<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Xu Y</submitter><funding>Health Scientific Research Innovation Ability Improvement Plan in Shaanxi Province of China</funding><funding>Natural Science Basic Research Plan in Shaanxi Province of China</funding><funding>Key R&amp;D plan of Shaanxi Province</funding><funding>Key R&amp;amp;D plan of Shaanxi Province</funding><funding>The National Natural Science Foundation of China</funding><funding>The National Natural Science Foundation of China (NSFC)</funding><pagination>1232-1245</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11263418</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>29(7-8)</volume><pubmed_abstract>MARCH5 is a ring-finger E3 ubiquitin ligase located in the outer membrane of mitochondria. A previous study has reported that MARCH5 was up-regulated and contributed to the migration and invasion of OC cells by serving as a competing endogenous RNA. However, as a mitochondrial localized E3 ubiquitin ligase, the function of MARCH5 in mitochondrial-associated metabolism reprogramming in human cancers remains largely unexplored, including OC. We first assessed the glycolysis effect of MARCH5 in OC both in vitro and in vivo. Then we analyzed the effect of MARCH5 knockdown or overexpression on respiratory activity by evaluating oxygen consumption rate, activities of OXPHOS complexes and production of ATP in OC cells with MARCH5. Co-immunoprecipitation, western-blot, and in vitro and vivo experi</pubmed_abstract><journal>Apoptosis : an international journal on programmed cell death</journal><pubmed_title>MARCH5 promotes aerobic glycolysis to facilitate ovarian cancer progression via ubiquitinating MPC1.</pubmed_title><pmcid>PMC11263418</pmcid><funding_grant_id>2022JQ-977</funding_grant_id><funding_grant_id>2023PT-07</funding_grant_id><funding_grant_id>S2023-YF-YBSF-0816</funding_grant_id><funding_grant_id>NO.82172993</funding_grant_id><funding_grant_id>2024JC-YBMS-703</funding_grant_id><pubmed_authors>Yang H</pubmed_authors><pubmed_authors>Li Y</pubmed_authors><pubmed_authors>Li J</pubmed_authors><pubmed_authors>Zhao S</pubmed_authors><pubmed_authors>Chen Z</pubmed_authors><pubmed_authors>Guo F</pubmed_authors><pubmed_authors>Shen Y</pubmed_authors><pubmed_authors>Dang Y</pubmed_authors><pubmed_authors>Xu Y</pubmed_authors></additional><is_claimable>false</is_claimable><name>MARCH5 promotes aerobic glycolysis to facilitate ovarian cancer progression via ubiquitinating MPC1.</name><description>MARCH5 is a ring-finger E3 ubiquitin ligase located in the outer membrane of mitochondria. A previous study has reported that MARCH5 was up-regulated and contributed to the migration and invasion of OC cells by serving as a competing endogenous RNA. However, as a mitochondrial localized E3 ubiquitin ligase, the function of MARCH5 in mitochondrial-associated metabolism reprogramming in human cancers remains largely unexplored, including OC. We first assessed the glycolysis effect of MARCH5 in OC both in vitro and in vivo. Then we analyzed the effect of MARCH5 knockdown or overexpression on respiratory activity by evaluating oxygen consumption rate, activities of OXPHOS complexes and production of ATP in OC cells with MARCH5. Co-immunoprecipitation, western-blot, and in vitro and vivo experi</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Aug</publication><modification>2025-06-01T01:15:39.98Z</modification><creation>2025-06-01T01:15:39.98Z</creation></dates><accession>S-EPMC11263418</accession><cross_references><pubmed>38615083</pubmed><doi>10.1007/s10495-024-01962-5</doi></cross_references></HashMap>