{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/Raw_file_experiment_list.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_ctrl3_s3_1c53p_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_TaV3_s9_1c19p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_AmB2_s5_0c97p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_ctrl2_s2_1c31p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_TaV1_s7_1c06p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_AmB1_s4_1c19p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_TaV2_s8_1c23p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_AmB3_s6_0c75p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/20220722_E3_RSLC1_Mazumdar_Kuchler_MPL_MUW_ctrl1_s1_1c92p.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/Cassiopeia_result.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD057542/SpectroNaut_search_result.sne"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["rounik.mazumdar@meduniwien.ac.at"],"submitter":["Markus Hartl"],"technology_type":["Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Candida auris","Tavaborole","Amphotericin b","Drug screening"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057542"],"tissue":["Cell Culture"],"sample_protocol":["Sample preparation for mass spectrometry analysis Protein pellets were resuspended in 50µL 4%(w/v) SDS, 100mM Tris/HCl pH 8.5, 0.1M DTT, shaken at RT till fully resuspended and incubated at 95°C for 4 min. Lysates were clarified by centrifugation at 16000g for 10 min at 20°C. Supernatants were transferred to new tubes and protein concentration was measured using 600nm protein assay kit (Pierce) with SDS compatibility reagent. Solutions were diluted 1:10 with dH2O, transferred to FASP filters in two steps, and centrifuged for 20 min at 12000g each step. Filters were washed with 200µL 8M urea in 100mM Tris/HCl pH 8.5 for 20 min at 12000g. 100µL 50mM iodoacetamide in 100mM Tris/HCl pH 8.5 were added, shaken for 1 min and incubated 30 min in the dark at room temperature. Filters were centrifuged for 10 min at 12000g followed by washing three times with 200µL 8M urea in 100mM Tris/HCl pH 8.5 and three times with 100µL 100mM Tris/HCl pH 8.5. Filters were transferred to new collection tubes, 40µL 50mM ABC containing 1µg trypsin (Promega) were added and kept at 37°C overnight in a wet chamber to prevent evaporation. Digested peptides were collected by centrifuging for 20 min at 12000g. Filters were washed with 40µL 100mM Tris/HCl pH 8.5, centrifuged for 15 min at 12000g resulting in pooled eluates. Digested peptides were acidified with 10µL 10% TFA and the peptides were desalted using an MCX 96 well plate (Waters).  Liquid chromatography separation coupled to mass spectrometry Peptides were separated on an Ultimate 3000 RSLC nano-flow chromatography system (Thermo-Fisher), using a pre-column for sample loading (Acclaim PepMap C18, 2 cm × 0.1 mm, 5 μm, Thermo-Fisher), and a C18 analytical column (Acclaim PepMap C18, 50 cm × 0.75 mm, 2 μm, Thermo-Fisher), applying a segmented linear gradient from 2% to 35% and finally 80% solvent B (80 % acetonitrile, 0.1 % formic acid; solvent A 0.1 % formic acid) at a flow rate of 230 nL/min over 120 min. Eluting peptides were analyzed on an Exploris 480 Orbitrap mass spectrometer (Thermo Fisher), which was coupled to the column with a FAIMS pro ion-source (Thermo-Fisher) using coated emitter tips (PepSep, MSWil).  Mass spectrometry data acquisition in data-independent acquisition mode (DIA) and raw data analysis The mass spectrometer was operated in DIA mode with the FAIMS CV set to -45, the survey scans were obtained in a mass range of 350-1200 m/z, at a resolution of 30k at 200 m/z and a normalized AGC target at 300%. 31 MSMS spectra with variable isolation width between 14 and 27 m/z covering 399.5-899.5 m/z range including 1 m/z windows overlap, were acquired in the HCD cell at 30% collision energy at a normalized AGC target of 1000% and a resolution of 30k. The max. injection time was set to auto."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data were processed using Spectronaut software (version 16.1.220730.53000, https://biognosys.com/software/spectronaut/) with the DirectDIA workflow. The Uniprot Candida Auris reference proteome (version 2022_02, www.uniprot.org), as well as a database of most common contaminants were used. The searches were performed with full trypsin specificity and a maximum of 2 missed cleavages at a protein and peptide spectrum match false discovery rate of 1%. Carbamidomethylation of cysteine residues were set as fixed, oxidation of methionine and N-terminal acetylation as variable modifications. The global normalization and imputation were done in Spectronaut - all other parameters were left at default. Spectronaut output tables were further processed using Cassiopeia_LFQ 4.6.4 (https://github.com/maxperutzlabs-ms/Cassiopeia_LFQ). Contaminant proteins, protein groups identified only by one peptide and protein groups with less than two quantitative values in one experimental group, were removed for further analysis. Differences between groups were statistically evaluated using the LIMMA package at 5% FDR (Benjamini-Hochberg)."],"omics_type":["Proteomics"],"labhead":["Rounik Mazumdar"],"instrument_platform":[""],"labhead_affiliation":["Medical University of Vienna"],"submission_type":["PARTIAL"],"species":["[candida] Auris"],"publication":["10.3389/FMICB.2026.1830629"],"submitter_mail":["proteomics@maxperutzlabs.ac.at"],"submitter_affiliation":["Max Perutz Labs, Mass Spectrometry Facility, Vienna Biocenter Campus (VBC), Dr. Bohr-Gasse 9, Vienna, Austria"],"submitter_country":["Austria"],"additional_accession":[]},"is_claimable":false,"name":"CandidOmics FWF-P33425: Integrative omics study to probe Candida auris","description":"CandidOmics: Integrative omics study to probe Candida 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