{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_20_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_2_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_3_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_10_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_1_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_11_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_13_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_4_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_5_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_19_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_12_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_9_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_7_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_14_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_18_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_17_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_6_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_16_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_15_B2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/20250303_RU_FF_8_B2.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/uniprotkb_Human_reviewed_2025_01_29.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/reportB2.parquet","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD063187/Lib_2MC_1VM_in_silico_2025.predicted.speclib"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["jeovanis.gil_valdes@med.lu.se"],"submitter":["Jeovanis Gil"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Fertility preservation","Atresia","Follicular fluid","Metabolism","Oocyte maturation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD063187"],"tissue":["Follicular Fluid"],"sample_protocol":["Sample Preparation and Protein Digestion Follicular fluid samples containing 50 µg of protein were adjusted to a final volume of 50 µL with a buffer consisting of 5% SDS, 50 mM TEAB, and 25 mM DTT. Samples were incubated at 95 °C for 5 min to achieve disulfide bridge reduction. Alkylation was then carried out by adding iodoacetamide (IAA) to a final concentration of 50 mM, followed by incubation in the dark for 20 min at room temperature. Proteins were subsequently digested using an S-Trap 96-well plate (PROTIFI, New York, USA) according to the manufacturer's instructions. Briefly, samples were acidified to a final concentration of 1.2% phosphoric acid, combined with binding buffer (90% methanol, 100 mM TEAB), loaded onto S-Trap columns, and washed four times with binding buffer. Digestion was performed overnight at 37 °C using trypsin at an enzyme-to-protein ratio of 1:40 in 50 mM TEAB. Peptides were eluted sequentially using 0.2% formic acid in water followed by 50% acetonitrile in water. Eluted peptides were dried and resuspended in loading buffer (0.1% TFA in 98:2 water:acetonitrile) prior to LC-MS/MS analysis. Liquid Chromatography-Mass Spectrometry (LC-MS/MS) LC-MS/MS analyses were performed on a Dionex Ultimate 3000 RSLCnano UPLC system coupled to a Q-Exactive HF-X mass spectrometer (Thermo Fisher Scientific, Waltham, MA, USA). For each run, 1 µg of peptides was injected and desalted on an Acclaim PepMap100 C18 trap column (3 µm, 100 Å, 75 µm × 2 cm, nanoViper) at 35 °C, then separated on an EASY-spray RSLC C18 analytical column (2 µm, 100 Å, 75 µm × 50 cm) maintained at 60 °C with a flow rate of 300 nL/min. A non-linear gradient was applied over 60 min: from 2% to 27% buffer B (80% acetonitrile, 0.1% formic acid) in 55 min, then ramped sequentially from 27% to 35% and 35% to 55% buffer B in 2 min each, followed by an increase to 90% buffer B over 1 min. The mass spectrometry method consisted of a full-cycle DIA (Data-Independent Acquisition) method comprising three MS1 scans and 54 variable-width MS2 scans over a mass range of 370–1460 m/z. MS2 window widths were determined empirically from prior DDA experiments, incorporating a 1 Da overlap. MS1 acquisition parameters included 120,000 resolution (@200 m/z), AGC target of 3×10^6, and a maximum injection time of 50 ms. MS2 scans were acquired at 30,000 resolution, AGC target of 1×10^6, automatic maximum injection time, and normalized collision energy (NCE) of 28."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Protein Identification and Quantification Raw mass spectrometry data were analyzed using DIA-NN 2.0 (Academia version) for protein identification and quantification. A predicted spectral library was generated with DIA-NN using a human proteome database (UniProt, accessed 2025-01-29). Library generation parameters allowed for two missed cleavages, fixed modification of carbamidomethylation on cysteine residues, and variable modifications including oxidation of methionine and protein N-terminal acetylation. Protein identifications were filtered to maintain a 1% false discovery rate (FDR), and Match Between Runs (MBR) was enabled. Cross-run global normalization was applied, and computation was optimized for speed and accuracy. Differentially abundant proteins between healthy and atretic follicular fluid were determined via paired t-tests, considering paired samples within each patient. Proteins were defined as significantly dysregulated at a p-value threshold of 0.05, with analyses conducted using GraphPad Prism v10.4.2. Gene Set Enrichment Analysis (GSEA) A pre-ranked protein list was generated from the paired t-test results. Proteins were ranked based on –log10 transformed p-values, with positive values for proteins enriched in atretic follicles and negative values for those enriched in healthy follicles. GSEA was performed using the Gene Ontology Biological Processes database (2024 release) and the GSEA software v4.3.2. Enrichment maps were visualized and finalized using Cytoscape v3.10.3."],"omics_type":["Proteomics"],"labhead":["Jeovanis Gil"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Translational Medicine, Lund University"],"species":["Homo Sapiens (human)"],"publication":["41720862 Kristensen SG, Subiran Adrados C, Elsner K, Cadenas J, Jensen LB, Tanvig MH, Greve VH, Colmorn LB, Marko-Varga G, Malm J, Gil J. Molecular signatures of oocyte viability identified by follicular fluid proteomics. Sci Rep. 2026 16(1):10010 10.1038/s41598-026-40907-7"],"submitter_mail":["jeovanis.gil_valdes@med.lu.se"],"submitter_affiliation":["Lund University"],"submitter_country":["Sweden"],"additional_accession":[]},"is_claimable":false,"name":"A Tale of Two Follicles: Proteomic Clues to Oocyte Success and Failure","description":"Women are born with thousands of follicles in their ovaries but less than 1% will produce a mature oocyte. What distinguishes the 99% of ovarian follicles destined for demise from the rare 1% that succeed? Here, we leveraged a unique clinical opportunity, paired follicular fluid samples from small antral follicles containing viable and atretic oocytes, to uncover the proteomic determinants governing  oocyte fate. Our analysis identified nearly 1,500 proteins, revealing that healthy follicular fluid is enriched with proteins crucial for energy metabolism, antioxidative defense, structural integrity, and robust signaling networks, supporting successful oocyte survival and maturation. In contrast, atretic follicles exhibited a distinct inflammatory signature characterized by acute-phase and immune activation proteins, indicative of active degeneration. These novel proteomic insights deepen our understanding of follicle biology and open new avenues for biomarker development, optimization of assisted reproductive technologies, and targeted therapeutic strategies to preserve and enhance female 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