{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067113/samples.xlsx"],"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067113/search_DIA-NN.tsv.zip"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067113/UP000005640_9606_original_Abeta_MaptIsoforms_additional.fasta"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/07/PXD067113/raw_data_part4.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["k.w.li@vu.nl"],"submitter":["Evangelia Thanou"],"technology_type":["Mass Spectrometry","diaPASEF","Gel-based experiment","Bottom-up proteomics","Data-independent acquisition"],"disease":["Alzheimer's Disease"],"software":[""],"submitter_keywords":["Post--mortem","App","Load","Ad","Abeta","Brain proteomics","Ptms","Mapt","Eoad","Alzheimer's"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067113"],"tissue":["Brain"],"sample_protocol":["Library generation Brain tissues were potter extracted in 1% n-dodecyl-β-D-maltoside (DDM), and centrifuged in the Eppendorf tubes for 10 min at 18,000x g, 4 °C. The soluble and insoluble fractions were separately solubilized in Tricine sample buffer (pH=8.45) and run on a 10% Tricine gel (Novex Tricine Mini Protein Gel from Invitrogen) that separated proteins down to 2.5 kDa. The gel lane was stained with colloidal Coomassie Blue G-250, cut into 26 fractions, destained and then digested by trypsin/Lys-C (Promega) as described previously.  The peptide solution was transferred to an Evotip and run on a 15 cm x 75 µm, 1.9 µm Performance Column (EV1112, EvoSep) using the Evosep One liquid chromatography system with the 30 samples per day program. Peptides were electro-sprayed into a TimsTOF Pro 2 mass spectrometer (Burke) and analyzed with ddaPASEF. The MS scan was between 100-1700 m/z. The Tims settings were 1/Ko from start to end between 0.6-1.6 Vs/cm2, ramp time 100 ms, accumulation time 100 ms, and ramp rate 9.42 Hz. The raw data were analyzed by Fragpipe Version 22.0 with variable modifications of Ser/Thr/Tyr phosphorylation, Lys ubiquitination, Lys acetylation, Lys methylation/di-methylation/tri-methylation, and Met oxidation, using trypsin digestion with 2 missed cleavages, precursor mass tolerance of 10ppm and fragment mass tolerance 20ppm. The FASTA files for database search consisted of UP000005640_9606.fasta from UniProt reference proteomes 2023-03. We created several artificial precursors that contain known Aβ isoforms and incorporated these into the FASTA for the database search. The validation tools used in Fragpipe were MSBooster with predict RT and predict spectra for rescoring using deep learning prediction, PSM validation with Percolator, PTM site localization with PTMprophet, and protein inference with proteinprophet. A spectral library was generated with EasyPQP version 0.1.50.  Sample preparation and LC-MS analysis Fresh frozen tissue of the middle temporal lobe was cut in 10 µm thick sections using a cryostat and mounted on polyethylene naphthalate-membrane slides (Leica, Herborn, DE). Sections were fixed in 100% ethanol for 1 minute and stained using 1% (w/v) toluidine blue in H2O (Fluka Analytical, Buchs, Switzerland) for 1 minute. Laser micro dissection (LMD) was performed using a Leica AS LMD system (Leica, Wetzlar, Germany) to isolate 0.5 mm3 of grey matter tissue and collected in 30 µl 3 M-PER lysis buffer (Thermo Scientific, Rockford, IL, USA) in 0.5 ml Eppendorf PCR tubes and stored at -80 °C until further use. Samples were heated to 95 °C for 5 minutes and loaded on 10% Bis/Tris- polyacrylamide gels and run into the gel for 15 min at 80 V using 1.5 M Tris/Glycine SDS running buffer at pH 8.3. Gels were fixed overnight and stained with colloidal Coomassie Blue G-250, before samples were cut out and small gel pieces of about 1 mm3 were placed in 96-well Nunc filter plates (Thermo Scientific, Rockford, IL, USA). Destaining, trypsin digestion, and peptide extraction were done as described. Tryptic peptides were analyzed in an Evosep-TimsTOF pro2 setup as described in the library generation section above, with the exception that diaPASEF was used."],"repository":["Pride"],"quantification_method":["Not available"],"modification":["","N6","N6-dimethyl-L-lysine"],"data_protocol":["The raw data were searched with DIA-NN 1.9.2, using the dedicated spectral library as described above. Protein inference was set to Isoform IDs. Match-between-runs was activated, with no shared spectra. MS-DAP 1.0.5 was used for downstream analysis of the DIA-NN results and to perform differential expression analysis. In MS-DAP settings, filter_min_detect was set to 3, filter_fraction_detect was set to 0.5, filter_fraction_quant was set to 0.5, Variance Stabilizing Normalization (VSN) and modebetween_protein was used to normalize the data.  The overexpression GO analysis was performed in Metascape, the gene set enrichment analysis was performed in GOAT. The analysis results of box-plots for tau tryptic peptides, the ROC plot, the correlation plot of peptide intensities between tau and post-translational modifications to Aβ, the volcano plot, and the heat map of Aβ intensities were generated using the CNSknowall platform (https://cnsknowall.com), the bar-plots and the cluster volcano plot by SRplot platform. Schematic diagram of tau with post-translational modification were drawn in the web server from IBS 2.0."],"omics_type":["Proteomics"],"labhead":["Ka Wan Li"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Molecular and Cellular Neurobiology, Center for Neurogenomics & Cognitive Research, Neuroscience Campus Amsterdam, VU University, Amsterdam, The Netherlands"],"species":["Homo Sapiens (human)"],"publication":["10.1002/ALZ.71662"],"submitter_mail":["e.thanou@vu.nl"],"submitter_affiliation":["Center for Neurogenomics and Cognitive Research, Department of Molecular and Cellular Neurobiology, Amsterdam Neuroscience, Vrije Universiteit Amsterdam, 1081 HV Amsterdam, The Netherlands."],"submitter_country":["Netherlands"],"additional_accession":[]},"is_claimable":false,"name":"Proteomics of post-mortem brains in early and late-onset Alzheimer's disease: unraveling differential Aβ effects and potential AD biomarkers_4","description":"Alzheimer’s disease (AD) is the most common form of neurodegeneration presented mainly as late-onset AD (LOAD), and in younger individuals early-onset AD (EOAD). The pathological hallmarks of AD are the hyperphosphorylated tau neurofibrillary tangles and the amyloid beta (Aβ) plaques. We examined changes in the proteome of post-mortem temporal cortex from individuals with EOAD and LOAD, and revealed that EOAD represents a more aggressive form of the disease. Notably, we observed up-regulation of AD biomarkers p-tau181, p-tau217, and p-tau23, and tau MTBR243, in AD tissues. Two abundant tau peptides phosphorylated at p-231/p-235 and p-231/p-235/p-237 were present largely in AD tissues, which may be developed as biomarkers. Aβ was detected in about half of the cognitively unimpaired elderly controls with subtle proteome changes that resembled in part the changes of biological processes in AD. This could indicate an early stage of neurodegeneration preceding clinical AD symptoms or represent an AD-resilient 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