{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/PDB-2023-0169.final_protein.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160859_KF20230700272_Se_2_HFX2_150min_30cm_2ug_20230810_F1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160853_KF20230700272_HK2_2_HFX2_150min_30cm_2ug_20230809_F1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160852_KF20230700272_HK2_1_HFX2_150min_30cm_2ug_20230809_F1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160857_KF20230700272_NaOx_3_HFX2_150min_30cm_2ug_20230809_F1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160858_KF20230700272_Se_1_HFX2_150min_30cm_2ug_20230810_F1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160856_KF20230700272_NaOx_2_HFX2_150min_30cm_2ug_20230809_F1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160854_KF20230700272_HK2_3_HFX2_150min_30cm_2ug_20230809_F1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160855_KF20230700272_NaOx_1_HFX2_150min_30cm_2ug_20230809_F1_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067701/Exp160860_KF20230700272_Se_3_HFX2_150min_30cm_2ug_20230810_F1_R1.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["doc_yang1999@163.com"],"submitter":["Junyi Yang"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Nephrolithiasis"],"software":["Not available"],"submitter_keywords":["ferroptosis","Hk-2;ferroptosis;oxalate","Hk-2","oxalate"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067701"],"tissue":["Permanent Cell Line Cell","Cell Culture"],"sample_protocol":["Protein extraction : Collected samples were washed three times with phosphate buffer saline (PBS) buffer to remove blood and debris. Samples were minced and lysed in lysis buffer (8 M urea, 100 mM Tris hydrochloride, pH 8.0) containing protease and phosphatase inhibitors and then sonicated for 1 min (3 s on and 3 s off, amplitude 25%). The lysates were centrifuged at 14,000 × g for 10 min and supernatants were collected as whole-tissue extracts. Protein concentrations were determined by the Bradford protein assay.   SDS-PAGE :  20 µg protein for each sample were mixed with 2X loading buffer respectively and boiled for 5 min. The proteins were separated on SDS-PAGE gel (constant current 120 V, 60 min). Protein bands were visualized by Coomassie Blue R-250 staining.  Filter-aided sample preparation (FASP Digestion) procedure 200ug protein for each sample were reduced with 10 mM dithiothreitol at 56 °C for 30 min and alkylated with 10 mM iodoacetamide at room temperature in the dark for 30 min. 200μg sample lysis buffer with 200 μl 8M urea bicarbonate in the filter unit, vortex and spin at 14000 rcf for 20 minutes, The filters were washed with 200 μL UA buffer three times and then 200 μl 50mM NH4HCO3 buffer three times. Finally, the protein suspensions were digested with 4 μg trypsin (Promega) in 100 μl 50mM NH4HCO3 buffer overnight at 37 °C, and the resulting peptides were collected as a filtrate. The samples were digested with trypsin using a filter-aided sample preparation method. Tryptic peptides were vacuum-dried (Concentrator Plus, Eppendorf).   1.2 Nano-LC–MS/MS analysis For the proteome profiling samples, peptides were analyzed on a Q Exactive HF-X Hybrid Quadrupole-Orbitrap Mass Spectrometer (Thermo Fisher Scientific) coupled with a high-performance liquid chromatography system (EASY nLC 1200, Thermo Fisher Scientific). Dried peptide samples re-dissolved in Solvent A (0.1% formic acid in water) were loaded onto a 2-cm self-packed trap column (100 μm inner diameter, 3 μm ReproSil-Pur C18-AQ beads, Dr. Maisch GmbH) using Solvent A and separated on a 150-μm-inner-diameter column with a length of 30 cm (1.9 μm ReproSil-Pur C18-AQ beads, Dr. Maisch GmbH) over a 150-min gradient (Solvent A: 0.1% formic acid in water; Solvent B: 0.1% formic acid in 80% ACN) at a constant flow rate of 600 nL/min (0–150 min, 0 min, 4% B; 0–10 min, 4–15% B; 10–125 min, 15–30% B; 125–140 min, 30–50% B; 140–141 min, 50–100% B; 141–150 min, 100% B). Eluted peptides were ionized at 2 kV and introduced into the mass spectrometer. Mass spectrometry was performed in data-dependent acquisition mode. For the MS1 Spectra full scan, ions with m/z ranging from 300 to 1400 were acquired by an Orbitrap mass analyzer at a high resolution of 120,000. The automatic gain control (AGC) target value was set to 3E+06. The maximal ion injection time was 80 ms. The top 60 precursor ions were selected for fragmentation in an HCD cell with a normalized collision energy of 27%. The resulting fragment ions were transferred to the Orbitrap analyzer, which operated at a resolution of 7500. The automatic gain control (AGC) was set to 5e4 for MS/MS. The maximum ion injection times were set to 20 ms. Dynamic exclusion of previously acquired precursor ions was enabled for 25 seconds."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Pheatmap R were used to performing hierarchical clustering analysis. Euclidean distance algorithm for similarity measure and average linkage clustering algorithm (clustering uses the centroids of the observations) for clustering were selected when performing hierarchical clustering. A heat map was often presented as a visual aid in addition to the dendrogram. Protein sequences are searched using the InterProScan software to identify protein domain signatures from the InterPro member database Pfam. The protein sequences of the selected differentially expressed proteins were locally searched using the NCBI BLAST+ client software (ncbi-blast-2.2.28+-win32.exe) and InterProScan to find homologue sequences, then gene ontology (GO) terms were mapped and sequences were annotated using the software program Blast2GO. The GO annotation results were plotted by R scripts.Following annotation steps, the studied proteins were blasted against the online Kyoto Encyclopedia of Genes and Genomes (KEGG) database (http://geneontology.org/) to retrieve their KEGG orthology identifications and were subsequently mapped to pathways in KEGG.Enrichment analysis were applied based on the Fisher’ exact test, considering the whole quantified proteins as background dataset. Benjamini- Hochberg correction for multiple testing was further applied to adjust derived p-values. And only functional categories and pathways with p-values under a threshold of 0.05 were considered as significant.The protein–protein interaction (PPI) information of the studied proteins was retrieved from IntAct molecular interaction database(http://www.ebi.ac.uk/intact/) by their gene symbols or STRING software (http://string-db.org/)."],"omics_type":["Proteomics"],"labhead":["Junyi Yang"],"instrument_platform":[""],"labhead_affiliation":["Tongji Hospital"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["doc_yang1999@163.com"],"publication":["41833934 Yang J, Ma Z, Wan W, Yuan D, Li J, Wang Y, Wang B, Lyu G, Xun Y, Yu X. The hippo-YAP1/TEAD1-SLC7A5 axis: uncovering a novel therapeutic target for oxalate-induced renal tubular ferroptosis. Redox Rep. 2026 31(1):2643967 10.1080/13510002.2026.2643967"],"submitter_affiliation":["Tongji Hospital"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Differential Protein Expression in HK-2 Cells under Sodium Oxalate and Sodium Selenite Treatments (4D Label Free Proteomics)","description":"This study aims to elucidate differential protein expression in HK-2 cells exposed to sodium oxalate and sodium selenite using 4D label free 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