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At the end of treatment, cells were harvested by incubation with EDTA solution (Versen, PanEco) and scraping, pelleted by centrifugation, washed once with ice-cold PBS, and stored at −80°C until further use. For each condition, 3 biological replicates were processed. Cell lysis was performed by resuspending pellets in 500 µL of 100 mM Tris-HCl pH 7.9 (Helicon, Russia) containing a protease inhibitor mixture (Pepstatin A, Chymostatin, PMSF) followed by five cycles of freezing and thawing.  Protein precipitation and delipidation were performed by adding 2 mL ice-cold acetone to each lysate, incubating overnight at −20°C, and centrifuging for 15 min at 8,000 × g at 4°C. Supernatants were discarded and pellets were allowed to dry in open-cap tubes at −20°C overnight. Dried pellets were solubilized in 250 µL of 100 mM Tris-HCl pH 8.5 containing 2% sodium deoxycholate (SDC; Sigma-Aldrich). Total protein concentration was determined using the MicroBCA assay (Thermo Fisher Scientific) according to the manufacturer’s protocol. Disulfide bonds were reduced and alkylated by adding tris(2-carboxyethyl)phosphine (TCEP) and 2-chloroacetamide (CAA) to final concentrations of 10 mM each, followed by incubation at 85°C for 30 min. Samples were diluted with triple-distilled water to a final SDC concentration of 1% and digested with modified recombinant LC-MS grade trypsin (Molecta, Russia) at a 1:50 (enzyme:protein) ratio overnight at 37°C. Digestion was quenched by adding 20 µL of 10% trifluoroacetic acid (TFA). SDC detergent was removed by liquid–liquid extraction with water-saturated ethyl acetate (5 iterations). The organic and aqueous phases were separated and solvents evaporated in a SpeedVac concentrator. Tryptic peptides were desalted using MCX-type StageTips. Final peptide eluates were dried completely in a SpeedVac and stored at −80°C until LC-MS/MS analysis. For LC-MS/MS, peptides were reconstituted in 5% acetonitrile / 0.1% TFA to a final concentration of 0.3 µg/µL. Samples (5 µL injections) were loaded on a Dionex Ultimate 3000 NCS-3500RS nano-HPLC system and concentrated on a trap column (100 µm × 50 mm, Luna C18, 3 µm) at 3 µL/min in 5% ACN/0.1% FA/0.02% TFA, then separated on an analytical nano-column (75 µm × 300 mm, Aeris Peptide C18 1.7 µm) using a 210-min concave gradient (5 − 55% ACN, curve coefficient = 6) at 300 nL/min. Eluting peptides were analyzed online on a Thermo Orbitrap Elite mass spectrometer via nano-ESI (emitter voltage 3 kV; capillary temperature 260°C). Data were acquired in data-dependent acquisition (DDA) mode. MS1 scans were collected in the Orbitrap at 60,000 resolution over 400–2000 m/z with a maximum injection time of 100 ms. The top 15 most abundant precursor ions were selected for CID fragmentation in the linear ion trap (MS2) with maximum IT 25 ms, isolation width 1.0 m/z, and normalized collision energy (NCE) 35%. Dynamic exclusion was set to 120 s. Instrumental technical replicates were acquired as duplicate injections per sample."],"repository":["Pride"],"labhead":["Igor Kasheverov"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["Laboratory of Ligand-Receptor Interactions, Department of molecular neuroimmun signaling, Shemyakin-Ovchinnikov Institute of bioorganic chemistry of Russian academy of sciences, Moscow, Russian Federation"],"publication":["10.6019/PXD070911","10.1007/s12031-026-02523-y"],"submitter_affiliation":["IBCH RAS"],"labhead_mail":["shak_ever@yahoo.com"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"disease":["Brain Glioblastoma Multiforme"],"submitter_keywords":["total proteome","choline","orbitrap elite","proteomics","u87mg","label-free quantification","Glioblastoma","Glioblastoma; u87mg; α7 nicotinic acetylcholine receptor; choline; total proteome; label-free quantification; orbitrap elite; proteomics","α7 nicotinic acetylcholine receptor"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070911"],"modification":[""],"quantification_method":[""],"data_protocol":["The raw data files were analyzed using PEAKS Studio 11 (Bioinformatics Solutions, Canada). Proteomic LC-MS/MS data were searched against the Human Protein Database (204,906 entries) imported from the UniProtKB reference proteome in December of 2023. The analysis workflow included de novo sequencing, database search, and label-free quantification (LFQ). Search parameters: enzyme = trypsin (C-terminal to K/R), allowing up to 3 missed cleavages; fixed modification = carbamidomethylation (C, +57.021 Da) introduced by CAA; variable modifications = oxidation (M, +15.995 Da), deamidation (N/Q, +0.984 Da); precursor mass tolerance = 15 ppm; fragment mass tolerance = 0.5 Da; maximum variable modifications per peptide = 3. Peptide-spectrum matches (PSMs) were filtered to a 1% false discovery rate (FDR) at the PSM level using the target-decoy approach. Proteins were reported using PEAKS 11 default protein inference/grouping rules and required at least two unique peptides for reporting. For LFQ processing, only features with intensities of at least 100,000 were retained, and alignment was performed using the control sample as the base reference. Peptide features were further filtered to include only those with an average peak area of at least 200,000, a quality score of 20 or higher, and charge states ranging from 2 to 5. Features were required to be detected in at least one sample per experimental group. Statistical analysis was conducted using ANOVA with modified exclusion and outlier removal enabled, and quantification was based on the top three peptides per protein. Normalization across samples was performed using the Total Ion Current (TIC) method.  After PEAKS processing, identification and quantification tables were exported and further analyzed using Microsoft Excel (version 2507, 2019, Microsoft Corporation) and the R statistical environment for additional filtering, visualization, and integration with downstream analyses."],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)"],"submitter_mail":["gondarenkoea@gmail.com"],"submitter_country":["Russia"],"doi":["10.6019/PXD070911"],"additional_accession":[]},"is_claimable":false,"name":"α7 Nicotinic Acetylcholine Receptor-Associated Signaling in U87MG Glioblastoma Cells (LFQ, Orbitrap Elite)","description":"This project investigates the role of α7 nicotinic acetylcholine receptor (α7 nAChR) signaling in glioblastoma using the U87MG human glioblastoma cell line. Cells were treated with selective α7 nAChR ligands (10 μM of agonist PNU282987, 1 μM of positive allosteric modulator PNU120596, 1 μM of antagonist α-cobratoxin) and their combination. Whole-cell lysates were processed for total proteome analysis, proteins were digested in-solution with trypsin and peptides analyzed by nano-ESI-LC-MS/MS on a Thermo Orbitrap Elite using DDA. Data were searched with PEAKS Studio 11 against the UniProtKB Human database and quantified by label-free quantification (LFQ). Proteomic changes in cytoskeletal, metabolic and ER-associated proteins were detected.","dates":{"publication":"2026-06-08","submission":"2025-11-18"},"accession":"PXD070911","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:906914","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:13037","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","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