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Specific dental tissues were isolated using a diamond wire based on images taken. Hard tissues were crushed into a fine powder using a Mikro-Dismembrator. The powder was decalcified with EDTA, excluding pulp samples. Proteins were extracted using Guanidine Hydrochloride (GnHCl) for all samples, and the resulting extracts were dialyzed, quantified, and digested. For proteomic analysis, samples were desalted using C18 ZipTips, then centrifuged and transferred to total recovery vials for high-resolution liquid chromatography-tandem mass spectrometry (LC–MS/MS) analysis. Approximately 300 ng of each sample was loaded onto a trapping column (PepMap100, C18, 300 µm × 3.5 mm, ThermoFisher) using partial loop injection, followed by a 7-minute run at a flow rate of 12 μL/min with 0.1% formic acid. Peptides were separated on an analytical column (Easy-Spray C18 75 µm × 500 mm, Fisher Scientific) using a 96.2% A (0.1% formic acid) / 3.8% B (79.95% acetonitrile, 19.95% water, 0.1% formic acid) gradient, progressing to 50% A/50% B over 90 minutes at a flow rate of 0.3 nL/min, with a 30-minute blank between samples. Data acquisition was performed on an Orbitrap with a 60,000-resolution full-scan MS (AGC set to 3e6 ions, max fill time of 100 ms). The 16 most abundant peaks per scan were selected for HCD MS/MS (30,000 resolution, AGC set to 1e5 ions, max fill time of 45 ms), with a 2 m/z ion selection window and normalized collision energy of 30%. Ion selection excluded singly charged ions and those with a charge state ≥ +6. A 60-second dynamic exclusion window was used to avoid repeated selection of peptides. All samples were analyzed in random order."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptide and protein identification was performed using an in-house Mascot server with the Unihorse database. Search parameters included peptide mass tolerance of 10.0 ppm, fragment mass tolerance of 0.01 Da, trypsin digestion with one missed cleavage, and modifications for carbamidomethylation (cysteine) and oxidation (methionine). Protein quantification was carried out using Progenesis QI software V4, considering only unique peptides. For data analysis, all processing was done in R version 4.2.2. Normalization was performed using NormalyzerDE, with various methods compared based on evaluation metrics such as density plots, Q–Q plots, and RLE plots. The data was normalized by median, then log2-transformed. Principal Component Analysis (PCA) was used to explore the relationships between biological replicates, and the effect of each protein on the components was assessed. Differentially abundant proteins were identified using NormalyzerDE with a limma-based approach, applying Benjamini-Hochberg correction for statistical significance (p ≤ 0.05, fold change 0.5 ≤ FC ≤ 2)."],"omics_type":["Proteomics"],"labhead":["Mandy Peffers"],"instrument_platform":[""],"labhead_affiliation":["University of Liverpool"],"submission_type":["COMPLETE"],"species":["Equus Caballus (horse)"],"publication":["Not available"],"submitter_mail":["a.chabronova@liverpool.ac.uk"],"submitter_affiliation":["University of Liverpool"],"submitter_country":["United Kingdom"],"doi":["10.6019/PXD065888"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic analyse of equine tooth (enamel) ageing","description":"This study investigates the proteomic profiles of horse tooth tissues, including pulp, dentin, cementum, and enamel, with a focus on the effects of age and disease. We analyzed tissue samples from young, old, and diseased teeth to explore how aging and disease influence protein expression across these dental tissues. The goal was to identify tissue-specific proteomic signatures and potential biomarkers associated with age-related changes and dental diseases. The findings offer insights into the molecular mechanisms underlying tooth aging and disease, providing a foundation for future studies on equine dental health and potential therapeutic 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