{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/report_pg.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/report.log.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA3_REP2_20250714003303.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT3_REP1_20250714154448.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT2_REP2_20250714113258.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA1_REP3_20250713153952.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF2_REP3_20250715055009.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT2_REP1_20250714095944.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT1_REP3_20250714075300.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF3_REP2_20250715092955.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA1_REP2_20250713140640.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT1_REP1_20250714044634.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA2_REP3_20250713205307.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA1_REP1_20250713123330.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF1_REP1_20250714213108.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA3_REP1_20250713225953.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT1_REP2_20250714061946.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT2_REP3_20250714130610.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT3_REP3_20250714185059.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF1_REP3_20250715003719.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF1_REP2_20250714230414.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA2_REP1_20250713174642.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF3_REP3_20250715110257.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA3_REP3_20250714020611.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/BT3_REP2_20250714171753.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF2_REP1_20250715024356.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF3_REP1_20250715075649.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MCF2_REP2_20250715041703.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD072964/MDA2_REP2_20250713191956.raw"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["montimar@unina.it"],"submitter":["ilaria iacobucci"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Breast Cancer"],"software":[""],"submitter_keywords":["Tel46","Quantitative proteomics","Biomarkes","Dna","Breast","Tnbc","Gquadruplex","Cancer"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072964"],"tissue":["Breast"],"sample_protocol":["Three independent pellets from BT-549 and MDA-MB-231 were processed in parallel with MCF10a as a non-tumorigenic control (n = 3 per cell line). Pellets were lysed in 5% SDS + 50 mM ammonium bicarbonate, then total proteins were trypsin-digested on S-Trap cartridges (Protifi) following the manufacturer’s protocol. Peptides were resuspended in 0.2% formic acid and analysed by LC–MS/MS on an Orbitrap Exploris 240 coupled to a Vanquish Neo nanoUPLC (Nanospray Flex source). Peptide separation was performed on a C18 capillary RP column (150 mm × 75 µm, 2 µm, 100 Å) at 250 nL/min using a 2–90% gradient of solvent B (0.2% FA in 95% ACN) in solvent A (0.2% FA, 2% ACN in water) over 88 min. MS acquisition was in DIA mode with a 2–90% gradient in 72 min, a full-scan range of m/z 400–900, and a 12 m/z isolation window. LC–MS/MS runs were performed in triplicate."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Proteins were identified using DIA-NN software (v2.1.0) with Homo sapiens UniProt database as reference. Default output filtering was applied at 1% FDR at both precursor and protein group levels. Peptides with length <7 or >30 amino acids were excluded. Peptides with charge states 2–4 were retained, and a maximum of 1 missed cleavage was allowed in the in silico trypsin digest (cut at K/R). Cysteine carbamidomethylation was designated as a fixed modification, and methionine oxidation (UniMod:35, Δ15.9949 Da) was considered as a variable modification. Peptides tagged with sRAP were excluded from normalization and protein quantification. Mass accuracy was set to 10 ppm for both MS1 and MS2. Furthermore, the output was filtered to include only proteins that had been identified with a minimum of three peptides and at least one unique peptide."],"omics_type":["Proteomics"],"labhead":["Maria Monti"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Università degli studi di Napoli Federico II - Dipartimento di Chimica"],"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 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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