{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074000/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074000/SB_4_59_YG_SS_27_R7.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074000/SB_4_59_YG_SS_27_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074000/SB_4_59_YG_SS_27_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074000/SB_4_59_YG_SS_27_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074000/SB_4_59_YG_SS_27_R6.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074000/SB_4_59_YG_SS_27_R5.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD074000/SB_4_64_S_M_SS27_DirectDIA_Analysis.sne"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["Dominic.Winter@uk-essen.de"],"submitter":["Sara Bonini"],"technology_type":["Mass Spectrometry","Data-independent acquisition","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074000"],"tissue":["Myoblast","Cell Culture"],"sample_protocol":["Samples were dissolved in 2% SDS lysis buffer (2%SDS in 50mM HEPES pH 7.5), incubated at 95°C for 5 min and further lysed in the Biorupture (3 cycle 30 sec on and 30 sec off). After the pellet was dissolved, the samples were centrifuged at 20,000 x g at room temperature for 20 min. The supernatant was transferred into a fresh 1.5 mL tube and further diluted (1:40) to estimate the protein concentration via manufacture’s instruction (Bio Rad DC protein assay). 1 mg of protein lysate was further transferred into a fresh tube and the sample was diluted with the required amount to obtain a final SDS concentration of 0.5% with 50 mM HEPES buffer.  Next the sample was used to perform the immunoprecipitation of biotinylated protein via streptavidin coupled Sepharose beads. For 1 mg of protein 75 µL of slurry were used and previously washed three times form the storage solution with 500 µL of 0.5% SDS in 50 mM HEPES buffer, incubated onto a tumbling tube rotator for 2 min at room temperature and finally centrifuged at 800 x g for 1 minute at room temperature. Next, the sample was incubated with the beads being sure to add enough volume to allow the beads to move and the tubes were placed on top of the rotator and incubated over night at 4°C into a cold room.  The following day, the beads were centrifuged at 800 x g for 1 min at room temperature. A series of 10 washed were performed on the beads in the following way: A volume of 500µL was added onto the beds, which were incubated for 2 min into a tumbling rotator at room temperature. After the incubation time the beads were centrifuged at 800 x g for 1 min at room temperature. Regarding the washing buffer containing urea, the buffer was added onto the beads and directly centrifuge without any further incubation. The buffer used to wash the beads are the following in order of execution: (i) RIPA buffer, (ii)RIPA buffer, (iii) 1 M KCl, (iv) 0.1 M Na2CO3, (v) 2 M Urea in 10 mM Tris-HCl pH:8, (vi) RIPA buffer, (vii) RIPA buffer, (viii) 0.1 M TEAB pH:8, (ix) 0.1 M TEAB pH:8 and (x) 2 M Urea in 0.1 M TEAB pH 8. Next, the sample were incubated with 300µL of 5 mM DTT in 4M Urea/100 mM TEAB pH 8 at 37°C for 1 hour, while rotating. After the incubation was completed, 25 mM acrylamide final concertation, was added to the sample and the sample further incubated for 30 min at room temperature while rotating. Next, 5 mM final concentration were added to each sample and incubated for 10 min at room temperature while rotating. Finally, for 1 mg of protein lysate 0.65 µg of LysC in 4 M Urea/100 mM TEAB pH 8 were added to the beads solution and the sample were incubated at 37°C for 6 hours while rotating. Next, 100 mM TEB were used to dilute the urea to the final concentration of 1.6 M and 1.65 µg of trypsin were added and further incubated at 37°C over night while rotating. The following day, the tubes were centrifuged at 800 x g for 1 min, the supernatant transferred into a fresh tube and the peptide were extracted by incubating the beads for 10 min with 300 µL of 5% ACN and 0.5% AcOH buffer while rotating at room temperature. The obtained supernatant was merged with the digestion mixture obtained before. The digestive enzymatic reaction was stopped by adding 1% final concentration of FA to ach samples which was further processed for desalting following the manufacture´s protocol."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Thermo.raw files were processed using Spectronaut software from Biognosys (v 19.5.24116.62635) in the directDIA mode. In particular, 3 to 6 fragment ions for each peptide with the Pulsar search engine incorporated in Spectronaut and UniProt Mus musculus (released 07-01-2022 with 17,090 entries). For database searching, the following settings were applied: trypsin/P (with 2 allowed missed cleavages); fixed modification: propionamide at cysteine; variable modifications: acetylation at protein N-termini and oxidation of methionine. Next, the false discovery rate (FDR) for peptide and protein identification was set to 1%. For peptide/protein quantification, a q-value cutoff of 0.01 and 0.05, respectively. No normalization strategies were applied."],"omics_type":["Proteomics"],"labhead":["Dominic Winter"],"instrument_platform":[""],"labhead_affiliation":["Research Center One Health Ruhr, University Alliance Ruhr & University Hospital Essen, Medical Faculty, University Duisburg-Essen"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["sarab@uni-bonn.de"],"submitter_affiliation":["Institute of Biochemistry and Molecular Biology"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Fractionated proteomics identifies a protein network mitigating resistance exercise-induced damage in human skeletal muscle","description":"Resistance exercise (RE) improves strength and muscle mass, with multiple benefits for human health. However, intense RE also induces acute myofibrillar damage. The molecular mechanisms that preserve, mark, degrade and restore damaged proteins in order to to keep skeletal muscle working under RE are incompletely understood. Here we study acute molecular and structural responses to RE-induced damage in repeatedly sampled human skeletal muscle in the unadapted, adapted and deadapted state. We show that acute, repeated and interrupted RE induces dynamic changes of the protein landscape associated with the muscular cytoskeleton and myofibrillar lesions. These changes correlate with changes in phosphorylation that are part of a larger molecular signaling footprint indicative of adaptation and deadaptation. We further identify a functional protein network linked to the muscle maintenance protein BAG3, which comprises the mechanosensory proteins PDLIM3 and XIRP1, the small heat shock proteins HSPB1 and HSPB5 and the lipid droplet associated protein PLIN5. All network components exhibit altered phosphorylation and increased cytoskeletal association after damaging RE and cooperate in the recognition of strained muscular structures and the degradation of damaged proteins through chaperone-assisted selective autophagy (CASA). Our study thus reveals previously unrecognized key regulators of muscle homeostasis in 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