{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/Raw_file_description_revised.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/checksum.txt"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/Mouse_Tissue_Contaminants.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/uniprot-proteome_UP000000589_mouse.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/Peptidergic_nonpeptidergic_single_tissue_cell_tissue_bulk_raw_data.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/mouse2023_contaminant.predicted.speclib","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/Neurofilaments_single_tissue_cell_raw_tissue_bulk_raw_data.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/Cell_culture_raw_data.rar","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/Cell_culture_DIA-NN_output.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/Peptidergic_nonpeptidergic_single_tissue_cell_DIA-NN_output.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD070495/Neurofilaments_singe_tissue_cell_tissue_DIA-NN_output.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["fabian.coscia@mdc-berlin.de"],"submitter":["Fabian Coscia"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070495"],"tissue":["Neuron","Pain Receptor Cell","Electrically Active Cell","Mechanoreceptor Cell"],"sample_protocol":["Sample preparation was performed as previously described17. Briefly, before sample prepara-tion, 15 μl of acetonitrile (HPLC grade, VWR, cat. 83640.290) was added to each well, vor-texed, and dried using speedvac. This drying process ensured that the sample contours were concentrated at the bottom of each well. Pipetting was performed either manually or using the MANTIS Liquid Dispenser (Formulatrix, V3.3 ACC RFID, software version 4.7.5) and high-volume diaphragm chips (Formulatrix, cat.no. 233128 ).For cell culture, samples were first incubated  in 4 μl 60mM Triethylammonium bicarbonate pH 8.5 (TEAB; Merck, cat.no. T7408-100ML) at 95 °C for 60 min. Then, the samples were cooled, and 1μl of 100% ACN (HPLC-grade, VWR, cat. 83640.290) was added and incubated for 60 min at 75 °C. Next, 1 μl of LysC (Promega, cat. no VA1170) (2 ng/μL) was added, fol-lowed by a 2 h digestion at 37 °C. Then, 1 μl of trypsin (Promega, cat.no. V5117) (2 ng/µL) was added with overnight incubation at 37 °C in the thermal cycler. Digestion was stopped the next day by addition of trifluoroacetic acid (TFA, final concentration 1% v/v) (cat. no. 96924-250ML-F). The samples were vacuum dried before peptide clean-up. For tissue samples, the lysis buffer for sample preparation consisted of 0.1% n-dodecyl-beta-maltoside (DDM; Sigma-Aldrich, cat.no. D4641-500MG), 5mM Tris (2-carboxyethyl) phos-phine hydrochloride (TCEP; Sigma-Aldrich, cat.no. C4706-2G), 20mM 2-chloroacetamide (CAA; Sigma-Aldrich, cat.no. C0267-100G and 0.1M TEAB in water. 2μL of lysis buffer were added to wells containing samples and incubated for 60 min at 95 °C. Subsequently, 1 μL of LysC (Promega, cat.no VA1170) (2 ng/μL) was added and digested for 2 h at 37°C, fol-lowed by addition of 1 μl of trypsin (Promega, cat.no. V5117) (2 ng/ul) and overnight diges-tion at 37 °C in a thermal cycler. After digestion, the reaction was stopped by adding trifluoroa-cetic acid (TFA, final concentration 1% v/v) (cat. 96924-250ML-F). The samples were then vacuum-dried before peptide clean-up by EvoTips."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["We used DIA-NN6 (version 1.8.1) for the dia-PASEF raw file analysis and spectral library generation. For spectral library generation to analyze dia-PASEF data, the mouse FASTA file was downloaded from Uniprot (2023 release, UP000000589_10090 Mus Musculus, down-loaded on August 2nd). DIA-NN in silico predicted libraries were generated using the mouse FASTA file, and frequently found contaminants62 (mouse + mouse tissue contaminants). Deep learning-based spectra, RTs, and IMs prediction were enabled for the appropriate mass range of 300-1000 m/z. N-terminal M excision and cysteine carbamidomethylation were enabled as fixed modifications. A maximum of two missed cleavages were allowed, and the precursor charge was set to 2–4. The library consisted of 22092 protein isoforms, 34222 protein groups, and 6776851 precursors in 3121869 elution groups.DIA-NN63 was operated in the default mode with minor adjustments. Briefly, MS1 and MS2 accuracies were set to 15.0, scan windows to 0 (assignment by DIA-NN), isotopologues were enabled, no MBR for project-specific DIA-NN-refined libraries, heuristic protein inference, and no shared spectra.  Proteins were inferred from genes, neural network classifier was set to single-pass mode, quantification strategy as ‘Robust LC (high precision).’ Cross-run normali-zation was set to ‘RT-dependent,’ library generation as ‘smart profiling,’ speed and RAM us-age as ‘optimal results.’"],"omics_type":["Proteomics"],"labhead":["Fabian Coscia"],"instrument_platform":[""],"labhead_affiliation":["Max-Delbrück-Center for Molecular Medicine in the Helmholtz Association (MDC), Spatial Proteomics Group, Berlin, Germany (lab head)"],"species":["Mus Musculus (mouse)"],"submission_type":["PARTIAL"],"submitter_mail":["fabian.coscia@mdc-berlin.de"],"publication":["10.1038/S41467-026-71418-8"],"submitter_affiliation":["Max Delbrück Center"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Deep visual proteomics uncovers nociceptor diversity and pain targets ","description":"The richness of our somatosensory experience is reflected in the functional diversity of somatic sensory neurons. Single-cell sequencing (scRNA) of sensory neurons has revealed a molecular basis for such diversity1–3. However, sensory neuron diversity has yet to be captured at the level of the proteome. Here, we combined electrophysiology with deep visual proteomics (DVP)4 to quantify over 6,000 proteins from phenotypically-defined sensory neurons in mice and identified proteomic markers of sensory neuron subtypes. Comparative analysis revealed both concordance and meaningful divergence between transcriptomes and proteomes. We further show that up to 3,000 proteins can be quantified from one-fourth of a single neuron, demonstrating subset-specific protein signatures. In culture, nociceptive neurons can be acutely sensitized to mechanical stimuli by nerve growth factor (NGF) which normally drives inflam-matory pain in vivo5.  Indeed, overnight exposure of peptidergic nociceptors to NGF and a pro-tein kinase C (PKC) activator produced functional sensitization associated with proteome changes. Functional knockdown experiments identified the up-regulated B3GNT2 enzyme as a potential effector of nociceptor sensitization. In summary, we present a high-resolution proteomic resource linking molecular identity to function, enabling the discovery of mechanisms un-derlying somatic sensation and pain sensitization. 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