ArticlePloS one2015
Characterization of the MUC1-C Cytoplasmic Domain as a Cancer Target.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
51 citing papers in PubMed, 66 citations in OpenAlex.
- M1C is a druggable target for NSCLC KRAS G12C mutant tumors resistant to KRAS inhibitors.Oncogene · 2026Article
- M1C IS NECESSARY FOR DARAXONRASIB RESISTANCE OF NSCLC KRAS(G12C) MUTANT CELLS.bioRxiv : the preprint server for biology · 2026Article
- Evolution of the MUC1 gene in eutherian mammals as an adaptation responsible for the increasing incidence of cancer in humans.Biochimica et biophysica acta. Reviews on cancer · 2026Review
- Activation of APOBEC3 cytidine deaminases and endogenous retroviruses is integrated by MUC1-C in NSCLC cells.Cell death discovery · 2025Article
- Transmembrane mucins in lung adenocarcinoma: understanding of current molecular mechanisms and clinical applications.Cell death discovery · 2025Review
- The multifaceted roles of mucins family in lung cancer: from prognostic biomarkers to promising targets.Frontiers in immunology · 2025Review
- The Role of MUC1 in Renal Cell Carcinoma.Biomolecules · 2024Review
- Cardamonin anticancer effects through the modulation of the tumor immune microenvironment in triple-negative breast cancer cells.American journal of cancer research · 2024Article
- MUC1-C is a master regulator of MICA/B NKG2D ligand and exosome secretion in human cancer cells.Journal for immunotherapy of cancer · 2023Article
- Irradiation Alters the Expression of MUC1, CD44 and Hyaluronan in Oral Mucosal Epithelium.Biomedicines · 2022Article
- Dependence on the MUC1-C Oncoprotein in Classic, Variant, and Non-neuroendocrine Small Cell Lung Cancer.Molecular cancer research : MCR · 2022Article
- Addiction of Cancer Stem Cells to MUC1-C in Triple-Negative Breast Cancer Progression.International journal of molecular sciences · 2022Review
- MUC1 is a potential target to overcome trastuzumab resistance in breast cancer therapy.Cancer cell international · 2022Review
- MUC1-C dictates neuroendocrine lineage specification in pancreatic ductal adenocarcinomas.Carcinogenesis · 2022Article
- Comparison of mucin-1 in human breast cancer and canine mammary gland tumor: a review study.Cancer cell international · 2022Review
- Novel insights into the roles and therapeutic implications of MUC1 oncoprotein via regulating proteins and non-coding RNAs in cancer.Theranostics · 2022Review
- Mucin1 and Mucin16: Therapeutic Targets for Cancer Therapy.Pharmaceuticals (Basel, Switzerland) · 2021Review
- MUC1 is an oncoprotein with a significant role in apoptosis (Review).International journal of oncology · 2021Review
- Mucins as anti-cancer targets: perspectives of the glycobiologist.Glycoconjugate journal · 2021Review
- MUC1-C Activates the BAF (mSWI/SNF) Complex in Prostate Cancer Stem Cells.Cancer research · 2021Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
Mucin 1 (MUC1) is a heterodimeric protein that is aberrantly expressed in diverse human carcinomas and certain hematologic malignancies. The oncogenic MUC1 transmembrane C-terminal subunit (MUC1-C) functions in part by transducing growth and survival signals from cell surface receptors. However, little is known about the structure of the MUC1-C cytoplasmic domain as a potential drug target. Using methods for structural predictions, our results indicate that a highly conserved CQCRRK sequence, which is adjacent to the cell membrane, forms a small pocket that exposes the two cysteine residues for forming disulfide bonds. By contrast, the remainder of the MUC1-C cytoplasmic domain has no apparent structure, consistent with an intrinsically disordered protein. Our studies thus focused on targeting the MUC1 CQCRRK region. The results show that L- and D-amino acid CQCRRK-containing peptides bind directly to the CQC motif. We further show that the D-amino acid peptide, designated GO-203, blocks homodimerization of the MUC1-C cytoplasmic domain in vitro and in transfected cells. Moreover, GO-203 binds directly to endogenous MUC1-C in breast and lung cancer cells. Colocalization studies further demonstrate that GO-203 predominantly binds to MUC1-C at the cell membrane. These findings support the further development of agents that target the MUC1-C cytoplasmic domain CQC motif and thereby MUC1-C function in cancer cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.