High-throughput mass spectrometry and bioinformatics analysis of breast cancer proteomic data.

{"sci_version": "1.2", "schema": "https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json", "id": "pmid:31294064", "kind": "science-record", "revision": 2, "content_hash": "sha256:979447ddf4e3ec233005319f7f9c520d1255284ea475ad7e652ce8c29c01e2fc", "created_at": "2026-11-01T15:40:47Z", "updated_at": "2026-11-01T18:51:02Z", "generator": {"name": "corpus-assay-engine", "run_id": "reading-sci-2026-11-01"}, "paper": {"state": "complete", "title": "High-throughput mass spectrometry and bioinformatics analysis of breast cancer proteomic data.", "doi": "10.1016/j.dib.2019.104125", "pmid": "31294064", "authors": ["Talita Helen Bombardelli Gomig", "Iglenir João Cavalli", "Ricardo Lehtonen Rodrigues de Souza", "Aline Castro Rodrigues Lucena", "Michel Batista", "Kelly Cavalcanti Machado", "Fabricio Klerynton Marchini", "Fabio Albuquerque Marchi", "Rubens Silveira Lima", "Cícero de Andrade Urban", "Luciane Regina Cavalli", "Enilze Maria de Souza Fonseca Ribeiro"], "journal": "Data in brief", "year": 2019, "abstract": "Data present here describe a comparative proteomic analysis among the malignant [primary breast tumor (PT) and axillary metastatic lymph nodes (LN)], and the non-tumor [contralateral (NCT) and adjacent (ANT)] breast tissues. Protein identification and quantification were performed through label-free mass spectrometry using a nano-liquid chromatography coupled to an electrospray ionization-mass spectrometry (nLC-ESI-MS/MS). The mass spectrometry proteomic data have been deposited to the ProteomeXchange Consortium via PRIDE partner repository with the dataset identifier PXD012431. A total of 462 differentially expressed proteins was identified among these tissues and was analyzed in six groups' comparisons (named NCTxANT, PTxNCT, PTxANT, LNxNCT, LNxANT and PTxLN). Proteins at 1.5 log2 fold change were submitted to the Ingenuity® Pathway Analysis (IPA) software version 2.3 (QIAGEN Inc.) to identify biological pathways, disease and function annotation, and interaction networks related to cancer biology. The detailed data present here provides information about the proteome alterations and their role on breast tumorigenesis. This information can lead to novel biological insights on cancer research. For further interpretation of these data, please see our research article 'Quantitative label-free mass spectrometry using contralateral and adjacent breast tissues reveal differentially expressed proteins and their predicted impacts on pathways and cellular functions in breast cancer' [2].", "claims": [{"id": "claim-data-access", "statement": "The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD012431. IPA's analyses are in this article.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:31294064", "locator": "sections[1] \"table-wrap\" paragraph 1", "quote": "The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifier PXD012431. 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