<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Scholtes GK</submitter><funding>NCI</funding><funding>NIAID NIH HHS</funding><funding>NCI NIH HHS</funding><funding>NIAID</funding><funding>NIGMS NIH HHS</funding><pagination>1-15</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8440357</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>237</volume><pubmed_abstract>The 7 members of the A3 family of cytidine deaminases (A3A to A3H) share a conserved catalytic activity that converts cytidines in single-stranded (ss) DNA into uridines, thereby inducing mutations. After their initial identification as cell-intrinsic defenses against HIV and other retroviruses, A3s were also found to impair many additional viruses. Moreover, some of the A3 proteins (A3A, A3B, and A3H haplotype I) are dysregulated in cancer cells, thereby causing chromosomal mutations that can be selected to fuel progression of malignancy. Viral mechanisms that increase transcription of A3 genes or induce proteasomal degradation of A3 proteins have been characterized. However, only a few underlying biological mechanisms regulating levels of A3s in uninfected cells have been described. Here</pubmed_abstract><journal>Translational research : the journal of laboratory and clinical medicine</journal><pubmed_title>The von Hippel-Lindau Cullin-RING E3 ubiquitin ligase regulates APOBEC3 cytidine deaminases.</pubmed_title><pmcid>PMC8440357</pmcid><funding_grant_id>P01 AI131346</funding_grant_id><funding_grant_id>P30 CA060553</funding_grant_id><funding_grant_id>T32 GM008061</funding_grant_id><funding_grant_id>P30 AI117943</funding_grant_id><pubmed_authors>Scholtes GK</pubmed_authors><pubmed_authors>Clerc I</pubmed_authors><pubmed_authors>Song C</pubmed_authors><pubmed_authors>Sawyer AM</pubmed_authors><pubmed_authors>Vaca CC</pubmed_authors><pubmed_authors>Roh M</pubmed_authors><pubmed_authors>D'Aquila RT</pubmed_authors></additional><is_claimable>false</is_claimable><name>The von Hippel-Lindau Cullin-RING E3 ubiquitin ligase regulates APOBEC3 cytidine deaminases.</name><description>The 7 members of the A3 family of cytidine deaminases (A3A to A3H) share a conserved catalytic activity that converts cytidines in single-stranded (ss) DNA into uridines, thereby inducing mutations. After their initial identification as cell-intrinsic defenses against HIV and other retroviruses, A3s were also found to impair many additional viruses. Moreover, some of the A3 proteins (A3A, A3B, and A3H haplotype I) are dysregulated in cancer cells, thereby causing chromosomal mutations that can be selected to fuel progression of malignancy. Viral mechanisms that increase transcription of A3 genes or induce proteasomal degradation of A3 proteins have been characterized. However, only a few underlying biological mechanisms regulating levels of A3s in uninfected cells have been described. Here</description><dates><release>2021-01-01T00:00:00Z</release><publication>2021 Nov</publication><modification>2026-06-04T03:01:16.326Z</modification><creation>2025-06-01T00:32:31.502Z</creation></dates><accession>S-EPMC8440357</accession><cross_references><pubmed>34004371</pubmed><doi>10.1016/j.trsl.2021.05.002</doi></cross_references></HashMap>