{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/Search_results_mouse_NMJ_proteomics.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/files_description.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/S20241211-25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/S20220929-07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/S20241211-24.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/S20220929-04.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/S20220929-03.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/Z20220722-07.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/S20220929-06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/Z20220722-06.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD067080/S20241211-23.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["rasband@bcm.edu"],"submitter":["Juan Oses-Prieto"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"disease":["Duchenne Muscular Dystrophy"],"software":["Not available"],"submitter_keywords":["Duchenne muscular dystrophy","Proximity labelling","Muscle proteomics","Neuromuscular junction","Turboid","Perijunctional zone","Perilipin 4"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067080"],"tissue":["Sternocleidomastoid Muscle"],"sample_protocol":["To biotinylate proteins, biotin was delivered intraperitoneally (240 mg/kg body weight) into control, NF-TurboID, and mdx;NF-TurboID mice. Muscles were harvested 24 hours later. Mice were euthanized and sternomastoid muscles dissected. Dissected muscles were placed in 1.5 mL tubes with 100 mg of 1 mm ZrO2 beads (Next Advance, Cat# ZrOB10) and 0.25 mL of lysis buffer (50mM Tris/HCl pH 7.5, 150 mM NaCl, 1 mM EDTA, 0.4% SDS, 2% Triton X100, 2% deoxycholate plus proteinase inhibitor cocktail and PMSF). Tissues were homogenized using a Bullet Blender 5E Pro (Next Advance, Cat# BT5E) for 1 minute on setting 10. Homogenate was cooled on ice for 5 minutes then briefly spun on a bench top centrifuge. 0.25 mL of 2x lysis buffer was added to the homogenate and. The homogenization procedure was repeated 3 times. The homogenate was then transferred to an Eppendorf tube and sonicated on ice with a probe sonicator 3 times for 7 seconds. The homogenate was then centrifuged at 1000Xg for 10 minutes at 4° C  and the supernatant was collected, and biotinylated proteins were captured using magnetic sepharose beads, and rinsed several times. Sample-incubated streptavidin sepharose beads were resuspended in 5 mM DTT in 100 mM NH4HCO3 and incubated for 30 min at room temperature. After this, iodoacetamide was added to a final concentration of 7.5 mM and samples incubated for 30 additional minutes. In all, 0.5 μg of sequencing grade trypsin (Promega) was added to each sample and incubated at 37 °C overnight. Supernatants of the beads were recovered, and beads digested again using 0.5 μg trypsin in 100 mM NH4HCO3 for 2 h. Peptides from both consecutive digestions were recovered by solid phase extraction using C18 ZipTips (Millipore, Cat# ZTC18S096), and resuspended in 0.1% formic acid for analysis by liquid chromatography-mass spectrometry"],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Peak lists were generated using PAVA software (Guan, S., Price, J.C., Prusiner, S.B., Ghaemmaghami, S., and Burlingame, A.L. (2011). Mol Cell Proteomics 10, M111 010728.).. All generated peak lists were searched against the mouse subset of the SwissProt database (SwissProt.2019.07.31) using Protein Prospector (Clauser, K.R., Baker, P., and Burlingame, A.L. (1999). Analytical chemistry 71, 2871-2882). The database search was performed with the following parameters: a mass tolerance of 10 ppm for precursor masses; 30 ppm for MS/MS, cysteine carbamidomethylation as a fixed modification and acetylation of the N terminus of the protein, pyroglutamate formation from N-terminal glutamine, and oxidation of methionine as variable modifications. All spectra identified as matches to peptides of a given protein were reported, and the number of spectra (Peptide Spectral Matches, PSMs) used for label free quantitation of protein abundance in the samples"],"omics_type":["Proteomics"],"labhead":["Matthew Rasband"],"instrument_platform":[""],"labhead_affiliation":["Professor and Vivian L. Smith Endowed Chair in Neuroscience Department of Neuroscience. Baylor College of Medicine  Houston, Texas United States"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["joses@cgl.ucsf.edu"],"publication":["Not available"],"submitter_affiliation":["UCSF"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"The Perijunctional Zone Is a Molecularly Distinct Muscle Subdomain Altered in Duchenne Muscular Dystrophy","description":"The neuromuscular junction (NMJ) is a well-established model for synapse development, structure, and function. Surrounding the NMJ is a narrow perijunctional zone (PJZ), enriched in muscle-specific voltage-gated sodium channels that prevent synaptic fatigue. Despite this role, the PJZ remains poorly characterized. To determine its molecular composition, we engineered mice to express the biotin ligase TurboID fused to the cell adhesion molecule neurofascin (Nfasc), and that localizes to the PJZ through ankyrin scaffolding proteins. Using proximity proteomics, we identified numerous PJZ-associated proteins, including Perilipin 4 (Plin4), that were highly enriched and clustered at the PJZ. We also performed proximity proteomics on the PJZ of mdx mice, a model of Duchenne muscular dystrophy.  We found broad changes in PJZ composition, including significantly reduced PJZ Plin4. These findings establish the PJZ as a molecularly distinct subdomain of skeletal muscle and provide insight into its potential roles in neuromuscular function and 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