{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077386/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077386/DEV_Nor.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077386/DEV_GEN.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077386/DEV_IGNITE.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077386/DEV_IGNITE.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077386/DEV_GEN.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077386/DEV_Nor.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["iamxgding@njupt.edu.cn"],"submitter":["Zhiwang Li"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":[""],"submitter_keywords":["Antigen presentation","Dendritic cells","Extracellular vesicles","Tumor immunotherapy"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077386"],"tissue":["Dendritic Cell"],"sample_protocol":["Gel pieces containing the target protein at the expected molecular mass were excised and destained using 50% acetonitrile in 50 mM ammonium bicarbonate (NH4HCO3). Destained gel pieces were dehydrated with 100% acetonitrile for 5 min, then reduced with 10 mM Tris(2-carboxyethyl)phosphine (TCEP) at 37 °C for 30 min. Subsequently, gel pieces were dehydrated again with 100% acetonitrile and alkylated with 25 mM iodoacetamide in the dark at room temperature for 30 min. Gel pieces were then washed with 50 mM NH4HCO3, dehydrated with 100% acetonitrile, and rehydrated in 50 mM NH4HCO3 containing 2 μg trypsin. In-gel digestion was performed overnight at 37 °C.Following digestion, peptides were extracted from gel pieces using 50% acetonitrile/0.1% formic acid. Extracts were dried in a SpeedVac concentrator and resuspended in 0.1% formic acid prior to LC-MS/MS analysis.Peptide samples were loaded onto an EASY nLC-1200 system (Thermo Scientific) with mobile phase A (0.1% formic acid). Peptide separation was performed at a constant flow rate of 400 nl/min using a gradient as follows: 2–7% mobile phase B (0.1% formic acid in 80% acetonitrile) for 1 min, 7–35% B for 35 min, 35–55% B for 9 min, 55–100% B for 7 min, and 100% B for 8 min.Eluted peptides were analyzed using a Q Exactive HF-X mass spectrometer (Thermo Scientific) equipped with a Nano electrospray source. The electrospray voltage was set to 2.0 kV. Full MS spectra were acquired in the Orbitrap at a resolution of 60,000. Data-dependent acquisition (DDA) was performed with the top 20 most abundant precursor ions selected for fragmentation (MS/MS) using a normalized collision energy (NCE) of 27. MS/MS spectra were recorded in the Orbitrap at a resolution of 15,000. A dynamic exclusion time of 20 s was applied to avoid repeated sequencing of the same precursor ion."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Mass spectra were processed and searched using Proteome Discoverer (version 2.4, Thermo Scientific) against the human Swissprot protein database (release 2023_09). Trypsin/P (or other enzymes if any) was specified as cleavage enzyme allowing up to 2 missing cleavages. The mass tolerance allowed for the precursor ions is 10 ppm, while the mass tolerance of fragment ions is set to 0.01 Da. Carbamidomethyl on Cysteine were specified as fixed modification ,while oxidation on Methionine and acetyl on protein N-terminal were specified as variable modification. Peptide confidence was set at high."],"omics_type":["Proteomics"],"labhead":["Jingjing Zhang"],"instrument_platform":[""],"labhead_affiliation":["State Key Laboratory of Organic Electronics and Information Displays Jiangsu Key Laboratory of Smart Biomaterials and Theranostic Technology, Nanjing University of Posts and Telecommunications, Nanjing 210023, China;"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["10.1038/S41565-026-02204-2"],"submitter_mail":["lizhiwang@cwmda.com"],"submitter_affiliation":["Cosmos Wisdom Institute of Excellence and Innovation"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Amplifying Tumor Antigen Presentations from Intratumorally Entrapped Dendritic Cells.","description":"This study aims to characterize the proteomic changes of extracellular vesicles (DEVs) released by ginseng vesicles (GEN) or IGNITE-treated mouse bone marrow-derived dendritic cells (BMDCs) using proteomics technology. DEVs were secreted by primary BMDCs . After 24-hour treatment of mouse bone marrow-derived dendritic cells (BMDCs) with either untreated material or ginseng vesicles (GEN) or IGNITE, the released extracellular vesicles (DEVs) under different treatments were collected. Proteins were extracted and subjected to enzymatic digestion, labeled with TMTpro/TMT 16-linked/TMT 10-linked reagents (select according to the actual kit), and analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS).The resulting datasets enable the identification and semi-quantitative analysis of differentially expressed proteins and related 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