{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/All_3_comparisons_re-PeptideList.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/checksum.txt"],"Mzml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/All_3_comparisons_re-1.mzML"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_EV2_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_EV3_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/DelCaj_EV3_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/DelCaj_EV3_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/DelCaj_EV2_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_TC3_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/DelCaj_EV1_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_TC1_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_TC2_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_EV2_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_EV1_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_EV3_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/DelCaj_EV2_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/DelCaj_EV1_01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_TC1_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_TC2_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_TC3_02.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD077377/W303WT_EV1_02.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["sahi@iiserb.ac.in"],"submitter":["Preeti Sagarika"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Molecular chaperones","Caj1"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077377"],"sample_protocol":["Cells were lysed in 8 M urea prepared in 50 mM ammonium bicarbonate (ABC) buffer (pH 8.0) by vortexing followed by sonication on ice (10 s on/10 s off cycles for 20 min). Urea was removed by stepwise dialysis against 50 mM ABC buffer containing decreasing concentrations of urea (6 M, 4 M, 2 M, and 0 M), with each step performed for 3 h at 4 °C. Protein concentration was determined using the Bradford assay, and 100 μg of total protein from each sample was used for downstream processing. Protein samples were subjected to enzymatic digestion and peptide purification prior to mass spectrometry analysis. Peptides were separated using an UltiMate 3000 RSLCnano UHPLC system (Thermo Scientific) on an EASY-Spray PepMap RSLC C18 column (75 μm × 50 cm, 2 μm particle size) with a 145 min nanoLC gradient."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Mass spectrometric analysis was performed on an Orbitrap Eclipse Fusion Tribrid mass spectrometer (Thermo Scientific) operated in data-dependent acquisition (DDA) mode.  Raw data files were processed using Proteome Discoverer (version 3.0.1.27). Spectra were searched against the Saccharomyces cerevisiae UniProt database (January 2025 release). Protein identification was filtered at a false discovery rate (FDR) of 1% at both peptide and protein levels.  Label-free quantification (LFQ) was used for relative protein quantification between WT + EV, TEF1-Caj1, delCaj1+EV samples."],"omics_type":["Proteomics"],"labhead":["Chandan Sahi"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Associate Professor Department of Biological Sciences Indian Institute of Science Education and Research-Bhopal MP, India"],"species":["Saccharomyces Cerevisiae (baker's Yeast)"],"publication":["10.1093/GENETICS/IYAG100"],"submitter_mail":["preetisagarika21@gmail.com"],"submitter_affiliation":["JNCASR"],"submitter_country":["India"],"additional_accession":[]},"is_claimable":false,"name":"Comparative proteomics analysis of wild-type vs Caj1 overexpressing cells","description":"This study presents a comparative label-free quantitative proteomic analysis of Saccharomyces cerevisiae wild-type cells carrying an empty vector (WT + EV), cells overexpressing Caj1 under the TEF1 promoter (TEF1-Caj1) and Caj1 deletion cells carrying an empty vector (del Caj1 + EV) . Caj1 is a cytosolic chaperone, and its overexpression is hypothesized to influence cellular protein homeostasis.  Whole-cell lysates were prepared from the indicated strains and subjected to LC–MS/MS analysis. The aim of this study is to identify differentially abundant proteins associated with Caj1 overexpression and to understand its impact on global proteome remodeling. The dataset provides insights into pathways potentially regulated by Caj1 and contributes to understanding chaperone-mediated proteostasis in 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