE2D2/3 ubiquitin-conjugating enzymes are essential for parkin-dependent mitophagy., J. Cell Sci., 127, p. 3280 77 false true Reference 71118965 /api/reference/71118965 78. Chen 2024: Mitophagy: Insights into its signaling molecules, biological functions, and therapeutic potential in breast cancer., Cell Death Discov., 10, p. 457, DOI: 10.1038/s41420-024-02226-6 78 10.1038/s41420-024-02226-6 false true Reference 71118966 /api/reference/71118966 79. Chu 2025: Mitophagy: A double-edged sword in tumor cell death regulation and therapeutic response., Biochem. Biophys. Res. Commun., 777, p. 152254, DOI: 10.1016/j.bbrc.2025.152254 79 10.1016/j.bbrc.2025.152254 false true Reference 71118967 /api/reference/71118967 80. Novak 2021: A brief overview of BNIP3L/NIX receptor-mediated mitophagy., FEBS Open Bio, 11, p. 3230, DOI: 10.1002/2211-5463.13307 80 10.1002/2211-5463.13307 false true Reference 71118968 /api/reference/71118968 81. Peschiaroli 2018: HUWE1 E3 ligase promotes PINK1/PARKIN-independent mitophagy by regulating AMBRA1 activation via IKKα., Nat. Commun., 9, p. 3755, DOI: 10.1038/s41467-018-05722-3 81 10.1038/s41467-018-05722-3 false true Reference 71118969 /api/reference/71118969 82. Cornelissen 2011: Ambra1: A Parkin-binding protein involved in mitophagy., Autophagy, 7, p. 1555, DOI: 10.4161/auto.7.12.17893 82 10.4161/auto.7.12.17893 false true Reference 71118970 /api/reference/71118970 83. Chen 2017: Mitochondrial E3 ligase MARCH 5 regulates FUNDC 1 to fine-tune hypoxic mitophagy., EMBO Rep., 18, p. 495, DOI: 10.15252/embr.201643309 83 10.15252/embr.201643309 false true Reference 71118971 /api/reference/71118971 84. Karbowski 2007: The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division., J. Cell Biol., 178, p. 71, DOI: 10.1083/jcb.200611064 84 10.1083/jcb.200611064 false true Reference 71118972 /api/reference/71118972 85. Nakamura 2006: MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology., EMBO Rep., 7, p. 1019, DOI: 10.1038/sj.embor.7400790 85 10.1038/sj.embor.7400790 false true Reference 71118973 /api/reference/71118973 86. Xu 2017: MFN2 suppresses cancer progression through inhibition of mTORC2/Akt signaling., Sci. Rep., 7, p. 41718, DOI: 10.1038/srep41718 86 10.1038/srep41718 false true Reference 71118974 /api/reference/71118974 87. Xu 2024: MARCH5 promotes aerobic glycolysis to facilitate ovarian cancer progression via ubiquitinating MPC1., Apoptosis, 29, p. 1232, DOI: 10.1007/s10495-024-01962-5 87 10.1007/s10495-024-01962-5 false true Reference 71118991 /api/reference/71118991 88. Sherpa 2021: Mitochondrial A-kinase anchoring proteins in cardiac ventricular myocytes., Physiol. Rep., 9, p. e15015, DOI: 10.14814/phy2.15015 88 10.14814/phy2.15015 false true Reference 71118975 /api/reference/71118975 89. Xu 2016: Mitochondrial E3 ubiquitin ligase MARCH5 controls mitochondrial fission and cell sensitivity to stress-induced apoptosis through regulation of MiD49 protein., Mol. Biol. Cell, 27, p. 349, DOI: 10.1091/mbc.e15-09-0678 89 10.1091/mbc.e15-09-0678 false true Reference 71118976 /api/reference/71118976 90. Cherok 2017: Novel regulatory roles of Mff and Drp1 in E3 ubiquitin ligase MARCH5-dependent degradation of MiD49 and Mcl1 and control of mitochondrial dynamics., Mol. Biol. Cell, 28, p. 396, DOI: 10.1091/mbc.e16-04-0208 90 10.1091/mbc.e16-04-0208 false true Reference 71118977 /api/reference/71118977 91. Wu 2023: Novel tumor therapy strategies targeting endoplasmic reticulum-mitochondria signal pathways., Ageing Res. Rev., 88, p. 101951, DOI: 10.1016/j.arr.2023.101951 91 10.1016/j.arr.2023.101951 false true Reference 71118978 /api/reference/71118978 92. Degechisa 2022: The mitochondrial associated endoplasmic reticulum membranes: A platform for the pathogenesis of inflammation-mediated metabolic diseases., Immun. Inflamm. Dis., 10, p. e647, DOI: 10.1002/iid3.647 92 10.1002/iid3.647 false true Reference 71118979 /api/reference/71118979 93. Weaver 2018: Endoplasmic Reticulum-Mitochondrial Contactology: Structure and Signaling Functions., Trends Cell Biol., 28, p. 523, DOI: 10.1016/j.tcb.2018.02.009 93 10.1016/j.tcb.2018.02.009 false true Reference 71118980 /api/reference/71118980 94. Chen 2024: Unraveling the complex interplay between Mitochondria-Associated Membranes (MAMs) and cardiovascular Inflammation: Molecular mechanisms and therapeutic implications., Int. Immunopharmacol., 141, p. 112930, DOI: 10.1016/j.intimp.2024.112930 94 10.1016/j.intimp.2024.112930 false true Reference 71118981 /api/reference/71118981 95. Liu 2025: Mitochondrial-endoplasmic reticulum crosstalk: Molecular mechanisms and implications for cardiovascular disease (Review)., Mol. Med. Rep., 32, p. 275, DOI: 10.3892/mmr.2025.13640 95 10.3892/mmr.2025.13640 false true Reference 71118982 /api/reference/71118982 96. Lalli 2019: ER-mitochondria interactions: Both strength and weakness within cancer cells., Biochim. Biophys. Acta Mol. Cell Res., 1866, p. 650, DOI: 10.1016/j.bbamcr.2019.01.009 96 10.1016/j.bbamcr.2019.01.009 false true Reference 71118983 /api/reference/71118983 97. Kmita, H., Messina, A.A., and De Pinto, V. (2023). VDAC as a Cellular Hub: Docking Molecules and Interactions. Int. J. Mol. Sci., 24., DOI: 10.3390/ijms24076649 97 10.3390/ijms24076649 false true Reference 71118984 /api/reference/71118984 98. Yang 2023: Mitochondria-associated endoplasmic reticulum membrane: Overview and inextricable link with cancer., J. Cell. Mol. Med., 27, p. 906, DOI: 10.1111/jcmm.17696 98 10.1111/jcmm.17696 false true Reference 71118985 /api/reference/71118985 99. Stoica 2012: VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis., Hum. Mol. Genet., 21, p. 1299, DOI: 10.1093/hmg/ddr559 99 10.1093/hmg/ddr559 false true Reference 71118986 /api/reference/71118986 100. He 2024: Novel insight into the role of A-kinase anchoring proteins (AKAPs) in ischemic stroke and therapeutic potentials., Biomed. Pharmacother., 175, p. 116715, DOI: 10.1016/j.biopha.2024.116715 100 10.1016/j.biopha.2024.116715 false true Reference 71118987 /api/reference/71118987 101. Welling, P.A. (2008). Scaffolding Proteins in Transport Regulation (chapter #12). Seldin and Giebisch’s The Kidney, Elsevier. Available online: https://linkinghub.elsevier.com/retrieve/pii/B9780120884889500152., DOI: 10.1016/B978-012088488-9.50015-2 101 10.1016/B978-012088488-9.50015-2 false true Reference 71118988 /api/reference/71118988 102. Liu 2025: Mitochondria-Associated Endoplasmic Reticulum Membranes in Human Health and Diseases., MedComm, 6, p. e70259, DOI: 10.1002/mco2.70259 102 10.1002/mco2.70259 false true Reference 71118989 /api/reference/71118989 103. Flippo 2018: AKAP1 Protects from Cerebral Ischemic Stroke by Inhibiting Drp1-Dependent Mitochondrial Fission., J. Neurosci., 38, p. 8233, DOI: 10.1523/JNEUROSCI.0649-18.2018 103 10.1523/JNEUROSCI.0649-18.2018 false true Reference 71118990 /api/reference/71118990 104. Luo 2025: Proximity-specific ribosome profiling reveals the logic of localized mitochondrial translation., Cell, 188, p. 5589, DOI: 10.1016/j.cell.2025.08.002 104 10.1016/j.cell.2025.08.002 false true Reference 71118992 /api/reference/71118992 105. Wang 2001: Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein., Proc. Natl. Acad. Sci. USA, 98, p. 3220, DOI: 10.1073/pnas.051633398 105 10.1073/pnas.051633398 false true Reference 71118993 /api/reference/71118993 106. Maric, D., Paterek, A., Delaunay, M., López, I.P., Arambasic, M., and Diviani, D. (2021). A-Kinase Anchoring Protein 2 Promotes Protection against Myocardial Infarction. Cells, 10., DOI: 10.3390/cells10112861 106 10.3390/cells10112861 false true Reference 71118994 /api/reference/71118994 107. Daňhelovská, T., Zdražilová, L., Štufková, H., Vanišová, M., Volfová, N., Křížová, J., Kuda, O., Sládková, J., and Tesařová, M. (2021). Knock-Out of ACBD3 Leads to Dispersed Golgi Structure, but Unaffected Mitochondrial Functions in HEK293 and HeLa Cells. Int. J. Mol. Sci., 22., DOI: 10.3390/ijms22147270 107 10.3390/ijms22147270 false true Reference 71118995 /api/reference/71118995 108. Li 2001: Identification, localization, and function in steroidogenesis of PAP7: A peripheral-type benzodiazepine receptor- and PKA (RIα)-associated protein., Mol. Endocrinol., 15, p. 2211 108 false true Reference 71118996 /api/reference/71118996 109. Darshi 2011: ChChd3, an Inner Mitochondrial Membrane Protein, Is Essential for Maintaining Crista Integrity and Mitochondrial Function., J. Biol. Chem., 286, p. 2918, DOI: 10.1074/jbc.M110.171975 109 10.1074/jbc.M110.171975 false true Reference 71118997 /api/reference/71118997 110. Means 2011: An entirely specific type I A-kinase anchoring protein that can sequester two molecules of protein kinase A at mitochondria., Proc. Natl. Acad. Sci. USA, 108, p. E1227, DOI: 10.1073/pnas.1107182108 110 10.1073/pnas.1107182108 false true Reference 71118998 /api/reference/71118998 111. Yang 2019: Sphingosine-1-phosphate signaling modulates terminal erythroid differentiation through the regulation of mitophagy., Exp. Hematol., 72, p. 47, DOI: 10.1016/j.exphem.2019.01.004 111 10.1016/j.exphem.2019.01.004 false true Reference 71118999 /api/reference/71118999 112. Ghazaly 2020: Repression of sphingosine kinase (SK)-interacting protein (SKIP) in acute myeloid leukemia diminishes SK activity and its re-expression restores SK function., J. Biol. Chem., 295, p. 5496, DOI: 10.1074/jbc.RA119.010467 112 10.1074/jbc.RA119.010467 false true Reference 71119000 /api/reference/71119000 113. Hong 2018: Deficiency of Sphingosine-1-Phosphate Reduces the Expression of Prohibitin and Causes β-Cell Impairment via Mitochondrial Dysregulation., Endocrinol. Metab., 33, p. 403, DOI: 10.3803/EnM.2018.33.3.403 113 10.3803/EnM.2018.33.3.403 false true Reference 71119001 /api/reference/71119001 114. Luan 2018: Identification of Wiskott-Aldrich syndrome protein (WASP) binding sites on the branched actin filament nucleator Arp2/3 complex., Proc. Natl. Acad. Sci. USA, 115, p. E1409, DOI: 10.1073/pnas.1716622115 114 10.1073/pnas.1716622115 false true Reference 71119002 /api/reference/71119002 115. Machesky 1999: Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex., Proc. Natl. Acad. Sci. USA, 96, p. 3739, DOI: 10.1073/pnas.96.7.3739 115 10.1073/pnas.96.7.3739 false true Reference 71119003 /api/reference/71119003 116. Kang 2010: WAVE1 regulates Bcl-2 localization and phosphorylation in leukemia cells., Leukemia, 24, p. 177, DOI: 10.1038/leu.2009.224 116 10.1038/leu.2009.224 false true Reference 71119004 /api/reference/71119004 117. Cheng 2007: Pancortin-2 interacts with WAVE1 and Bcl-xL in a mitochondria-associated protein complex that mediates ischemic neuronal death., J. Neurosci., 27, p. 1519, DOI: 10.1523/JNEUROSCI.5154-06.2007 117 10.1523/JNEUROSCI.5154-06.2007 false true Reference 71119005 /api/reference/71119005 118. Danial 2003: BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis., Nature, 424, p. 952, DOI: 10.1038/nature01825 118 10.1038/nature01825 false true Reference 71119006 /api/reference/71119006 119. Bui 2010: Rab32 modulates apoptosis onset and mitochondria-associated membrane (MAM) properties., J. Biol. Chem., 285, p. 31590, DOI: 10.1074/jbc.M110.101584 119 10.1074/jbc.M110.101584 false true Reference 71119024 /api/reference/71119024 120. Yang 2016: Mitochondria and Mitochondrial ROS in Cancer: Novel Targets for Anticancer Therapy., J. Cell. Physiol., 231, p. 2570, DOI: 10.1002/jcp.25349 120 10.1002/jcp.25349 false true Reference 71119007 /api/reference/71119007 121. Cribbs 2007: Reversible phosphorylation of Drp1 by cyclic AMP-dependent protein kinase and calcineurin regulates mitochondrial fission and cell death., EMBO Rep., 8, p. 939, DOI: 10.1038/sj.embor.7401062 121 10.1038/sj.embor.7401062 false true Reference 71119008 /api/reference/71119008 122. Yap 2021: Rab32 uses its effector reticulon 3L to trigger autophagic degradation of mitochondria-associated membrane (MAM) proteins., Biol. Direct, 16, p. 22, DOI: 10.1186/s13062-021-00311-9 122 10.1186/s13062-021-00311-9 false true Reference 71119009 /api/reference/71119009 123. Zhang 2024: A bird’s eye view of mitochondrial unfolded protein response in cancer: Mechanisms, progression and further applications., Cell Death Dis., 15, p. 667, DOI: 10.1038/s41419-024-07049-y 123 10.1038/s41419-024-07049-y false true Reference 71119010 /api/reference/71119010 124. Fiorese 2016: The Transcription Factor ATF5 Mediates a Mammalian Mitochondrial UPR., Curr. Biol., 26, p. 2037, DOI: 10.1016/j.cub.2016.06.002 124 10.1016/j.cub.2016.06.002 false true Reference 71119011 /api/reference/71119011 125. Paerhati, P., Liu, J., Jin, Z., Jakoš, T., Zhu, S., Qian, L., Zhu, J., and Yuan, Y. (2022). Advancements in Activating Transcription Factor 5 Function in Regulating Cell Stress and Survival. Int. J. Mol. Sci., 23., DOI: 10.3390/ijms23137129 125 10.3390/ijms23137129 false true Reference 71119012 /api/reference/71119012 126. Fessler 2020: A pathway coordinated by DELE1 relays mitochondrial stress to the cytosol., Nature, 579, p. 433, DOI: 10.1038/s41586-020-2076-4 126 10.1038/s41586-020-2076-4 false true Reference 71119013 /api/reference/71119013 127. Guo 2020: Mitochondrial stress is relayed to the cytosol by an OMA1-DELE1-HRI pathway., Nature, 579, p. 427, DOI: 10.1038/s41586-020-2078-2 127 10.1038/s41586-020-2078-2 false true Reference 71119014 /api/reference/71119014 128. Adams 2007: Role of the Transcription Factor ATF4 in the Anabolic Actions of Insulin and the Anti-anabolic Actions of Glucocorticoids., J. Biol. Chem., 282, p. 16744, DOI: 10.1074/jbc.M610510200 128 10.1074/jbc.M610510200 false true Reference 71119015 /api/reference/71119015 129. Fusakio 2016: Transcription factor ATF4 directs basal and stress-induced gene expression in the unfolded protein response and cholesterol metabolism in the liver., Mol. Biol. Cell, 27, p. 1536, DOI: 10.1091/mbc.E16-01-0039 129 10.1091/mbc.E16-01-0039 false true Reference 71119016 /api/reference/71119016 130. Yan 2025: The ATF4-glutamine axis: A central node in cancer metabolism, stress adaptation, and therapeutic targeting., Cell Death Discov., 11, p. 390, DOI: 10.1038/s41420-025-02683-7 130 10.1038/s41420-025-02683-7 false true Reference 71119017 /api/reference/71119017 131. Yeh 2017: ATF4 overexpression induces early onset of hyperlipidaemia and hepatic steatosis and enhances adipogenesis in zebrafish., Sci. Rep., 7, p. 16362, DOI: 10.1038/s41598-017-16587-9 131 10.1038/s41598-017-16587-9 false true Reference 71119018 /api/reference/71119018 132. Torres, A.K., Fleischhart, V., and Inestrosa, N.C. (2024). Mitochondrial unfolded protein response (UPRmt): What we know thus far. Front. Cell Dev. Biol., 12., DOI: 10.3389/fcell.2024.1405393 132 10.3389/fcell.2024.1405393 false true Reference 71119019 /api/reference/71119019 133. Charmpilas 2025: The mitochondrial unfolded protein response: Acting near and far., Biol. Chem., 406, p. 229, DOI: 10.1515/hsz-2025-0107 133 10.1515/hsz-2025-0107 false true Reference 71119020 /api/reference/71119020 134. Lee, H.-Y., Nga, H.T., Tian, J., and Yi, H.-S. (2021). Mitochondrial Metabolic Signatures in Hepatocellular Carcinoma. Cells, 10., DOI: 10.3390/cells10081901 134 10.3390/cells10081901 false true Reference 71119021 /api/reference/71119021 135. Ahmed, D.S., Isnard, S., Berini, C., Lin, J., Routy, J.-P., and Royston, L. (2022). Coping With Stress: The Mitokine GDF-15 as a Biomarker of COVID-19 Severity. Front. Immunol., 13., DOI: 10.3389/fimmu.2022.820350 135 10.3389/fimmu.2022.820350 false true Reference 71119022 /api/reference/71119022 136. Jena, J., García-Peña, L.M., and Pereira, R.O. (2023). The roles of FGF21 and GDF15 in mediating the mitochondrial integrated stress response. Front. Endocrinol., 14., DOI: 10.3389/fendo.2023.1264530 136 10.3389/fendo.2023.1264530 false true Reference 71119023 /api/reference/71119023 137. Weinberg 2015: Targeting mitochondria metabolism for cancer therapy., Nat. Chem. Biol., 11, p. 9, DOI: 10.1038/nchembio.1712 137 10.1038/nchembio.1712 false true Reference 71119025 /api/reference/71119025 138. Czegle, I., Huang, C., Soria, P.G., Purkiss, D.W., Shields, A., and Wappler-Guzzetta, E.A. (2023). The Role of Genetic Mutations in Mitochondrial-Driven Cancer Growth in Selected Tumors: Breast and Gynecological Malignancies. Life, 13., DOI: 10.3390/life13040996 138 10.3390/life13040996 false true Reference 71119026 /api/reference/71119026 139. Nantasupha 2021: Metabolic reprogramming in epithelial ovarian cancer., Am. J. Transl. Res., 13, p. 9950 139 false true Reference 71119027 /api/reference/71119027 140. Wang, L., Cybula, M., Rostworowska, M., Wang, L., Mucha, P., Bulicz, M., and Bieniasz, M. (2022). Upregulation of Succinate Dehydrogenase (SDHA) Contributes to Enhanced Bioenergetics of Ovarian Cancer Cells and Higher Sensitivity to Anti-Metabolic Agent Shikonin. Cancers, 14., DOI: 10.3390/cancers14205097 140 10.3390/cancers14205097 false true Reference 71119028 /api/reference/71119028 141. Wang 2021: Clinical Characteristics and Optimal Therapy of Acute Myeloid Leukemia with Myelodysplasia-Related Changes: A Retrospective Analysis of a Cohort of Chinese Patients., Turk. J. Haematol., 38, p. 188 141 false true Reference 71119029 /api/reference/71119029 142. Chen 2011: Inherited Variants in Mitochondrial Biogenesis Genes May Influence Epithelial Ovarian Cancer Risk., Cancer Epidemiol. Biomark. Prev., 20, p. 1131, DOI: 10.1158/1055-9965.EPI-10-1224 142 10.1158/1055-9965.EPI-10-1224 false true Reference 71119030 /api/reference/71119030 143. Koc, Z.C., Sollars, V.E., Bou Zgheib, N., Rankin, G.O., and Koc, E.C. (2023). Evaluation of mitochondrial biogenesis and ROS generation in high-grade serous ovarian cancer. Front. Oncol., 13., DOI: 10.3389/fonc.2023.1129352 143 10.3389/fonc.2023.1129352 false true Reference 71119031 /api/reference/71119031 144. Gentric 2019: PML-Regulated Mitochondrial Metabolism Enhances Chemosensitivity in Human Ovarian Cancers., Cell Metab., 29, p. 156, DOI: 10.1016/j.cmet.2018.09.002 144 10.1016/j.cmet.2018.09.002 false true Reference 71119032 /api/reference/71119032 145. Sun 2023: UQCRFS1 serves as a prognostic biomarker and promotes the progression of ovarian cancer., Sci. Rep., 13, p. 8335, DOI: 10.1038/s41598-023-35572-z 145 10.1038/s41598-023-35572-z false true Reference 71119033 /api/reference/71119033 146. Schusdziarra 2013: Methylation-controlled J-protein MCJ acts in the import of proteins into human mitochondria., Hum. Mol. Genet., 22, p. 1348, DOI: 10.1093/hmg/dds541 146 10.1093/hmg/dds541 false true Reference 71119034 /api/reference/71119034 147. Miglietta 2025: Mitochondrial chaperonin DNAJC15 promotes vulnerability to ferroptosis of chemoresistant ovarian cancer cells., Open Biol., 15, p. 240151, DOI: 10.1098/rsob.240151 147 10.1098/rsob.240151 false true Reference 71119035 /api/reference/71119035 148. Kumar 2013: Metformin intake is associated with better survival in ovarian cancer: A case-control study., Cancer, 119, p. 555, DOI: 10.1002/cncr.27706 148 10.1002/cncr.27706 false true Reference 71119036 /api/reference/71119036 149. Ismail, T., Kim, Y., Lee, H., Lee, D.-S., and Lee, H.-S. (2019). Interplay Between Mitochondrial Peroxiredoxins and ROS in Cancer Development and Progression. Int. J. Mol. Sci., 20., DOI: 10.3390/ijms20184407 149 10.3390/ijms20184407 false true Reference 71119037 /api/reference/71119037 150. Farook 2024: Loss of mitochondrial pyruvate carrier 1 supports proline-dependent proliferation and collagen biosynthesis in ovarian cancer., Mol. Metab., 81, p. 101900, DOI: 10.1016/j.molmet.2024.101900 150 10.1016/j.molmet.2024.101900 false true Reference 71119038 /api/reference/71119038 151. Li 2016: Decreased expression of pyruvate dehydrogenase A1 predicts an unfavorable prognosis in ovarian carcinoma., Am. J. Cancer Res., 6, p. 2076 151 false true Reference 71119039 /api/reference/71119039 152. Dahl 2019: Targeting IDH1 as a Prosenescent Therapy in High-grade Serous Ovarian Cancer., Mol. Cancer Res., 17, p. 1710, DOI: 10.1158/1541-7786.MCR-18-1233 152 10.1158/1541-7786.MCR-18-1233 false true Reference 71119040 /api/reference/71119040 153. Zhou 2019: Dichloroacetic acid upregulates apoptosis of ovarian cancer cells by regulating mitochondrial function., OncoTargets Ther., 12, p. 1729, DOI: 10.2147/OTT.S194329 153 10.2147/OTT.S194329 false true Reference 71119041 /api/reference/71119041 154. Do 2024: Abstract 7155: Dichloroacetate reverses cisplatin resistance in ovarian cancer through promoting ROS production., Cancer Res., 84, p. 7155, DOI: 10.1158/1538-7445.AM2024-7155 154 10.1158/1538-7445.AM2024-7155 false true Reference 71119042 /api/reference/71119042 155. Zhang 2019: Pyruvate dehydrogenase kinase 1 contributes to cisplatin resistance of ovarian cancer through EGFR activation., J. Cell. Physiol., 234, p. 6361, DOI: 10.1002/jcp.27369 155 10.1002/jcp.27369 false true Reference 71119043 /api/reference/71119043 156. Bindra 2021: Mitochondria in epithelial ovarian carcinoma exhibit abnormal phenotypes and blunted associations with biobehavioral factors., Sci. Rep., 11, p. 11595, DOI: 10.1038/s41598-021-89934-6 156 10.1038/s41598-021-89934-6 false true Reference 71119044 /api/reference/71119044 157. Chen, L., Liu, T., Zhou, J., Wang, Y., Wang, X., Di, W., and Zhang, S. (2014). Citrate Synthase Expression Affects Tumor Phenotype and Drug Resistance in Human Ovarian Carcinoma. PLoS ONE, 9., DOI: 10.1371/journal.pone.0115708 157 10.1371/journal.pone.0115708 false true Reference 71119045 /api/reference/71119045 158. Chen 2025: Ivosidenib enhances cisplatin sensitivity in ovarian cancer by reducing cancer cell stemness., Cancer Drug Resist., 8, p. 20 158 false true Reference 71119046 /api/reference/71119046 159. Shang 2020: Integrated analysis of transcriptomic and metabolomic data demonstrates the significant role of pyruvate carboxylase in the progression of ovarian cancer., Aging, 12, p. 21874, DOI: 10.18632/aging.104004 159 10.18632/aging.104004 false true Reference 71119047 /api/reference/71119047 160. Yang 2019: Tankyrase Promotes Aerobic Glycolysis and Proliferation of Ovarian Cancer through Activation of Wnt/β-Catenin Signaling., BioMed Res. Int., 2019, p. 2686340 160 false true Reference 71119048 /api/reference/71119048 161. Matassa 2022: Regulation of mitochondrial complex III activity and assembly by TRAP1 in cancer cells., Cancer Cell Int., 22, p. 402, DOI: 10.1186/s12935-022-02788-4 161 10.1186/s12935-022-02788-4 false true Reference 71119049 /api/reference/71119049 162. Tessarollo 2018: Chemosensitizing effects of metformin on cisplatin- and paclitaxel-resistant ovarian cancer cell lines., Pharmacol. Rep., 70, p. 409, DOI: 10.1016/j.pharep.2017.11.007 162 10.1016/j.pharep.2017.11.007 false true Reference 71119050 /api/reference/71119050 163. Fan, Y., Cheng, H., Liu, Y., Liu, S., Lowe, S., Li, Y., Bentley, R., King, B., Tuason, J.P.W., and Zhou, Q. (2022). Metformin anticancer: Reverses tumor hypoxia induced by bevacizumab and reduces the expression of cancer stem cell markers CD44/CD117 in human ovarian cancer SKOV3 cells. Front. Pharmacol., 13., DOI: 10.3389/fphar.2022.955984 163 10.3389/fphar.2022.955984 false true Reference 71119051 /api/reference/71119051 164. Mikhael, S., Kurdi, A., Khoueiry-Zgheib, N., Tahtouh, R., Nasr, R., and Hilal, G. (2024). Evaluating synergistic effects of metformin and simvastatin on ovarian cancer cells. PLoS ONE, 19., DOI: 10.1371/journal.pone.0298127 164 10.1371/journal.pone.0298127 false true Reference 71119052 /api/reference/71119052 165. Jafarzadeh 2025: Targeting Cancer Stem Cells and Hedgehog Pathway: Enhancing Cisplatin Efficacy in Ovarian Cancer With Metformin., J. Cell. Mol. Med., 29, p. e70508, DOI: 10.1111/jcmm.70508 165 10.1111/jcmm.70508 false true Reference 71119053 /api/reference/71119053 166. Han 2019: Mitochondrial fission causes cisplatin resistance under hypoxic conditions via ROS in ovarian cancer cells., Oncogene, 38, p. 7089, DOI: 10.1038/s41388-019-0949-5 166 10.1038/s41388-019-0949-5 false true Reference 71119054 /api/reference/71119054 167. Matassa 2016: Oxidative metabolism drives inflammation-induced platinum resistance in human ovarian cancer., Cell Death Differ., 23, p. 1542, DOI: 10.1038/cdd.2016.39 167 10.1038/cdd.2016.39 false true Reference 71119055 /api/reference/71119055 168. Ricci 2019: Overcoming platinum-acquired resistance in ovarian cancer patient-derived xenografts., Ther. Adv. Med. Oncol., 11, p. 1758835919839543, DOI: 10.1177/1758835919839543 168 10.1177/1758835919839543 false true Reference 71119056 /api/reference/71119056 169. Wu 2025: Metformin combined with CB-839 specifically inhibits KRAS-mutant ovarian cancer., Sci. Rep., 15, p. 6072, DOI: 10.1038/s41598-025-90963-8 169 10.1038/s41598-025-90963-8 false true Reference 71119057 /api/reference/71119057 170. Zhang 2024: Metformin combined with cisplatin reduces anticancer activity via ATM/CHK2-dependent upregulation of Rad51 pathway in ovarian cancer., Neoplasia, 57, p. 101037, DOI: 10.1016/j.neo.2024.101037 170 10.1016/j.neo.2024.101037 false true Reference 71119058 /api/reference/71119058 171. Ayhan 2023: Does the addition of metformin to carboplatin treatment decreases ovarian reserve damage associated with carboplatin usage?., J. Ovarian Res., 16, p. 184, DOI: 10.1186/s13048-023-01259-2 171 10.1186/s13048-023-01259-2 false true Reference 71119059 /api/reference/71119059 172. Zhang 2025: Metformin Enhances PD-L1 Inhibitor Efficacy in Ovarian Cancer by Modulating the Immune Microenvironment and RBMS3 Expression., FASEB J., 39, p. e70705, DOI: 10.1096/fj.202500906R 172 10.1096/fj.202500906R false true Reference 71119060 /api/reference/71119060 173. Ghilardi 2022: PGC1α/β Expression Predicts Therapeutic Response to Oxidative Phosphorylation Inhibition in Ovarian Cancer., Cancer Res., 82, p. 1423, DOI: 10.1158/0008-5472.CAN-21-1223 173 10.1158/0008-5472.CAN-21-1223 false true Reference 71119061 /api/reference/71119061 174. Fan, Y., Wang, J., Fang, Z., Pierce, S.R., West, L., Staley, A., Tucker, K., Yin, Y., Sun, W., and Kong, W. (2022). Anti-Tumor and Anti-Invasive Effects of ONC201 on Ovarian Cancer Cells and a Transgenic Mouse Model of Serous Ovarian Cancer. Front. Oncol., 12., DOI: 10.3389/fonc.2022.789450 174 10.3389/fonc.2022.789450 false true Reference 71119062 /api/reference/71119062 175. Romero 2025: Metformin for patients with advanced stage ovarian cancer: A randomized phase II placebo-controlled trial., Gynecol. Oncol., 194, p. 18, DOI: 10.1016/j.ygyno.2025.02.001 175 10.1016/j.ygyno.2025.02.001 false true Reference 71119063 /api/reference/71119063 176. Brown 2020: Phase II clinical trial of metformin as a cancer stem cell-targeting agent in ovarian cancer., JCI Insight, 5, p. e133247 176 false true Reference 71119064 /api/reference/71119064 177. Zheng 2019: Metformin plus first-line chemotherapy versus chemotherapy alone in the treatment of epithelial ovarian cancer: A prospective open-label pilot trial., Cancer Chemother. Pharmacol., 84, p. 1349, DOI: 10.1007/s00280-019-03963-7 177 10.1007/s00280-019-03963-7 false true Reference 71119065 /api/reference/71119065 178. Wang 2019: No Effect of Metformin on Ovarian Cancer Survival: A Systematic Review and Meta-Analysis of Cohort Studies., Curr. Pharm. Des., 25, p. 2595, DOI: 10.2174/1381612825666190716113126 178 10.2174/1381612825666190716113126 false true Reference 71119066 /api/reference/71119066 179. Wang 2017: Continuous use of metformin can improve survival in type 2 diabetic patients with ovarian cancer: A retrospective study., Medicine, 96, p. e7605, DOI: 10.1097/MD.0000000000007605 179 10.1097/MD.0000000000007605 false true Reference 71119067 /api/reference/71119067 180. Aspuria 2014: Succinate dehydrogenase inhibition leads to epithelial-mesenchymal transition and reprogrammed carbon metabolism., Cancer Metab., 2, p. 21, DOI: 10.1186/2049-3002-2-21 180 10.1186/2049-3002-2-21 false true Reference 71119068 /api/reference/71119068 181. Lorusso 1997: Revertant and potentiating activity of lonidamine in patients with ovarian cancer previously treated with platinum., J. Clin. Oncol., 15, p. 3208, DOI: 10.1200/JCO.1997.15.10.3208 181 10.1200/JCO.1997.15.10.3208 false true Reference 71119069 /api/reference/71119069 182. Jiang 2023: A traditional gynecological medicine inhibits ovarian cancer progression and eliminates cancer stem cells via the LRPPRC-OXPHOS axis., J. Transl. Med., 21, p. 504, DOI: 10.1186/s12967-023-04349-3 182 10.1186/s12967-023-04349-3 false true Reference 71119070 /api/reference/71119070 183. Zhu 2023: Targeting ATP Synthase by Bedaquiline as a Therapeutic Strategy to Sensitize Ovarian Cancer to Cisplatin., Nutr. Cancer, 75, p. 1271, DOI: 10.1080/01635581.2023.2180825 183 10.1080/01635581.2023.2180825 false true Reference 71119071 /api/reference/71119071 184. Li 2017: Mitochondrial pyruvate carrier function determines cell stemness and metabolic reprogramming in cancer cells., Oncotarget, 8, p. 46363, DOI: 10.18632/oncotarget.18199 184 10.18632/oncotarget.18199 false true Reference 71119072 /api/reference/71119072 185. Patel 2024: Combination of paclitaxel with rosiglitazone induces synergistic cytotoxic effects in ovarian cancer cells., Sci. Rep., 14, p. 30672, DOI: 10.1038/s41598-024-74277-9 185 10.1038/s41598-024-74277-9 false true Reference 71119073 /api/reference/71119073 186. Wang 2020: Rosiglitazone ameliorates senescence and promotes apoptosis in ovarian cancer induced by olaparib., Cancer Chemother. Pharmacol., 85, p. 273, DOI: 10.1007/s00280-019-04025-8 186 10.1007/s00280-019-04025-8 false true Reference 71119074 /api/reference/71119074 187. Al-Alem, L., Southard, R.C., Kilgore, M.W., and Curry, T.E. (2011). Specific Thiazolidinediones Inhibit Ovarian Cancer Cell Line Proliferation and Cause Cell Cycle Arrest in a PPARγ Independent Manner. PLoS ONE, 6., DOI: 10.1371/journal.pone.0016179 187 10.1371/journal.pone.0016179 false true Reference 71119075 /api/reference/71119075 188. Bai 2016: Targeting of topoisomerases for prognosis and drug resistance in ovarian cancer., J. Ovarian Res., 9, p. 35, DOI: 10.1186/s13048-016-0244-9 188 10.1186/s13048-016-0244-9 false true Reference 71119076 /api/reference/71119076 189. Gabrielson, M., Björklund, M., Carlson, J., and Shoshan, M. (2014). Expression of mitochondrial regulators PGC1α and TFAM as putative markers of subtype and chemoresistance in epithelial ovarian carcinoma. PLoS ONE, 9., DOI: 10.1371/journal.pone.0107109 189 10.1371/journal.pone.0107109 false true Reference 71119077 /api/reference/71119077 190. Hu 2020: Impact of mitochondrial transcription factor A expression on the outcomes of ovarian, endometrial and cervical cancers., Am. J. Transl. Res., 12, p. 5343 190 false true Reference 71119078 /api/reference/71119078 191. Kleih 2019: Direct impact of cisplatin on mitochondria induces ROS production that dictates cell fate of ovarian cancer cells., Cell Death Dis., 10, p. 851, DOI: 10.1038/s41419-019-2081-4 191 10.1038/s41419-019-2081-4 false true Reference 71119079 /api/reference/71119079 192. Wu 2022: Mitochondrial transcription factor B2 overexpression increases M2 macrophage infiltration via cytosolic mitochondrial DNA-stimulated Interleukin-6 secretion in ovarian cancer., Bioengineered, 13, p. 12211, DOI: 10.1080/21655979.2022.2074615 192 10.1080/21655979.2022.2074615 false true Reference 71119080 /api/reference/71119080 193. Li, Y., Kang, J., Fu, J., Luo, H., Liu, Y., Li, Y., and Sun, L. (2021). PGC1α Promotes Cisplatin Resistance in Ovarian Cancer by Regulating the HSP70/HK2/VDAC1 Signaling Pathway. Int. J. Mol. Sci., 22., DOI: 10.3390/ijms22052537 193 10.3390/ijms22052537 false true Reference 71119081 /api/reference/71119081 194. Shen 2018: PGC1α promotes cisplatin resistance in human ovarian carcinoma cells through upregulation of mitochondrial biogenesis., Int. J. Oncol., 53, p. 404 194 false true Reference 71119082 /api/reference/71119082 195. Huang 2020: Immunohistochemical Analysis of PGC-1α and ERRα Expression Reveals Their Clinical Significance in Human Ovarian Cancer., OncoTargets Ther., 13, p. 13055, DOI: 10.2147/OTT.S288332 195 10.2147/OTT.S288332 false true Reference 71119083 /api/reference/71119083 196. Yin 2024: Mitochondrial-Derived Peptide MOTS-c Suppresses Ovarian Cancer Progression by Attenuating USP7-Mediated LARS1 Deubiquitination., Adv. Sci., 11, p. 2405620, DOI: 10.1002/advs.202405620 196 10.1002/advs.202405620 false true Reference 71119084 /api/reference/71119084 197. Wang 2006: Association of decreased mitochondrial DNA content with ovarian cancer progression., Br. J. Cancer, 95, p. 1087, DOI: 10.1038/sj.bjc.6603377 197 10.1038/sj.bjc.6603377 false true Reference 71119085 /api/reference/71119085 198. Signorile, A., De Rasmo, D., Cormio, A., Musicco, C., Rossi, R., Fortarezza, F., Palese, L.L., Loizzi, V., Resta, L., and Scillitani, G. (2019). Human Ovarian Cancer Tissue Exhibits Increase of Mitochondrial Biogenesis and Cristae Remodeling. Cancers, 11., DOI: 10.3390/cancers11091350 198 10.3390/cancers11091350 false true Reference 71119086 /api/reference/71119086 199. Shukla 2021: The mitochondrial landscape of ovarian cancer: Emerging insights., Carcinogenesis, 42, p. 663, DOI: 10.1093/carcin/bgab033 199 10.1093/carcin/bgab033 false true Reference 71119087 /api/reference/71119087 200. Meng 2019: Circulating Mitochondrial DNA is Linked to Progression and Prognosis of Epithelial Ovarian Cancer., Transl. Oncol., 12, p. 1213, DOI: 10.1016/j.tranon.2019.05.015 200 10.1016/j.tranon.2019.05.015 false true Reference 71119135 /api/reference/71119135 201. Hu 2017: MARCH5 RNA promotes autophagy, migration, and invasion of ovarian cancer cells., Autophagy, 13, p. 333, DOI: 10.1080/15548627.2016.1256520 201 10.1080/15548627.2016.1256520 false true Reference 71119088 /api/reference/71119088 202. Kong 2015: Single nucleotide polymorphisms in the D-loop region of mitochondrial DNA are associated with epithelial ovarian cancer prognosis., Mitochondrial DNA, 26, p. 848, DOI: 10.3109/19401736.2013.861425 202 10.3109/19401736.2013.861425 false true Reference 71119089 /api/reference/71119089 203. Kong 2016: Single nucleotide polymorphisms in the mitochondrial displacement loop and age-at-onset of epithelial ovarian cancer., Mitochondrial DNA Part A, 27, p. 1141, DOI: 10.3109/19401736.2014.936320 203 10.3109/19401736.2014.936320 false true Reference 71119090 /api/reference/71119090 204. Cui 2024: Targeting mitochondria: A novel approach for treating platinum-resistant ovarian cancer., J. Transl. Med., 22, p. 968, DOI: 10.1186/s12967-024-05770-y 204 10.1186/s12967-024-05770-y false true Reference 71119091 /api/reference/71119091 205. Guerra 2012: Mitochondrial DNA Mutation in Serous Ovarian Cancer: Implications for Mitochondria-Coded Genes in Chemoresistance., J. Clin. Oncol., 30, p. e373, DOI: 10.1200/JCO.2012.43.5933 205 10.1200/JCO.2012.43.5933 false true Reference 71119092 /api/reference/71119092 206. Ni 2020: Pathogenic Heteroplasmic Somatic Mitochondrial DNA Mutation Confers Platinum-Resistance and Recurrence of High-Grade Serous Ovarian Cancer., Cancer Manag. Res., 12, p. 11085, DOI: 10.2147/CMAR.S277724 206 10.2147/CMAR.S277724 false true Reference 71119093 /api/reference/71119093 207. Borgogno 2016: Tolerance of DNA Mismatches in Dmc1 Recombinase-mediated DNA Strand Exchange., J. Biol. Chem., 291, p. 4928, DOI: 10.1074/jbc.M115.704718 207 10.1074/jbc.M115.704718 false true Reference 71119094 /api/reference/71119094 208. Branzei 2017: Building up and breaking down: Mechanisms controlling recombination during replication., Crit. Rev. Biochem. Mol. Biol., 52, p. 381, DOI: 10.1080/10409238.2017.1304355 208 10.1080/10409238.2017.1304355 false true Reference 71119095 /api/reference/71119095 209. Brouwer 2018: Two distinct conformational states define the interaction of human RAD 51-ATP with single-stranded DNA., EMBO J., 37, p. e98162, DOI: 10.15252/embj.201798162 209 10.15252/embj.201798162 false true Reference 71119096 /api/reference/71119096 210. Feng 2021: Predictive value of RAD51 on the survival and drug responsiveness of ovarian cancer., Cancer Cell Int., 21, p. 249, DOI: 10.1186/s12935-021-01953-5 210 10.1186/s12935-021-01953-5 false true Reference 71119097 /api/reference/71119097 211. Ahmed 2025: Mitochondrial dysfunction route as a possible biomarker and therapy target for human cancer., Biomed. J., 48, p. 100714, DOI: 10.1016/j.bj.2024.100714 211 10.1016/j.bj.2024.100714 false true Reference 71119098 /api/reference/71119098 212. De Rasmo, D., Cormio, A., Cormio, G., and Signorile, A. (2023). Ovarian Cancer: A Landscape of Mitochondria with Emphasis on Mitochondrial Dynamics. Int. J. Mol. Sci., 24., DOI: 10.3390/ijms24021224 212 10.3390/ijms24021224 false true Reference 71119099 /api/reference/71119099 213. Dier, U., Shin, D.-H., Hemachandra, L.P.M.P., Uusitalo, L.M., and Hempel, N. (2014). Bioenergetic analysis of ovarian cancer cell lines: Profiling of histological subtypes and identification of a mitochondria-defective cell line. PLoS ONE, 9., DOI: 10.1371/journal.pone.0098479 213 10.1371/journal.pone.0098479 false true Reference 71119100 /api/reference/71119100 214. Tanwar 2016: Crosstalk between the mitochondrial fission protein, Drp1, and the cell cycle is identified across various cancer types and can impact survival of epithelial ovarian cancer patients., Oncotarget, 7, p. 60021, DOI: 10.18632/oncotarget.11047 214 10.18632/oncotarget.11047 false true Reference 71119101 /api/reference/71119101 215. Wang 2017: Nutrient Starvation Sensitizes Human Ovarian Cancer SKOV3 Cells to BH3 Mimetic via Modulation of Mitochondrial Dynamics., Anat. Rec., 300, p. 326, DOI: 10.1002/ar.23454 215 10.1002/ar.23454 false true Reference 71119102 /api/reference/71119102 216. Javed 2024: Drp1 splice variants regulate ovarian cancer mitochondrial dynamics and tumor progression., EMBO Rep., 25, p. 4281, DOI: 10.1038/s44319-024-00232-4 216 10.1038/s44319-024-00232-4 false true Reference 71119103 /api/reference/71119103 217. Farrand, L., Kim, J.Y., Im-Aram, A., Suh, J.-Y., Lee, H.J., and Tsang, B.K. (2013). An Improved Quantitative Approach for the Assessment of Mitochondrial Fragmentation in Chemoresistant Ovarian Cancer Cells. PLoS ONE, 8., DOI: 10.1371/journal.pone.0074008 217 10.1371/journal.pone.0074008 false true Reference 71119104 /api/reference/71119104 218. Zou 2021: Mitochondrial Dynamics Mediated by DRP1 and MFN2 Contributes to Cisplatin Chemoresistance in Human Ovarian Cancer SKOV3 cells., J. Cancer, 12, p. 7358, DOI: 10.7150/jca.61379 218 10.7150/jca.61379 false true Reference 71119105 /api/reference/71119105 219. Ghosh 2023: Ets1 facilitates EMT/invasion through Drp1-mediated mitochondrial fragmentation in ovarian cancer., iScience, 26, p. 107537, DOI: 10.1016/j.isci.2023.107537 219 10.1016/j.isci.2023.107537 false true Reference 71119106 /api/reference/71119106 220. Grieco, J.P., Allen, M.E., Perry, J.B., Wang, Y., Song, Y., Rohani, A., Compton, S.L.E., Smyth, J.W., Swami, N.S., and Brown, D.A. (2021). Progression-Mediated Changes in Mitochondrial Morphology Promotes Adaptation to Hypoxic Peritoneal Conditions in Serous Ovarian Cancer. Front. Oncol., 10., DOI: 10.3389/fonc.2020.600113 220 10.3389/fonc.2020.600113 false true Reference 71119107 /api/reference/71119107 221. Qian 2014: Novel combination of mitochondrial division inhibitor 1 (mdivi-1) and platinum agents produces synergistic pro-apoptotic effect in drug resistant tumor cells., Oncotarget, 5, p. 4180, DOI: 10.18632/oncotarget.1944 221 10.18632/oncotarget.1944 false true Reference 71119108 /api/reference/71119108 222. Zhu 2025: CPT1A-mediated MFF succinylation promotes stemness maintenance in ovarian cancer stem cells., Commun. Biol., 8, p. 250, DOI: 10.1038/s42003-025-07720-w 222 10.1038/s42003-025-07720-w false true Reference 71119109 /api/reference/71119109 223. Zhu 2023: Carnitine palmitoyltransferase 1A promotes mitochondrial fission by enhancing MFF succinylation in ovarian cancer., Commun. Biol., 6, p. 618, DOI: 10.1038/s42003-023-04993-x 223 10.1038/s42003-023-04993-x false true Reference 71119110 /api/reference/71119110 224. Zhao 2020: MIEF2 over-expression promotes tumor growth and metastasis through reprogramming of glucose metabolism in ovarian cancer., J. Exp. Clin. Cancer Res., 39, p. 286, DOI: 10.1186/s13046-020-01802-9 224 10.1186/s13046-020-01802-9 false true Reference 71119111 /api/reference/71119111 225. Cheng, M., Yu, H., Kong, Q., Wang, B., Shen, L., Dong, D., and Sun, L. (2022). The Mitochondrial PHB2/OMA1/DELE1 Pathway Cooperates with Endoplasmic Reticulum Stress to Facilitate the Response to Chemotherapeutics in Ovarian Cancer. Int. J. Mol. Sci., 23., DOI: 10.3390/ijms23031320 225 10.3390/ijms23031320 false true Reference 71119112 /api/reference/71119112 226. Kong 2014: p53 Is Required for Cisplatin-induced Processing of the Mitochondrial Fusion Protein L-Opa1 That Is Mediated by the Mitochondrial Metallopeptidase Oma1 in Gynecologic Cancers., J. Biol. Chem., 289, p. 27134, DOI: 10.1074/jbc.M114.594812 226 10.1074/jbc.M114.594812 false true Reference 71119113 /api/reference/71119113 227. Liao 2022: Mitochondrial AAA protease gene associated with immune infiltration is a prognostic biomarker in human ovarian cancer., Pathol. Res. Pract., 240, p. 154215, DOI: 10.1016/j.prp.2022.154215 227 10.1016/j.prp.2022.154215 false true Reference 71119114 /api/reference/71119114 228. Zhang, S., Wang, Y., Cao, Y., Wu, J., Zhang, Z., Ren, H., Xu, X., Kaznacheyeva, E., Li, Q., and Wang, G. (2022). Inhibition of the PINK1-Parkin Pathway Enhances the Lethality of Sorafenib and Regorafenib in Hepatocellular Carcinoma. Front. Pharmacol., 13., DOI: 10.3389/fphar.2022.851832 228 10.3389/fphar.2022.851832 false true Reference 71119115 /api/reference/71119115 229. Yan 2020: Insight into the role of p62 in the cisplatin resistant mechanisms of ovarian cancer., Cancer Cell Int., 20, p. 128, DOI: 10.1186/s12935-020-01196-w 229 10.1186/s12935-020-01196-w false true Reference 71119116 /api/reference/71119116 230. Zheng 2023: PINK1-PTEN axis promotes metastasis and chemoresistance in ovarian cancer via non-canonical pathway., J. Exp. Clin. Cancer Res., 42, p. 295, DOI: 10.1186/s13046-023-02823-w 230 10.1186/s13046-023-02823-w false true Reference 71119117 /api/reference/71119117 231. Tanbir 2025: SREBP1a induced PINK1-Parkin mediated mitophagy facilitates ovarian cancer progression., Biochim. Biophys. Acta Mol. Basis Dis., 1872, p. 168043, DOI: 10.1016/j.bbadis.2025.168043 231 10.1016/j.bbadis.2025.168043 false true Reference 71119136 /api/reference/71119136 232. Fan 2022: MCUR1 is a prognostic biomarker for ovarian cancer patients., Cancer Biomark., 33, p. 311, DOI: 10.3233/CBM-210166 232 10.3233/CBM-210166 false true Reference 71119118 /api/reference/71119118 233. Hu 2020: Chaetomugilin J Enhances Apoptosis in Human Ovarian Cancer A2780 Cells Induced by Cisplatin Through Inhibiting Pink1/Parkin Mediated Mitophagy., OncoTargets Ther., 13, p. 9967, DOI: 10.2147/OTT.S273435 233 10.2147/OTT.S273435 false true Reference 71119119 /api/reference/71119119 234. Zhang 2017: Sorafenib targets the mitochondrial electron transport chain complexes and ATP synthase to activate the PINK1-Parkin pathway and modulate cellular drug response., J. Biol. Chem., 292, p. 15105, DOI: 10.1074/jbc.M117.783175 234 10.1074/jbc.M117.783175 false true Reference 71119120 /api/reference/71119120 235. Iwadate 2015: High Expression of p62 Protein Is Associated with Poor Prognosis and Aggressive Phenotypes in Endometrial Cancer., Am. J. Pathol., 185, p. 2523, DOI: 10.1016/j.ajpath.2015.05.008 235 10.1016/j.ajpath.2015.05.008 false true Reference 71119121 /api/reference/71119121 236. 2022: Prognostic relevance of autophagy-related markers p62, LC3, and Beclin1 in ovarian cancer., Croat. Med. J., 63, p. 453, DOI: 10.3325/cmj.2022.63.453 236 10.3325/cmj.2022.63.453 false true Reference 71119122 /api/reference/71119122 237. Wang 2018: Expression and role of autophagy-associated p62 (SQSTM1) in multidrug resistant ovarian cancer., Gynecol. Oncol., 150, p. 143, DOI: 10.1016/j.ygyno.2018.04.557 237 10.1016/j.ygyno.2018.04.557 false true Reference 71119123 /api/reference/71119123 238. Yu 2011: p62/SQSTM1 involved in cisplatin resistance in human ovarian cancer cells by clearing ubiquitinated proteins., Eur. J. Cancer, 47, p. 1585, DOI: 10.1016/j.ejca.2011.01.019 238 10.1016/j.ejca.2011.01.019 false true Reference 71119124 /api/reference/71119124 239. Tamura 2025: mTOR-mediated p62/SQSTM1 stabilization confers a robust survival mechanism for ovarian cancer., Cancer Lett., 616, p. 217565, DOI: 10.1016/j.canlet.2025.217565 239 10.1016/j.canlet.2025.217565 false true Reference 71119125 /api/reference/71119125 240. Chao 2017: Lysine-specific demethylase 1 (LSD1) destabilizes p62 and inhibits autophagy in gynecologic malignancies., Oncotarget, 8, p. 74434, DOI: 10.18632/oncotarget.20158 240 10.18632/oncotarget.20158 false true Reference 71119126 /api/reference/71119126 241. Zhu 2020: UBE2N Regulates Paclitaxel Sensitivity of Ovarian Cancer via Fos/P53 Axis., OncoTargets Ther., 13, p. 12751, DOI: 10.2147/OTT.S271164 241 10.2147/OTT.S271164 false true Reference 71119127 /api/reference/71119127 242. Fan 2019: Deletion of SMURF 1 represses ovarian cancer invasion and EMT by modulating the DAB2IP/AKT/Skp2 feedback loop., J. Cell. Biochem., 120, p. 10643, DOI: 10.1002/jcb.28354 242 10.1002/jcb.28354 false true Reference 71119128 /api/reference/71119128 243. Li 2016: shRNA-mediated AMBRA1 knockdown reduces the cisplatin-induced autophagy and sensitizes ovarian cancer cells to cisplatin., J. Toxicol. Sci., 41, p. 45, DOI: 10.2131/jts.41.45 243 10.2131/jts.41.45 false true Reference 71119129 /api/reference/71119129 244. Jia 2020: BNIP3 contributes to cisplatin-induced apoptosis in ovarian cancer cells., FEBS Open Bio, 10, p. 1463, DOI: 10.1002/2211-5463.12881 244 10.1002/2211-5463.12881 false true Reference 71119130 /api/reference/71119130 245. Fan 2025: BNIP3 as a potential target of esculetin for treating ovarian cancer and prognostic biomarker in ovarian cancer patients., Eur. J. Pharmacol., 999, p. 177698, DOI: 10.1016/j.ejphar.2025.177698 245 10.1016/j.ejphar.2025.177698 false true Reference 71119131 /api/reference/71119131 246. Wang 2025: TAM-derived exosomal miR-589-3p accelerates ovarian cancer progression through BCL2L13., J. Ovarian Res., 18, p. 36, DOI: 10.1186/s13048-025-01618-1 246 10.1186/s13048-025-01618-1 false true Reference 71119132 /api/reference/71119132 247. Yuan, Q., Sun, N., Zheng, J., Wang, Y., Yan, X., Mai, W., Liao, Y., and Chen, X. (2019). Prognostic and Immunological Role of FUN14 Domain Containing 1 in Pan-Cancer: Friend or Foe?. Front. Oncol., 9., DOI: 10.3389/fonc.2019.01502 247 10.3389/fonc.2019.01502 false true Reference 71119133 /api/reference/71119133 248. Wu 2024: Blockade of the lncRNA-PART1-PHB2 axis confers resistance to PARP inhibitor and promotes cellular senescence in ovarian cancer., Cancer Lett., 602, p. 217192, DOI: 10.1016/j.canlet.2024.217192 248 10.1016/j.canlet.2024.217192 false true Reference 71119134 /api/reference/71119134 249. Tang 2019: Inhibition LC3B can increase chemosensitivity of ovarian cancer cells., Cancer Cell Int., 19, p. 199, DOI: 10.1186/s12935-019-0921-z 249 10.1186/s12935-019-0921-z false true Reference 71119137 /api/reference/71119137 250. Chakraborty 2017: MICU1 drives glycolysis and chemoresistance in ovarian cancer., Nat. Commun., 8, p. 14634, DOI: 10.1038/ncomms14634 250 10.1038/ncomms14634 false true Reference 71119138 /api/reference/71119138 251. Arvizo 2013: Probing novel roles of the mitochondrial uniporter in ovarian cancer cells using nanoparticles., J. Biol. Chem., 288, p. 17610, DOI: 10.1074/jbc.M112.435206 251 10.1074/jbc.M112.435206 false true Reference 71119139 /api/reference/71119139 252. Rezuchova 2019: Type 3 inositol 1,4,5-trisphosphate receptor has antiapoptotic and proliferative role in cancer cells., Cell Death Dis., 10, p. 186, DOI: 10.1038/s41419-019-1433-4 252 10.1038/s41419-019-1433-4 false true Reference 71119140 /api/reference/71119140 253. Xie 2018: TAT-fused IP3R-derived peptide enhances cisplatin sensitivity of ovarian cancer cells by increasing ER Ca2+ release., Int. J. Mol. Med., 41, p. 809 253 false true Reference 71119141 /api/reference/71119141 254. Li 2022: GRP75-faciliated Mitochondria-associated ER Membrane (MAM) Integrity controls Cisplatin-resistance in Ovarian Cancer Patients., Int. J. Biol. Sci., 18, p. 2914, DOI: 10.7150/ijbs.71571 254 10.7150/ijbs.71571 false true Reference 71119142 /api/reference/71119142 255. Li 2017: AKAP2 is upregulated in ovarian cancer, and promotes growth and migration of cancer cells., Mol. Med. Rep., 16, p. 5151, DOI: 10.3892/mmr.2017.7286 255 10.3892/mmr.2017.7286 false true Reference 71119143 /api/reference/71119143 256. Zhang 2012: High level of WAVE1 expression is associated with tumor aggressiveness and unfavorable prognosis of epithelial ovarian cancer., Gynecol. Oncol., 127, p. 223, DOI: 10.1016/j.ygyno.2012.06.008 256 10.1016/j.ygyno.2012.06.008 false true Reference 71119144 /api/reference/71119144 257. Zhang 2013: WAVE1 gene silencing via RNA interference reduces ovarian cancer cell invasion, migration and proliferation., Gynecol. Oncol., 130, p. 354, DOI: 10.1016/j.ygyno.2013.05.005 257 10.1016/j.ygyno.2013.05.005 false true Reference 71119145 /api/reference/71119145 258. Chen 2012: ATF5 is overexpressed in epithelial ovarian carcinomas and interference with its function increases apoptosis through the downregulation of Bcl-2 in SKOV-3 cells., Int. J. Gynecol. Pathol., 31, p. 532, DOI: 10.1097/PGP.0b013e31824df26b 258 10.1097/PGP.0b013e31824df26b false true Reference 71119146 /api/reference/71119146 259. Ishihara 2025: Stiff extracellular matrix activates the transcription factor ATF5 to promote the proliferation of cancer cells., iScience, 28, p. 112057, DOI: 10.1016/j.isci.2025.112057 259 10.1016/j.isci.2025.112057 false true Reference 71119147 /api/reference/71119147 260. Zhong 2022: Fibroblast growth factor 21 is related to cisplatin resistance in ovarian cancer., Chin. Med. J., 135, p. 1500, DOI: 10.1097/CM9.0000000000002095 260 10.1097/CM9.0000000000002095 false true Reference 71119148 /api/reference/71119148 261. Griner 2013: Growth differentiation factor 15 stimulates rapamycin-sensitive ovarian cancer cell growth and invasion., Biochem. Pharmacol., 85, p. 46, DOI: 10.1016/j.bcp.2012.10.007 261 10.1016/j.bcp.2012.10.007 false true Reference 71119149 /api/reference/71119149 262. Wang 2025: GDF15 drives de novo lipogenesis and contributes to ovarian cancer metastasis., Biochim. Biophys. Acta BBA Mol. Basis Dis., 1871, p. 167868, DOI: 10.1016/j.bbadis.2025.167868 262 10.1016/j.bbadis.2025.167868 false true Reference 71119150 /api/reference/71119150 263. Boso 2023: Anti-VEGF therapy selects for clones resistant to glucose starvation in ovarian cancer xenografts., J. Exp. Clin. Cancer Res., 42, p. 196, DOI: 10.1186/s13046-023-02779-x 263 10.1186/s13046-023-02779-x false true Reference 71119151 /api/reference/71119151 264. Boso 2024: Pathogenic mitochondrial DNA variants are associated with response to anti-VEGF therapy in ovarian cancer PDX models., J. Exp. Clin. Cancer Res., 43, p. 325, DOI: 10.1186/s13046-024-03239-w 264 10.1186/s13046-024-03239-w false true Reference 71119152 /api/reference/71119152 265. Kawahara 2017: Candidate synthetic lethality partners to PARP inhibitors in the treatment of ovarian clear cell cancer., Biomed. Rep., 7, p. 391, DOI: 10.3892/br.2017.990 265 10.3892/br.2017.990 false true Reference 71119153 /api/reference/71119153 266. Nussenzweig 2017: The multifaceted roles of PARP1 in DNA repair and chromatin remodelling., Nat. Rev. Mol. Cell Biol., 18, p. 610, DOI: 10.1038/nrm.2017.53 266 10.1038/nrm.2017.53 false true Reference 71119154 /api/reference/71119154 267. Friedlander 2018: Health-related quality of life and patient-centred outcomes with olaparib maintenance after chemotherapy in patients with platinum-sensitive, relapsed ovarian cancer and a BRCA1/2 mutation (SOLO2/ENGOT Ov-21): A placebo-controlled, phase 3 randomised trial., Lancet Oncol., 19, p. 1126, DOI: 10.1016/S1470-2045(18)30343-7 267 10.1016/S1470-2045(18)30343-7 false true Reference 71119155 /api/reference/71119155 268. Ledermann 2016: Overall survival in patients with platinum-sensitive recurrent serous ovarian cancer receiving olaparib maintenance monotherapy: An updated analysis from a randomised, placebo-controlled, double-blind, phase 2 trial., Lancet Oncol., 17, p. 1579, DOI: 10.1016/S1470-2045(16)30376-X 268 10.1016/S1470-2045(16)30376-X false true Reference 71119156 /api/reference/71119156 269. Coleman 2017: Bevacizumab and paclitaxel–carboplatin chemotherapy and secondary cytoreduction in recurrent, platinum-sensitive ovarian cancer (NRG Oncology/Gynecologic Oncology Group study GOG-0213): A multicentre, open-label, randomised, phase 3 trial., Lancet Oncol., 18, p. 779, DOI: 10.1016/S1470-2045(17)30279-6 269 10.1016/S1470-2045(17)30279-6 false true Reference 71119157 /api/reference/71119157 270. Mirza 2016: Niraparib Maintenance Therapy in Platinum-Sensitive, Recurrent Ovarian Cancer., N. Engl. J. Med., 375, p. 2154, DOI: 10.1056/NEJMoa1611310 270 10.1056/NEJMoa1611310 false true Reference 71119158 /api/reference/71119158 271. Bahar, E., Kim, J.-Y., Kim, D.-C., Kim, H.-S., and Yoon, H. (2021). Combination of Niraparib, Cisplatin and Twist Knockdown in Cisplatin-Resistant Ovarian Cancer Cells Potentially Enhances Synthetic Lethality through ER-Stress Mediated Mitochondrial Apoptosis Pathway. Int. J. Mol. Sci., 22., DOI: 10.3390/ijms22083916 271 10.3390/ijms22083916 false true Reference 71119159 /api/reference/71119159 272. Hou 2018: Increased oxidative stress mediates the antitumor effect of PARP inhibition in ovarian cancer., Redox Biol., 17, p. 99, DOI: 10.1016/j.redox.2018.03.016 272 10.1016/j.redox.2018.03.016 false true Reference 71119160 /api/reference/71119160 273. Gao 2025: Olaparib Triggers Mitochondrial Fission Through the CDK5/Drp-1 Signaling Pathway in Ovarian Cancer Cells., J. Biochem. Mol. Toxicol., 39, p. e70273, DOI: 10.1002/jbt.70273 273 10.1002/jbt.70273 false true Reference 71119161 /api/reference/71119161 274. Yang 2004: Twist, a Master Regulator of Morphogenesis, Plays an Essential Role in Tumor Metastasis., Cell, 117, p. 927, DOI: 10.1016/j.cell.2004.06.006 274 10.1016/j.cell.2004.06.006 false true Reference 71119162 /api/reference/71119162 275. Ohuchida 2007: Twist, a novel oncogene, is upregulated in pancreatic cancer: Clinical implication of Twist expression in pancreatic juice., Int. J. Cancer, 120, p. 1634, DOI: 10.1002/ijc.22295 275 10.1002/ijc.22295 false true Reference 71119163 /api/reference/71119163 276. Kang 2004: Epithelial-Mesenchymal Transitions., Cell, 118, p. 277, DOI: 10.1016/j.cell.2004.07.011 276 10.1016/j.cell.2004.07.011 false true Reference 71119164 /api/reference/71119164 277. Bahar, E., Kim, J.-Y., Kim, H.-S., and Yoon, H. (2020). Establishment of Acquired Cisplatin Resistance in Ovarian Cancer Cell Lines Characterized by Enriched Metastatic Properties with Increased Twist Expression. Int. J. Mol. Sci., 21., DOI: 10.3390/ijms21207613 277 10.3390/ijms21207613 false true Reference 71119165 /api/reference/71119165 278. Maestro 1999: twist is a potential oncogene that inhibits apoptosis., Genes Dev., 13, p. 2207, DOI: 10.1101/gad.13.17.2207 278 10.1101/gad.13.17.2207 false true Reference 71119166 /api/reference/71119166 279. Magdeleine 2004: Oncogenic cooperation between H-Twist and N-Myc overrides failsafe programs in cancer cells., Cancer Cell, 6, p. 625, DOI: 10.1016/j.ccr.2004.09.033 279 10.1016/j.ccr.2004.09.033 false true Reference 71119167 /api/reference/71119167 280. Roberts 2016: TWIST1 drives cisplatin resistance and cell survival in an ovarian cancer model, via upregulation of GAS6, L1CAM, and Akt signalling., Sci. Rep., 6, p. 37652, DOI: 10.1038/srep37652 280 10.1038/srep37652 false true Reference 71119168 /api/reference/71119168 281. Cheng 2007: Twist Transcriptionally Up-regulates AKT2 in Breast Cancer Cells Leading to Increased Migration, Invasion, and Resistance to Paclitaxel., Cancer Res., 67, p. 1979, DOI: 10.1158/0008-5472.CAN-06-1479 281 10.1158/0008-5472.CAN-06-1479 false true Reference 71119169 /api/reference/71119169 282. Ellgaard 2003: Quality control in the endoplasmic reticulum., Nat. Rev. Mol. Cell Biol., 4, p. 181, DOI: 10.1038/nrm1052 282 10.1038/nrm1052 false true Reference 71119170 /api/reference/71119170 283. Csala 2010: Redox Control of Endoplasmic Reticulum Function., Antioxid. Redox Signal., 13, p. 77, DOI: 10.1089/ars.2009.2529 283 10.1089/ars.2009.2529 false true Reference 71119171 /api/reference/71119171 284. Read, A., and Schröder, M. (2021). The Unfolded Protein Response: An Overview. Biology, 10., DOI: 10.3390/biology10050384 284 10.3390/biology10050384 false true Reference 71119172 /api/reference/71119172 285. Oakes 2015: The Role of Endoplasmic Reticulum Stress in Human Pathology., Annu. Rev. Pathol. Mech. Dis., 10, p. 173, DOI: 10.1146/annurev-pathol-012513-104649 285 10.1146/annurev-pathol-012513-104649 false true Reference 71119173 /api/reference/71119173 286. Hetz 2012: The unfolded protein response: Controlling cell fate decisions under ER stress and beyond., Nat. Rev. Mol. Cell Biol., 13, p. 89, DOI: 10.1038/nrm3270 286 10.1038/nrm3270 false true Reference 71119174 /api/reference/71119174 287. Senft 2015: UPR, autophagy, and mitochondria crosstalk underlies the ER stress response., Trends Biochem. Sci., 40, p. 141, DOI: 10.1016/j.tibs.2015.01.002 287 10.1016/j.tibs.2015.01.002 false true Reference 71119175 /api/reference/71119175 288. Walter 2011: The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation., Science, 334, p. 1081, DOI: 10.1126/science.1209038 288 10.1126/science.1209038 false true Reference 71119176 /api/reference/71119176 289. Hetz 2013: Targeting the unfolded protein response in disease., Nat. Rev. Drug Discov., 12, p. 703, DOI: 10.1038/nrd3976 289 10.1038/nrd3976 false true Reference 71119177 /api/reference/71119177 290. Verfaillie 2013: Pro-apoptotic signaling induced by photo-oxidative ER stress is amplified by Noxa, not Bim., Biochem. Biophys. Res. Commun., 438, p. 500, DOI: 10.1016/j.bbrc.2013.07.107 290 10.1016/j.bbrc.2013.07.107 false true Reference 71119178 /api/reference/71119178 291. Rutkowski, D.T., Arnold, S.M., Miller, C.N., Wu, J., Li, J., Gunnison, K.M., Mori, K., Sadighi Akha, A.A., Raden, D., and Kaufman, R.J. (2006). Adaptation to ER Stress Is Mediated by Differential Stabilities of Pro-Survival and Pro-Apoptotic mRNAs and Proteins. PLoS Biol., 4., DOI: 10.1371/journal.pbio.0040374 291 10.1371/journal.pbio.0040374 false true Reference 71119179 /api/reference/71119179 292. Lei 2024: Molecular mechanism of ATF6 in unfolded protein response and its role in disease., Heliyon, 10, p. e25937, DOI: 10.1016/j.heliyon.2024.e25937 292 10.1016/j.heliyon.2024.e25937 false true Reference 71119180 /api/reference/71119180 293. Ong 2024: IRE1 signaling increases PERK expression during chronic ER stress., Cell Death Dis., 15, p. 276, DOI: 10.1038/s41419-024-06663-0 293 10.1038/s41419-024-06663-0 false true Reference 71119181 /api/reference/71119181 294. Bernasconi 2011: ERAD and ERAD tuning: Disposal of cargo and of ERAD regulators from the mammalian ER., Curr. Opin. Cell Biol., 23, p. 176, DOI: 10.1016/j.ceb.2010.10.002 294 10.1016/j.ceb.2010.10.002 false true Reference 71119182 /api/reference/71119182 295. Meusser 2005: ERAD: The long road to destruction., Nat. Cell Biol., 7, p. 766, DOI: 10.1038/ncb0805-766 295 10.1038/ncb0805-766 false true Reference 71119183 /api/reference/71119183 296. Nagakannan 2016: Perturbation of redox balance after thioredoxin reductase deficiency interrupts autophagy-lysosomal degradation pathway and enhances cell death in nutritionally stressed SH-SY5Y cells., Free Radic. Biol. Med., 101, p. 53, DOI: 10.1016/j.freeradbiomed.2016.09.026 296 10.1016/j.freeradbiomed.2016.09.026 false true Reference 71119184 /api/reference/71119184 297. Araki 2011: Protein Folding and Quality Control in the ER., Cold Spring Harb. Perspect. Biol., 3, p. a007526, DOI: 10.1101/cshperspect.a007526 297 10.1101/cshperspect.a007526 false true Reference 71119185 /api/reference/71119185 298. Shimizu 2010: Ubiquitylation of an ERAD Substrate Occurs on Multiple Types of Amino Acids., Mol. Cell, 40, p. 917, DOI: 10.1016/j.molcel.2010.11.033 298 10.1016/j.molcel.2010.11.033 false true Reference 71119186 /api/reference/71119186 299. Bertolotti 2000: Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response., Nat. Cell Biol., 2, p. 326, DOI: 10.1038/35014014 299 10.1038/35014014 false true Reference 71119187 /api/reference/71119187 300. Hetz 2009: The UPR as a survival factor of cancer cells: More than folding proteins?., Leuk. Res., 33, p. 880, DOI: 10.1016/j.leukres.2009.02.017 300 10.1016/j.leukres.2009.02.017 false true Reference 71119188 /api/reference/71119188 301. Lin 2019: Cancer and ER stress: Mutual crosstalk between autophagy, oxidative stress and inflammatory response., Biomed. Pharmacother., 118, p. 109249, DOI: 10.1016/j.biopha.2019.109249 301 10.1016/j.biopha.2019.109249 false true Reference 71119189 /api/reference/71119189 302. Yan 2023: Targeting endoplasmic reticulum stress signaling in ovarian cancer therapy., Cancer Biol. Med., 20, p. 748 302 false true Reference 71119190 /api/reference/71119190 303. Samanta 2017: Expression of protein disulfide isomerase family members correlates with tumor progression and patient survival in ovarian cancer., Oncotarget, 8, p. 103543, DOI: 10.18632/oncotarget.21569 303 10.18632/oncotarget.21569 false true Reference 71119191 /api/reference/71119191 304. Samanta 2020: Clinicopathological significance of endoplasmic reticulum stress proteins in ovarian carcinoma., Sci. Rep., 10, p. 2160, DOI: 10.1038/s41598-020-59116-x 304 10.1038/s41598-020-59116-x false true Reference 71119192 /api/reference/71119192 305. Zhang, M., Wang, Y., Xu, S., Huang, S., Wu, M., Chen, G., and Wang, Y. (2023). Endoplasmic Reticulum Stress-Related Ten-Biomarker Risk Classifier for Survival Evaluation in Epithelial Ovarian Cancer and TRPM2: A Potential Therapeutic Target of Ovarian Cancer. Int. J. Mol. Sci., 24., DOI: 10.3390/ijms241814010 305 10.3390/ijms241814010 false true Reference 71119193 /api/reference/71119193 306. Zhang, R., Zhang, Z., Xie, L., Yu, Z., Gao, R., Zhang, Z.-R., Zhang, Y., Wei, X., Chen, Y., and Jiao, S. (2025). In vitro analysis of the molecular mechanisms of ursolic acid against ovarian cancer. BMC Complement. Med. Ther., 25., DOI: 10.1186/s12906-025-04808-y 306 10.1186/s12906-025-04808-y false true Reference 71119194 /api/reference/71119194 307. Yang 2025: Crosstalk between ferroptosis and endoplasmic reticulum stress: A potential target for ovarian cancer therapy (Review)., Int. J. Mol. Med., 55, p. 97, DOI: 10.3892/ijmm.2025.5538 307 10.3892/ijmm.2025.5538 false true Reference 71119195 /api/reference/71119195 308. Jung 2020: Overcoming Multidrug Resistance by Activating Unfolded Protein Response of the Endoplasmic Reticulum in Cisplatin-Resistant A2780/CisR Ovarian Cancer Cells., BMB Rep., 53, p. 88, DOI: 10.5483/BMBRep.2020.53.2.108 308 10.5483/BMBRep.2020.53.2.108 false true Reference 71119196 /api/reference/71119196 309. Agalakova, N.I. (2025). Modulation of Endoplasmic Reticulum Stress in Experimental Anti-Cancer Therapy. Int. J. Mol. Sci., 26., DOI: 10.3390/ijms26136407 309 10.3390/ijms26136407 false true Reference 71119197 /api/reference/71119197 310. Horak 2015: Tumor suppressor candidate 3 (TUSC3) prevents the epithelial-to-mesenchymal transition and inhibits tumor growth by modulating the endoplasmic reticulum stress response in ovarian cancer cells., Int. J. Cancer, 137, p. 1330, DOI: 10.1002/ijc.29502 310 10.1002/ijc.29502 false true Reference 71119198 /api/reference/71119198 311. Silberman 2015: ER Stress Sensor XBP1 Controls Anti-tumor Immunity by Disrupting Dendritic Cell Homeostasis., Cell, 161, p. 1527, DOI: 10.1016/j.cell.2015.05.025 311 10.1016/j.cell.2015.05.025 false true Reference 71119199 /api/reference/71119199 312. Song 2018: IRE1α–XBP1 controls T cell function in ovarian cancer by regulating mitochondrial activity., Nature, 562, p. 423, DOI: 10.1038/s41586-018-0597-x 312 10.1038/s41586-018-0597-x false true Reference 71119200 /api/reference/71119200 313. Chen, Q., Li, C., Wei, W., Li, J., Liu, F., Fu, Y., Tang, L., and Han, F. (2024). Endoplasmic reticulum stress response pathway-mediated cell death in ovarian cancer. Front. Oncol., 14., DOI: 10.3389/fonc.2024.1446552 313 10.3389/fonc.2024.1446552 false true Reference 71119201 /api/reference/71119201 314. Li 2014: Cisplatin-induced senescence in ovarian cancer cells is mediated by GRP78., Oncol. Rep., 31, p. 2525, DOI: 10.3892/or.2014.3147 314 10.3892/or.2014.3147 false true /api/publication/36833696 Wappler-Guzzetta Edina Amalia et al. Subcellular Stress Markers in Epithelial Ovarian Cancer. (2026) INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 1661-6596 1422-0067 27 1<div class="JournalArticle Publication long-list"> <div class="authors"> <img title="Forrásközlemény" style="float: left" src="/frontend/resources/grid/publication-core-icon.png"> <img title="Idézőközlemény" style="float: left" src="/frontend/resources/grid/publication-citation-icon.png"> <div class="autype autype0"> <span class="author-name" >Wappler-Guzzetta Edina Amalia </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10015704"><a href="/gui2/?type=authors&mode=browse&sel=10015704" target="_blank">Margittai Eva (<span class="authorship-author-name">Margittai Éva</span> <span class="authorAux-mtmt"> Molekuláris Biológiai</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Transzlációs Medicina Intézet</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10074867"><a href="/gui2/?type=authors&mode=browse&sel=10074867" target="_blank">Veszelyi Krisztina (<span class="authorship-author-name">Veszelyi Krisztina Nóra</span> <span class="authorAux-mtmt"> molekuláris biológia</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Intézet">I</span>/Transzlációs Medicina Intézet</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Pickard Shanel </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" >Merwin Caroline </span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10003519"><a href="/gui2/?type=authors&mode=browse&sel=10003519" target="_blank">Molvarec Attila (<span class="authorship-author-name">Molvarec Attila</span> <span class="authorAux-mtmt"> Szülészet-nőgyógyászat</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Klinikum">K</span>/Szülészeti és Nőgyógyászati Klinika</span> ;&nbsp;&nbsp;&nbsp; <span class="author-name" mtid="10023838"><a href="/gui2/?type=authors&mode=browse&sel=10023838" target="_blank">Czegle Ibolya ✉ (<span class="authorship-author-name">Czegle Ibolya</span> <span class="authorAux-mtmt"> Onkológia, belgyógyászat</span>) </a> </span> <span class="author-affil"><span title="Semmelweis Egyetem">SE</span>/<span title="Általános Orvostudományi Kar">AOK</span>/<span title="Klinikum">K</span>/Belgyógyászati és Hematológiai Klinika</span> </div> </div> <div class="title"><a href="/gui2/?mode=browse&params=publication;36833696" target="_blank">Subcellular Stress Markers in Epithelial Ovarian Cancer</a></div> <div> <span class="journal-title">INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES</span> <span class="journal-issn">(<a target="_blank" href="https://portal.issn.org/resource/ISSN/1661-6596">1661-6596</a> <a target="_blank" href="https://portal.issn.org/resource/ISSN/1422-0067">1422-0067</a>)</span>: <span class="journal-volume">27</span> <span class="journal-issue">1</span> <span class="page"> Paper 342. 45 p. </span> <span class="year">(2026)</span> </div> <div class="pub-footer"> <span class="language" xmlns="http://www.w3.org/1999/html">Nyelv: Angol | </span> <span class="identifiers"> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="10.3390/ijms27010342" target="_blank" href="https://doi.org/10.3390/ijms27010342"> DOI </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="001657437600001" target="_blank" href="https://www.webofscience.com/wos/woscc/full-record/001657437600001"> WoS </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="105026969813" target="_blank" href="http://www.scopus.com/record/display.url?origin=inward&eid=2-s2.0-105026969813"> Scopus </a> </span> <span class="id identifier oa_none" title="none"> <a style="color:blue" title="41516218" target="_blank" href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=41516218&dopt=Abstract"> PubMed </a> </span> <span class="id identifier oa_NONE" title=" Nincs "> <a style="color:blue" title="https://www.scopus.com/inward/record.uri?eid=2-s2.0-105026969813&doi=10.3390%2Fijms27010342&partnerID=40&md5=cd8be9409f0a2140c0b1cd2b2154408a" target="_blank" href="https://www.scopus.com/inward/record.uri?eid=2-s2.0-105026969813&doi=10.3390%2Fijms27010342&partnerID=40&md5=cd8be9409f0a2140c0b1cd2b2154408a"> Egyéb URL </a> </span> </span> <OnlyViewableByAuthor><div class="ratings"> <div class="journal-subject">Folyóirat szakterülete: Scopus - Inorganic Chemistry&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;D1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Organic Chemistry&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;D1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Spectroscopy&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;D1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Catalysis&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Computer Science Applications&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Medicine (miscellaneous)&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Physical and Theoretical Chemistry&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q1</div> <div class="journal-subject">Folyóirat szakterülete: Scopus - Molecular Biology&nbsp;&nbsp;&nbsp;SJR indikátor:&nbsp;Q2</div> <div class="journal-subject">Norvég listás folyóirat</div> </div></OnlyViewableByAuthor> <div class="publication-citation"> <a target="_blank" href="/api/publication?cond=citations.related;eq;36833696&sort=publishedYear,desc&sort=title"> Idézett közlemények száma: 5 </a> </div> <div class="mtid"><span class="long-pub-mtid">Közlemény: 36833696</span> | <span class="status-data status-VALIDATED"> Egyeztetett </span> Forrás Idéző | <span class="type-subtype">Folyóiratcikk ( Összefoglaló cikk ) </span> | <span class="pub-category">Tudományos</span> | <span class="publication-sourceOfData">DOI XML</span> </div> <div class="funder"> (The APC was funded by Semmelweis University) </div> <div class="lastModified">Utolsó módosítás: 2026.02.10. 11:06 Kajtár Virág Anna (SE_AOK_Biokemia_Admin5_KV, admin) </div> <pre class="comment" style="margin-top: 0; margin-bottom: 0;"><u>Megjegyzés</u>: Funding Agency and Grant Number: University of California; Semmelweis University Funding text: The APC was funded by Semmelweis University and University of California.</pre> </div></div>