{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/checksum.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/evidence.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/XC341062.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/mqpar.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/OE01346_NSF_1_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/OE01345_NSF_1_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/OE01351_NSF_3_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/OE01352_NSF_3_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/OE01348_NSF_2_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD057496/OE01349_NSF_2_2.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["magnojunqueira@iq.ufrj.br"],"submitter":["Guillaume Nugue"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Ipcs","Neurosphere","Lc-ms/ms","Tmt"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD057496"],"tissue":["Cell Suspension Culture","Fibroblast"],"sample_protocol":["To compare methods, we evaluated 10 distinct protein extraction protocols: Urea and Thiourea (UT), Urea (U), SDC, SDS, SPEED, FASP, and S-Trap. As a subsequent step, we included a detergent wash precipitation.  Protein digestions were performed using trypsin (Promega, USA) at a 1:50 trypsin-to-protein ratio, incubated overnight at 37°C. The digests were acidified by adding formic acid (FA) to a final concentration of 1%, then centrifuged to pellet insoluble material. Samples were desalted using home-made C18 Tips (R2 Poros®), with the wash solvent being 0.1% TFA, and elution solvents comprising 0.1% TFA in 50% acetonitrile (ACN) and 0.1% TFA in 70% ACN. The eluates were dried by vacuum centrifugation and stored at -80 °C.  Each condition of the TMT-10 Plex involved labeling 2 µg of peptides in 2 µl of 50 mM HEPES at pH 8.5, with the addition of 14 µg of TMT in acetonitrile (ACN) to achieve a final concentration of 12 mM. The labeling process included a 1-hour incubation at room temperature, with specific conditions assigned to each TMT channel as follows: 126: UT; 127N: U; 127C: SPEED; 128N: SDC; 128C: SDS; 129N: UT-A; 129C: U-A; 130N: SDC-P; 130C: FASP; and 131: S-Trap. Replicates for each method were designed across three separate TMT sets (Figure 3). Quenching was accomplished by adding 0.2 µl of 5% hydroxylamine and incubating for 15 minutes. The samples were then pooled in equal ratios (1:1:1:1:1:1:1:1:1:1) and subjected to washing using home-made C18 Tips (R2 Poros®) with a wash solvent of 0.1% TFA and elution solvents of 0.1% TFA in 50% ACN and 0.1% TFA in 70% ACN. The pooled samples were dried via vacuum centrifugation and subsequently frozen at -80 °C."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Tryptic peptides for single-shot analyses were examined using a Vanquish Neo UHPLC system coupled to an Exploris 480 mass spectrometer (Thermo Fisher Scientific). Following reconstitution in 0.1% TFA, 500 ng of peptides were injected. Peptide separation was achieved on a 75 µm x 75 cm analytical column (EASY-Spray, C18 resin; Thermo Fisher Scientific) with a flow rate of 300 nl/min. A 5-minute linear gradient was initiated with 2% LC solvent B (90% ACN, 0.1% FA) in solvent A (0.1% FA), followed by a three-step gradient: from 2% to 25% at 105 minutes, from 25% to 40% at 125 minutes, and reaching 99% at 125.1 minutes. The mass spectrometer operated in data-dependent acquisition mode with positive ionization. MS1 spectra were recorded at a resolution of 120k, with an automatic gain control (AGC) target of 3e6 or 1e6 charges and a maximum injection time (maxIT) of 105 ms. MS2 spectra were acquired at a resolution of 60k, using an AGC target of 6e4 and a maxIT of 105 ms. The cycle time was set to 2 seconds.  MaxQuant software version 2.4.9.0 was utilized to analyze the raw mass spectrometry (MS) data. For the MS2 search, the canonical Homo sapiens (human) Swiss-Prot database (UP000005640.fasta, release 2024_15_01, www.uniprot.org) was queried. The search parameters included trypsin/P digestion with a maximum of 2 missed cleavages allowed. A precursor mass tolerance of 20 ppm and a 0.05 Da tolerance for MS2 fragments were specified. The isobaric labels for TMT 10 Plex were configured with a 0.003 Da reporter mass tolerance for Reporter MS2. Carbamidomethylation of cysteines was set as a fixed modification, while variable modifications included oxidation of methionine, protein N-terminal acetylation. To ensure data reliability, a false discovery rate of < 1% for both peptides and proteins was enforced using a reverse database search strategy."],"omics_type":["Proteomics"],"labhead":["Magno Rodrigues Junqueira"],"instrument_platform":[""],"labhead_affiliation":["Laboratory of Translational Mass Spectrometry and Neuroproteomics, IQ-UFRJ"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["nugueg@me.com"],"publication":["10.1016/J.JPROT.2025.105576"],"submitter_affiliation":["UFRJ"],"submitter_country":["Brazil"],"additional_accession":[]},"is_claimable":false,"name":"Optimized Pipeline for Personalized Neurobiological Insights from Single Patient-Derived Neurospheres","description":"Quantitative proteomic approaches such as TMT labeling enable the amplification of biological material by combining multiple samples into a single analysis. This technique maximizes the data extracted from each sample and allows for precise comparative quantitative analysis between different experimental groups. In this study, we aimed to optimize the workflow for proteomic investigations using neurospheres derived from induced pluripotent stem cells (iPSCs). To improve both the efficiency and accuracy of our proteomic analysis, we compared different protocols and employed Tandem Mass Tag (TMT) labeling. Human neurospheres are three-dimensional, free-floating clusters primarily composed of neural progenitor cells, early-stage neurons, and radial glia. This diverse cell population more closely replicates the complexity of neural development compared to traditional 2D cultures, providing a more relevant model for studying neurogenesis, cell differentiation, and the underlying mechanisms of neurological diseases. Enhancing in vitro models through advanced cell culture techniques is crucial for reducing reliance on animal studies. In neural research, where access to human-relevant data is increasingly feasible, such improvements foster a deeper understanding of neural mechanisms and potential therapeutic targets. The use of 3D cultures represents a significant step forward in accurately modeling neural behavior and disease progression. By optimizing proteomic workflows and employing advanced labeling techniques, this study contributes to the development of more reliable and comprehensive in vitro neural models. This, in turn, supports the broader goal of advancing neural research while reducing reliance on animal models, leading to more ethical and potentially more accurate scientific outcomes that are clinically relevant to 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