{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/checksum.txt"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/combined_XA01653B1LPMa.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LPMa_C3_Slot1-24_1_3935.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LQ_EXP2_Slot1-12_1_8345.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LQ_C3_Slot1-16_1_8350.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/combined_XA01653B1LQ.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LQ_EXP1_Slot1-11_1_8344.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LPMa_C1_Slot1-22_1_3931.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LPMa_C2_Slot1-23_1_3933.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LQ_C1_Slot1-14_1_8348.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LQ_C2_Slot1-15_1_8349.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LPMa_EXP3_Slot1-21_1_3924.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LQ_EXP3_Slot1-13_1_8346.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LPMa_EXP2_Slot1-20_1_3922.d.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD075276/XA01653B1LPMa_EXP1_Slot1-19_1_3920.d.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["13600182648@163.com"],"submitter":["Yaling Feng"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Malonylation","Placenta","Preeclampsia"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075276"],"tissue":["Placenta"],"sample_protocol":["Protein Extraction Samples were taken out from -80 °C, and an appropriate amount of each sample was transferred into a liquid nitrogen-precooled mortar, followed by thorough grinding into powder with liquid nitrogen. A 4-fold volume of lysis buffer (1% Triton X-100, 1% protease inhibitor cocktail, 3 μM trichostatin A (TSA), 50 mM nicotinamide (NAM)) was added to the powdered sample of each group, and sonication was performed to achieve lysis. After centrifugation at 12,000×g for 10 min at 4 °C, the supernatant was transferred to a new centrifuge tube, and the protein concentration was determined using a BCA protein assay kit. Trypsin Digestion An equal amount of protein from each sample was collected for digestion, and the volume was adjusted to be consistent with lysis buffer. Trichloroacetic acid (TCA) was slowly added to a final concentration of 20%, followed by vortex mixing and incubation for 2 h at 4 °C for protein precipitation. After centrifugation at 4,500×g for 5 min, the supernatant was discarded, and the pellet was washed 2–3 times with precooled acetone. The pellet was air-dried, then triethylammonium bicarbonate (TEAB) was added to a final concentration of 200 mM, and the pellet was dispersed by sonication. Trypsin was added at a mass ratio of 1:50 (trypsin:protein) for overnight digestion. Dithiothreitol (DTT) was added to a final concentration of 5 mM, followed by reduction at 56 °C for 30 min. Subsequently, iodoacetamide (IAA) was added to a final concentration of 11 mM, and the mixture was incubated at room temperature in the dark for 15 min. Modification Enrichment Peptides were dissolved in IP buffer (100 mM NaCl, 1 mM ethylenediaminetetraacetic acid (EDTA), 50 mM Tris-HCl, 0.5% Nonidet P-40 (NP-40), pH 8.0), and the supernatant was transferred to pre-washed resin (antibody resin, Cat. No. PTM904, PTM Bio, Hangzhou Jingjie Biotechnology Co., Ltd.). The mixture was incubated on a rotary shaker with gentle shaking at 4 °C overnight. After incubation, the resin was washed 4 times with IP buffer and twice with deionized water successively. The peptides bound to the resin were eluted with 0.1% trifluoroacetic acid (TFA) eluent three times, and the eluates were collected and vacuum freeze-dried. The dried samples were desalted following the instructions of C18 ZipTips, then vacuum freeze-dried again for liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS) Analysis Peptides were dissolved in liquid chromatography mobile phase A and separated using a NanoElute ultra-high performance liquid chromatography (UHPLC) system. Mobile phase A was an aqueous solution containing 0.1% formic acid and 2% acetonitrile; mobile phase B was an acetonitrile-water solution containing 0.1% formic acid. The liquid chromatography gradient was set as: 0–42 min, 6%–22% B; 42–52 min, 22%–30% B; 52–56 min, 30%–80% B; 56–60 min, 80% B, with a constant flow rate of 450 nl/min. After UHPLC separation, peptides were ionized via a capillary ion source and analyzed using a timsTOF Pro 2 mass spectrometer. The ion source voltage was set to 1.50 kV, and both precursor ions and their fragment ions were detected and analyzed by high-resolution time-of-flight (TOF) mass spectrometry. The tandem mass spectrometry scan range was set to 100–1700 m/z. Data were acquired in parallel accumulation serial fragmentation (PASEF) mode. After one full-scan mass spectrum acquisition, 10 PASEF MS/MS scans were performed for precursor ions with charge numbers ranging from 0 to 5. The dynamic exclusion time for tandem mass spectrometry scanning was set to 24 s to avoid repeated scanning of precursor ions"],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The secondary mass spectrometry data in this study were searched using MaxQuant (v1.6.15.0).Search parameters were set as follows: The database employed was Homo_sapiens_9606_SP_20230103.fasta (containing 20,389 sequences). A decoy database was added to calculate the false discovery rate (FDR) derived from random matching, and a common contaminant database was incorporated to eliminate the interference of contaminant proteins in the identification results.Enzyme digestion was set to Trypsin/P; the number of missed cleavage sites was set to 4; the minimum peptide length was set to 7 amino acid residues; the maximum number of modifications per peptide was set to 5.The precursor ion mass tolerances for the first search and main search were set to 20 ppm and 20 ppm, respectively, and the mass tolerance for fragment ions was set to 20 ppm.Carbamidomethyl (C) on cysteine was set as a fixed modification. Variable modifications included oxidation of methionine, acetylation of the protein N‑terminus, and malonylation of lysine.The FDR thresholds for both protein identification and peptide spectrum match (PSM) identification were set to 1%."],"omics_type":["Proteomics"],"labhead":["Yaling Feng"],"instrument_platform":[""],"labhead_affiliation":["Department of Women Health Care, Wuxi School of Medicine, Wuxi Maternal and Child Health Hospital, Jiangnan University, Wuxi, 214002, Jiangsu Province, PR China."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["13600182648@163.com"],"publication":["Not available"],"submitter_affiliation":["Wuxi Maternal and Child Health Hospital"],"submitter_country":["China"],"additional_accession":[]},"is_claimable":false,"name":"Placental 4D Label-free quantitative proteome and malonylation quantitative modificomics analysis","description":"The diagnosis of PE is strictly followed by the guidelines issued by the American College of Obstetricians and Gynecologists. Placental tissue is collected from the placental villi (avoiding arteries and calcified areas) immediately after delivery and is repeatedly gently cleaned with phosphate buffers. Samples should be stored in 4% formaldehyde or immediately frozen at -80℃ for subsequent analysis. There are a total of 6 placental tissue samples, including 3 from the preeclampsia (PE) group and 3 from the healthy control 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