{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/ID24223_Raw_file_experiment_list.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/20240918_E2_NEO5_Rozmaric_Ogrodnik_MPLGmbH_Academic_MPLID24223_C4_DONUT_p21_50p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/20240918_E2_NEO5_Rozmaric_Ogrodnik_MPLGmbH_Academic_MPLID24223_C6_MICRON_p21_50p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/20240918_E2_NEO5_Rozmaric_Ogrodnik_MPLGmbH_Academic_MPLID24223_C3_DONUT_LacZ_50p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/20240918_E2_NEO5_Rozmaric_Ogrodnik_MPLGmbH_Academic_MPLID24223_C5_MICRON_LacZ_50p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/20240918_E2_NEO5_Rozmaric_Ogrodnik_MPLGmbH_Academic_MPLID24223_C2_CTRL_p21_50p.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/20240918_E2_NEO5_Rozmaric_Ogrodnik_MPLGmbH_Academic_MPLID24223_C1_CTRL_LacZ_50p.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/2024_04_UP000008227_S_scrofa_Duroc_1ppg.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/contaminants_2023_03.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/MsReport_Result.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD075222/FragPipe_Result.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mikolaj.ogrodnik@lbg.ac.at"],"submitter":["Markus Hartl"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075222"],"tissue":["Skin"],"sample_protocol":["Three different types of pig skin samples were collected: control skin, biopsy punches from the proximity of excision wounds, and microneedled skin areas. For generation of wounded skin samples, pig skin undergone either excision injury with a 4 mm biopsy punch or microneedled 50 times at a depth of 3 mm using a DermaStamp. Excision wound samples were generated by collecting a 6 mm biopsy punch from around the excision wound, resulting in donut (ring)-shaped samples representing ~1 mm of tissue around the injury site. All wounded skin samples were collected 1.5 hours post-injury. Control and microneedled skin samples were collected using a 4 mm biopsy punch. All the biopsies were removed using tweezers and sharp scissors. The biopsy was washed in PBS, and the dermal layer was trimmed away as much as possible with a razor blade. Each biopsy punch was then immediately fixed in 4% formaldehyde for 6 hours. After the fixation, the samples were washed three times with 50 mL of chilled PBS.   Fifty biopsy samples per group were ground in liquid nitrogen with a mortar and pestle, then transferred to 50 mL Falcon tubes containing 10× volume lysis buffer (50 mM Tris-Cl pH 7.0, 10 mM EDTA, 1% SDS, PMSF, protease inhibitors, and Superase-In). Samples were kept on ice and homogenized (ULTRA TURRAX T25) six times for 1 min at maximum speed, followed by sonication (Bandelin Sonoplus mini20) 20× for 1 min at 40% energy with 1 min rest intervals. Homogenates were incubated on ice for 45 min, centrifuged (16,100 RCF, 10 min, 4°C), and supernatants collected. Each was pre-cleared with Dynabeads MyOne Streptavidin C1 (30 µL beads/mL), incubated at 37°C, and washed twice. Hybridization buffer (750 mM NaCl, 1% SDS, 50 mM Tris-Cl pH 7.0, 1 mM EDTA, inhibitors) and 260 pmol raPOOL probe were added per sample and incubated overnight at 37°C. Fresh C1 beads (100 µL per 100 pmol probe) were added for 30 min binding at 37°C, washed five times with preheated SSC/SDS buffer, and eluted in biotin/HEPES buffer. After 20 min shaking at room temperature and 10 min at 65°C, beads were removed, and eluates were de-crosslinked overnight at 65°C. The 400µL samples were reduced and alkylated by adding 10 µL of 5 mM TCEP and 9.6µL 12mM iodoacetamide and incubating for 20 min at 25 ˚C at 1200rpm shaking in the dark. Sera-MagSpeed Beads mix (GE Life Sciences, cat. nos. 45152105050350 and 65152105050350) was added to the sample at beads:protein ratio of 10:1 and mixed with ethanol to real 50% final ethanol concentration. The tubes were kept in a thermomixer for 10min at 1000rpm at 23˚C to let protein bind to the beads. Then the supernatant was removed using a magnetic rack and the beads were washed with 500µL 80% ethanol in water off the rack. And the wash procedure was repeated 3 more times. Afterwards, 20µL 50mM ammonium bicarbonate with 200ng trypsin (Trypsin Gold, Promega) and 50ng LysC (mass spectrometry grade, FUJIFILM Wako chemicals) was added to the beads and incubated at 37°C 1000rpm overnight. The beads were settled on a magnetic rack and the supernatant was transferred to a new tube. The beads were rinsed with 8.5 µL ammonium bicarbonate and sonicated for 30s and the supernatant was pooled to the supernatant from the previous step. Then the samples were centrifugated at 20000g for 2min and the supernatant was transferred to a new tube to remove any remaining beads. Trifluoroacetic acid was added to reach a final concentration of 0.5 %. Peptides were separated on a Vanquish Neo nano-flow chromatography system (Thermo-Fisher), using a trap-elute method for sample loading (Acclaim PepMap C18, 2 cm × 0.1 mm, 5 μm, Thermo-Fisher), and a C18 analytical column (Acclaim PepMap C18, 50 cm × 0.75 mm, 2 μm, Thermo-Fisher), applying a segmented linear gradient from 2% to 35% and finally 80% solvent B (80 % acetonitrile, 0.1 % formic acid; solvent A 0.1 % formic acid) at a flow rate of 230 nL/min over 120min. Eluting peptides were analyzed on an Exploris 480 Orbitrap mass spectrometer (Thermo-Fisher Scientific) coupled to the column with a FAIMS pro ion-source (Thermo-Fisher Scientific) using coated emitter tips (PepSep, MSWil) with the following settings: The mass spectrometer was operated in DDA mode with two FAIMS compensation voltages (CV) set to -45 or -60 and 1.5 s cycle time per CV. The survey scans were obtained in a mass range of 350-1500 m/z, at a resolution of 60k at 200 m/z, and a normalized AGC target at 100%. The most intense ions were selected with an isolation width of 1.4 m/z, fragmented in the HCD cell at 30% collision energy, and the spectra recorded for max. 100 ms at a normalized AGC target of 100% and a resolution of 15k. Peptides with a charge of +2 to +6 were included for fragmentation, the peptide match feature was set to preferred, the exclude isotope feature was enabled, and selected precursors were dynamically excluded from repeated sampling for 45 seconds."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["The RAW MS data were analyzed with FragPipe (22.0), using MSFragger (4.1), IonQuant (1.10.27, and Philosopher (5.0.0). The default FragPipe workflow for label free quantification (LFQ-MBR) was used, except “Normalize intensity across runs” was turned off. Cleavage specificity was set to Trypsin/P, with two missed cleavages allowed. The protein FDR was set to 1%. A mass of 57.02146 (carbamidomethyl) was used as fixed cysteine modification; methionine oxidation and protein N-terminal acetylation were specified as variable modifications. MS2 spectra were searched against the Sus scrofa 1 protein per gene reference proteome from Uniprot (Proteome ID: UP000008227, release 2024_04), concatenated with a database of 382 common laboratory contaminants (release 2023.03, https://github.com/maxperutzlabs-ms/perutz-ms-contaminants) and two additional protein sequences corresponding to the expressed transgenic constructs. Computational analysis was performed using Python and the in-house developed Python library MsReport (version 0.0.26). Only non-contaminant proteins identified with a minimum of two peptides and being quantified in at least one replicate of one experiment were considered for the analysis. LFQ protein intensities reported by FragPipe were log2-transformed and normalized across samples using the ModeNormalizer from MsReport. This method involves calculating log2 protein ratios for all pairs of samples and determining normalization factors based on the modes of all ratio distributions. Missing values were imputed with fixed values close to the detection limit. The in-house Python library XlsxReport (0.0.8) was used to create a formatted Excel file summarizing the results of protein quantification."],"omics_type":["Proteomics"],"labhead":["Mikolaj Ogrodnik"],"instrument_platform":[""],"labhead_affiliation":["Ludwig Boltzmann Institute for Traumatology, The Research Center in Cooperation with AUVA, Austrian Cluster for Tissue Regeneration, The laboratory for Tissue Damage Responses in Regeneration and Aging,Donaueschingenstrasse 13, A-1200 Vienna, Austria,"],"submission_type":["PARTIAL"],"species":["Sus Scrofa Domesticus (domestic Pig)"],"submitter_mail":["proteomics@maxperutzlabs.ac.at"],"publication":["Not available"],"submitter_affiliation":["Max Perutz Labs, Mass Spectrometry Facility, Vienna Biocenter Campus (VBC), Dr. Bohr-Gasse 9, Vienna, Austria"],"submitter_country":["Austria"],"additional_accession":[]},"is_claimable":false,"name":"Pull-down experiment of Cdkn1a mRNA and its protein binding partners in wounds and homeostatic skin of porcine skin","description":"To elucidate the mechanism responsible for the absence of p21 (protein) in homeostatic porcine skin and its rapid generation upon injury, we performed a pull-down experiment of Cdkn1a mRNA and its protein binding partners. For this, we utilized a variant of the comprehensive identification of RNA binding proteins by mass spectrometry (ChIRP-MS), which has been successfully used in human cells for large noncoding RNAs, but never before applied to tissues in vivo or to small targets such as Cdkn1a 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