<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zhang S</submitter><funding>Scientific and Technological Innovation Fund of Longhua Shenzhen</funding><pagination>e0338641</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC12851463</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>21(1)</volume><pubmed_abstract>In this study, we systematically integrated proteome and acetyl proteome (acetylome) approaches to investigate the characteristics of renal proteins in a CaOx crystal rat model. We aimed to understand the pathogenesis of kidney calculi and delineate the landscape of acetylation within kidney calculi, potentially leading to the identification of valuable and novel biomarkers. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS), we analyzed the protein expression profiles and lysine acetylation (Kac) features in kidney tissues obtained from rats with kidney calculi and those without (normal controls). Our results revealed 118 downregulated and 129 upregulated proteins. Furthermore, we identified 538 upregulated Kac sites in 258 proteins and 133 downregulated Kac sites in 118 prot</pubmed_abstract><journal>PloS one</journal><pubmed_title>Systematic proteomics analysis of lysine acetylation reveals critical features of renal proteins in kidney calculi formation.</pubmed_title><pmcid>PMC12851463</pmcid><funding_grant_id>11501A20240704F5EB6FF</funding_grant_id><pubmed_authors>Liang H</pubmed_authors><pubmed_authors>Jiang H</pubmed_authors><pubmed_authors>Deng Q</pubmed_authors><pubmed_authors>Jin M</pubmed_authors><pubmed_authors>Zhang S</pubmed_authors><pubmed_authors>Wang Z</pubmed_authors><pubmed_authors>Wang J</pubmed_authors></additional><is_claimable>false</is_claimable><name>Systematic proteomics analysis of lysine acetylation reveals critical features of renal proteins in kidney calculi formation.</name><description>In this study, we systematically integrated proteome and acetyl proteome (acetylome) approaches to investigate the characteristics of renal proteins in a CaOx crystal rat model. We aimed to understand the pathogenesis of kidney calculi and delineate the landscape of acetylation within kidney calculi, potentially leading to the identification of valuable and novel biomarkers. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS), we analyzed the protein expression profiles and lysine acetylation (Kac) features in kidney tissues obtained from rats with kidney calculi and those without (normal controls). Our results revealed 118 downregulated and 129 upregulated proteins. Furthermore, we identified 538 upregulated Kac sites in 258 proteins and 133 downregulated Kac sites in 118 prot</description><dates><release>2026-01-01T00:00:00Z</release><publication>2026</publication><modification>2026-06-12T10:21:28.025Z</modification><creation>2026-06-12T03:12:22.839Z</creation></dates><accession>S-EPMC12851463</accession><cross_references><pubmed>41604379</pubmed><doi>10.1371/journal.pone.0338641</doi></cross_references></HashMap>