{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074961/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074961/10290-1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074961/10290-5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074961/10290-6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074961/10290-4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074961/10290-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074961/10290-3.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD074961/proteomics_results.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["weiwei@nju.edu.cn"],"submitter":["lihao Ji"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["B16f10","Quantitative proteomics","Sm@cmc-kp101","Proteomics","Mouse melanoma","Lc-ms/ms","Smt","4d-dia"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074961"],"tissue":["Melanocyte","Cell Culture"],"sample_protocol":["B16F10 mouse melanoma cells were seeded onto six-well plates at 2.0 × 10^6 cells/well and cultured for 24 h. Cells were then treated with PBS (control group) or SM@CMC-KP101 (SMT treatment group) at a final concentration of 4.0 × 10^7 CFU/mL and incubated for 12 h at 37 °C. After incubation, cells were collected and immediately frozen at −80 °C until proteomic analysis.  Frozen cell pellets (approximately 100 mg) were quickly ground into a fine powder in liquid nitrogen and lysed in 300 µL lysis buffer supplemented with 1 mM PMSF. Samples were further lysed by sonication (1 s on/1 s off at 80 W for 2 min) on ice and centrifuged at 12,000 rpm for 10 min at 4 °C to remove insoluble material; a second centrifugation step was performed to further clarify the supernatant. Protein concentration was determined using a BCA assay, and protein aliquots were stored at −80 °C.  For SDS-PAGE quality control, 10 µg protein from each sample was separated on 12% SDS-PAGE gels, stained with Coomassie Brilliant Blue, washed for 15 min and scanned using an automatic digital gel image analysis system (Tanon 1600).  Based on the measured protein concentrations, 50 µg protein from each sample was adjusted to the same concentration. DTT was added to a final concentration of 5 mM and samples were incubated at 55 °C for 30–60 min, followed by cooling to room temperature. Iodoacetamide was then added to a final concentration of 10 mM and samples were incubated in the dark for 15–30 min. Proteins were precipitated with six volumes of pre-cooled acetone at −20 °C overnight and centrifuged at 8,000 × g for 10 min at 4 °C to collect the pellets. Pellets were resuspended in 100 µL of 50 mM NH4HCO3, and proteins were digested with trypsin at an enzyme-to-substrate ratio of 1:50 (w/w) at 37 °C for 12 h. Digestion was stopped by adjusting the pH to 3 with phosphoric acid, and peptides were desalted using SOLA™ SPE cartridges. After vacuum drying, peptides were resuspended in buffer containing iRT peptides (1:10) prior to LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Proteomic analyses were performed by Shanghai OE Biotech Co., Ltd. using a Q Exactive HF mass spectrometer (Thermo Fisher Scientific) equipped with a Nanospray Flex source. Peptides were separated on a C18 analytical column (25 cm × 75 µm) at a flow rate of 300 nL/min. The LC gradient was: 0–40 min, 5–28% solvent B; 40–60 min, 28–42% solvent B; 60–65 min, 42–90% solvent B; 65–75 min, 90% solvent B. The MS acquisition range was 350–1650 m/z, with a resolution of 70,000 for full MS scans and 35,000 for MS/MS scans. The ten most intense precursor ions were selected for higher-energy collisional dissociation (HCD) with a normalized collision energy of 30. A 4D-DIA data acquisition strategy was employed.  Raw MS data were processed and searched using MaxQuant (version X.X; please specify the exact version) with default parameters for DIA analysis. Spectra were searched against the UniProt Mus musculus reference proteome database (downloaded on [date]). Carbamidomethylation of cysteine was set as a fixed modification, and oxidation of methionine and N-terminal acetylation were set as variable modifications. Trypsin/P was specified as the digestion enzyme with up to two missed cleavages allowed. Peptide-spectrum matches and protein identifications were filtered at a false discovery rate (FDR) of 1% at both peptide and protein levels. Quantitative analysis was based on DIA signal intensities as implemented in MaxQuant, and downstream statistical analyses were performed using standard workflows."],"omics_type":["Proteomics"],"labhead":["Wei wei"],"instrument_platform":[""],"labhead_affiliation":["State Key Laboratory of Coordination Chemistry, Chemistry and Biomedicine Innovation Center (ChemBIC), School of Life Sciences, Nanjing University, Nanjing 210093, P. R. China."],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["10.1038/S41467-026-70949-4"],"submitter_mail":["lihaojji@163.com"],"submitter_affiliation":["nanjing university"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"4D-DIA proteomic analysis of SMT-induced cytotoxicity in B16F10 mouse melanoma cells","description":"This dataset contains a 4D-DIA proteomic analysis of B16F10 mouse melanoma cells treated with SMT (SM@CMC-KP101). B16F10 cells were divided into two groups: a PBS control group and an SMT treatment group. After drug exposure, cellular proteins were extracted, digested and analyzed by LC-MS/MS using a Q Exactive HF mass spectrometer. The aim of this study is to identify differentially expressed proteins and perturbed pathways associated with the cytotoxic and anti-tumor effects of SMT on melanoma cells, providing insights into its molecular mechanisms of tumor cell 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