{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/proteinGroups_MDA.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/proteinGroups_PD_BT549.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/checksum.txt"],"Xml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/mqpar_bt549.xml","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/mqpar_mdamb231.xml"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/PD_BT_7LUGLIO25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/PC_BT_7LUGLIO25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/PD_MDA_7LUGLIO25.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072866/PC_MDA_7LUGLIO25.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["montimar@unina.it"],"submitter":["ilaria iacobucci"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"disease":["Breast Cancer"],"software":[""],"submitter_keywords":["Human","Pulldown","Aptamers","Tumor","Tnbc","G4","Gquadruplex","Triple negative breast cancer","Cancer"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072866"],"tissue":["Breast"],"sample_protocol":["Nuclear extracts from MDA-MB-231 (~600 µg) and BT-549 (~1000 µg) cells were pre-cleared by incubation with 40 µg CPG-ds27 beads in buffer C (20 mM HEPES pH 7.9, 150 mM NaCl, 100 mM KCl, 1 mM EDTA, 1 mM EGTA, 0.5 mM PMSF, 0.05% Tween-20) for 2 hours at 4°C. The unbound fraction was then incubated overnight at 4°C with 37.5 µg CPG-tel46 beads (AP-MS workflow). Beads were washed three times with buffer C and bound proteins were eluted using 5% SDS in 50 mM ammonium bicarbonate (pH 8 after 10 minutes at 99°C. Eluates were processed by shotgun proteomics: proteins were digested on S-Trap microcolumns (Protifi) and peptides were resuspended in 0.2% formic acid. LC–MS/MS analysis was performed on an Orbitrap Exploris 240 coupled to a Vanquish Neo nanoUPLC (Nanospray Flex source) using a solvent gradient from 2% to 30% B over 60 minutes and to 50% B over 5 minutes (solvent A: 2% acetonitrile, 0.2% formic acid in water; solvent B: 0.2% formic acid in acetonitrile with 2% water). Data were acquired in DDA mode selecting the top 20 precursors, m/z 300–1800, Orbitrap resolution 120,000."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Raw files were processed in MaxQuant v2.0.1.0 using the Andromeda search engine against the UniProt Homo sapiens reference proteome. Protein identification required ≥3 peptides per protein, including ≥1 unique peptide. Variable modifications were set to methionine oxidation and N-terminal pyroglutamate formation from glutamine. Mass tolerances were 10 ppm for the first search and 5 ppm for the main search. A reverse decoy approach was used to control identifications at 1% FDR (FDR = 0.01). Proteins detected with CPG-ds27 were subtracted, and proteins recovered with CPG-tel46 were considered specific interactors. To reduce non-specific binders, the interactor list was filtered using CRAPome (Workflow 1; database “H. sapiens – All”), removing proteins present in >40% of prior experiments."],"omics_type":["Proteomics"],"labhead":["Maria Monti"],"instrument_platform":[""],"labhead_affiliation":["Università degli studi di Napoli Federico II Dipartimento delle Scienze Chimiche"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["40898188 Iacobucci I, Cipollone I, Cozzolino F, Gaglione R, Mentino MR, Platella C, Musumeci D, Arciello A, Montesarchio D, Monti M. Integrating proteomics and bioinformatics for the identification of breast cancer biomarkers interacting with telomeric G-quadruplex. Cancer Cell Int. 2025 25(1):319 10.1186/s12935-025-03955-z"],"submitter_mail":["iacobucci@ceinge.unina.it"],"submitter_affiliation":["Department of Chemical Sciences, University of Naples Federico II, Naples 80126, Italy \nCEINGE Advanced Biotechnologies, University of Naples Federico II, Naples 80145, Italy"],"submitter_country":["Italy"],"pubmed_abstract":["The identification of reliable biomarkers is essential for improving breast cancer (BC) detection, prognosis, and treatment. This study explores a human telomeric G-quadruplex (G4) model, tel<sub>46</sub>, functionalized on Controlled Pore Glass (CPG) support, as a novel biomarker discovery tool. The oligonucleotide tel<sub>46</sub> mimics multimeric G4 structures in telomeric overhangs. Using affinity purification-mass spectrometry, 93 proteins interacting with tel<sub>46</sub> were identified starting from nuclear extract of MCF7 cells, linking them to pathways in DNA replication, repair, and genome stability, which are frequently altered in cancer. Integrating AP-MS data with quantitative proteomics comparing MCF7 to non-tumorigenic MCF10A cells, 27 tel<sub>46</sub> interactors were identified among upregulated proteins. Functional analyses revealed enrichment in genome maintenance and repair pathways, while downregulated proteins were associated with fundamental cellular functions. Further bioinformatics analysis using public cancer proteomics database 19 were validated. Bioinformatic analysis based on transcriptomics and clinical data revealed MSH6, MSH2, ESRP1, and WDHD1 as the most promising potential biomarkers for breast cancer. Indeed, these proteins are highly expressed in BC and generally correlated to poor prognosis: in addition to their role as potential biomarkers for early diagnosis, these proteins might be used as targets for specific treatment, enhancing radiation sensitivity or decreasing tumour cell proliferation. As a proof-of-concept, this study proposes tel<sub>46</sub>-functionalized CPG as a potential tool for isolating cancer-related proteins and underscores the potential of G4-interacting proteins as biomarkers for BC diagnosis and therapy. Moreover, these findings establish a basis for further research into G4-mediated cancer mechanisms."],"pubmed_title":["Integrating proteomics and bioinformatics for the identification of breast cancer biomarkers interacting with telomeric G-quadruplex."],"pubmed_authors":["Iacobucci Ilaria I, Cipollone Irene I, Cozzolino Flora F, Gaglione Rosa R, Mentino Maria Rosaria MR, Platella Chiara C, Musumeci Domenica D, Arciello Angela A, Montesarchio Daniela D, Monti Maria M"],"additional_accession":[]},"is_claimable":false,"name":"Combining proteomics and machine learning to identify potential triple negative breast cancer biomarkers binding telomeric G-Quadruplex","description":"Triple-negative breast cancer (TNBC) lacks ER, PR and HER2 expression, represents ~10–20% of invasive breast cancers, and is clinically aggressive with limited targeted treatment options. Its pronounced molecular heterogeneity challenges single-marker diagnostics, motivating the development of robust biomarker panels for early detection and disease monitoring. Aptamers, and particularly guanine-rich DNA sequences forming G-quadruplexes (G4s), provide stable and versatile molecular recognition tools. Telomeric G4 structures are biologically relevant in genome maintenance and can enrich disease-related protein interactors, making them attractive baits for translational biomarker discovery.  Here, we employed an overhang human telomere model capable of forming two consecutive G4s (tel46) immobilized on Controlled Pore Glass (CPG) to profile the nuclear G4 interactome in two TNBC cell lines, MDA-MB-231 and BT-549. Using affinity purification–mass spectrometry (AP-MS) with CPG-tel46 combined with quantitative proteomics and stringent background subtraction, we identified tel46-associated proteins consistently upregulated in both tumour models and prioritized 11 candidates supported by downstream bioinformatic validation.  To move beyond single-marker evaluation, we implemented a machine-learning framework to assess candidate proteins as a coordinated molecular signature. Regularized models with embedded feature selection and cross-validation were used to identify stable, discriminative combinations while controlling overfitting. This integrative strategy supports G4-based capture as a practical approach to enrich clinically relevant interactors and prioritize diagnostic panels. We propose a five-protein signature (KIF4A, ACIN1, RBM12, FOXK1 and NCAPD2) as a candidate classifier for TNBC early diagnosis, providing a foundation for independent validation in clinical 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