{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065567/checksum.txt"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065567/iq_PG_quantification.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065567/report.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065567/QExactiveHF02_12993_NME-GPS_idiopathic_III_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065567/QexHF03_003453_NME-GPS_idiopathic_II_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065567/QExactiveHF02_12841_NME-GPS_idiopathic_3.raw"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065567/UP000005640_9606_additional.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD065567/UP000005640_9606.fasta"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["Andreas.Roos@uk-essen.de"],"submitter":["Marc Pauper"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Congenital Myopathy"],"software":[""],"submitter_keywords":["Human","Lc-msms","Muscle","Dia","Nmd-gps"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065567"],"tissue":["Quadriceps"],"sample_protocol":["- Snap-frozen quadriceps muscle sample was subjected to lysis by the addition of 200 µL of 50 mM triethylammonium bicarbonate (TEAB) buffer (pH 8.5), containing 5% sodium dodecyl sulfate (SDS) and a protease inhibitor cocktail (cOmplete ULTRA, Roche). The lysed sample was then processed using the Bioruptor® sonication system (Diagenode) under the following conditions: 10 minutes of treatment at 4°C with alternating 30-second cycles of sonication (on and off), for a total of 10 cycles. To ensure complete lysis, an additional sonication step was performed using an ultra-sonic probe (30s, 1s/1s, amplitude 40%) followed by centrifugation at 4 °C and 20,000 g for 15 min. to remove debris. Protein concentration in the supernatant was quantified using a bicinchoninic acid (BCA) assay, following the manufacturer’s instructions.   To reduce disulfide bonds, tris(2-carboxyethyl)phosphine (TCEP) was added to a final concentration of 10 mM, and the reaction was incubated at 37°C for 30 minutes. Subsequently, free sulfhydryl groups were alkylated by the addition of 15 mM iodoacetamide (IAA) and incubated at room temperature in the dark for 30 minutes.     For proteolytic digestion, 100 µg of protein from the sample was processed according to the S-Trap protocol (Protifi), with a protein-to-trypsin ratio of 20:1. The samples were incubated for proteolysis at 47°C for 2 hours.     Following digestion, the resulting peptide mixture was desalted according to manufacture instructions (Protifi), and digestion completeness was verified by monolithic column separation using a PepSwift PS-DVB (PL-CAP200-PM, Dionex) column on an Ultimate 3000 HPLC system (Dionex, Germering, Germany). A 0.5 µg aliquot was directly injected into the column. A binary gradient was employed for separation, with solvent A consisting of 0.1% trifluoroacetic acid (TFA) in water, and solvent B composed of 0.08% TFA in 84% acetonitrile (ACN). The gradient progressed from 5% to 12% solvent B over 5 minutes, followed by an increase to 50% solvent B over 15 minutes, at a flow rate of 2.2 µL/min and a temperature of 60°C. UV absorbance was monitored at 214 nm to confirm peptide separation   - The sample was analyzed in triplicates using an UltiMate 3000 RSLC nano UHPLC system coupled with a QExactive HF mass spectrometer. For each analysis, a total of 1 µg of peptides was injected. Initially, the peptide mixtures were loaded onto a pre-column (75 µm × 2 cm, 100 Å, C18) at a flow rate of 10 µL/min for 20 minutes. The peptides were then separated on the analytical column (75 µm × 50 cm, 100 Å, C18) with a flow rate of 250 nL/min. The separation was performed using a linear gradient, where mobile phase A consisted of 99.9% water and 0.1% formic acid, and mobile phase B consisted of 84% acetonitrile, 15.9% water, and 0.1% formic acid. The gradient spanned 120 minutes, progressing from 3% to 35% of solution B. Specifically, the gradient steps were as follows: 3% B for the first 20 minutes, followed by an increase from 3% to 35% B over 120 minutes. After the gradient, three wash steps were conducted, each bringing the concentration of buffer B to 95% for 3 minutes. Finally, the system was allowed to equilibrate for 20 minutes before the next sample was introduced.   Mass spectrometry data were acquired using data-independent acquisition (DIA) mode, supported by an in-house generated spectral library. Each sample was spiked with an appropriate amount of iRT (indexed retention time) standard (Biognosys) to ensure accurate retention time alignment. Full MS scans were conducted within the mass-to-charge (m/z) range of 300–1100, using the Orbitrap mass analyzer at a resolution of 60,000. The polysiloxane ion at 445.12002 m/z served as the lock mass for internal calibration. The automatic gain control (AGC) was set to a target value of 3 × 106, with a maximum injection time of 20 milliseconds. Following each full MS scan, 23 DIA windows were acquired, each spanning 28 m/z with a 1 m/z overlap, starting at 400 m/z. These DIA scans were collected with a resolution of 30,000 on the Orbitrap, using an AGC target of 3 × 106 and a normalized collision energy (nCE) of 27 for fragmentation via collision-induced dissociation (CID)."],"repository":["pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["The raw MS files were converted to mzML format using the ThermoRawFileParser (version 1.4.2). Peptide identification and quantification was done with DIA-NN (version 1.8.1) using library-free search and match-between-runs enabled. For the first step of the library-free search, in silico prediction of the spectral library was done from the full human proteome reference and additional sequences obtained from UniProt (UniProtKB ID: UP000005640_9606). False discovery rate threshold was set to 1% for peptide and protein identification. The R package iq (version 1.9.12) was used for protein quantification, which implements the MaxLFQ algorithm for DIA-based data. Finally, protein intensity values were log2-transformed."],"omics_type":["Proteomics"],"labhead":["Andreas Roos"],"instrument_platform":[""],"labhead_affiliation":["Department of Pediatric Neurology, Centre for Neuromuscular Disorders, University Duisburg-Essen, 45147 Essen, Germany"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41776713 Pauper M, Kölbel H, Karakesisoglou I, Schänzer A, Böhm J, Thompson R, Kohlschmidt N, Ringel B, Bonne G, Neuhoff K, Gangfuß A, Kilicarslan OA, Agullo SB, Hentschel A, Schara-Schmidt U, Lochmüller H, Polavarapu K, Roos A. A muscular dystrophy associated with bi-allelic LEMD2 variants: Expanding the genotype of nuclear envelopathies. Brain Pathol. 2026 36(4):e70082 10.1111/bpa.70082"],"submitter_mail":["marc.pauper@cnag.eu"],"submitter_affiliation":["Centro Nacional de Análisis Genómico"],"submitter_country":["Spain"],"additional_accession":[]},"is_claimable":false,"name":"NMD-GPS_NME-058_Quadriceps_triplicate_DIA","description":"Untargeted LC-MSMS proteomics from muscle biopsy of index patient NME-058 of the NMD-GPS 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