ArticleAmerican journal of cancer research2023
Nuclear export signal mutation of epidermal growth factor receptor enhances malignant phenotypes of cancer cells.
Article in American journal of cancer research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 9 citations in OpenAlex.
- Repurposing Niflumic Acid-Loaded PEGylated Cerosomes for Topical Solid Ehrlich's Carcinoma Management via EGFR/ERK/miR-21 Signaling Pathway Modulation.Pharmaceutics · 2026Article
- Dynamic therapeutic response to osimertinib and immunotherapy in an EGFR L747S and L858R co-mutant NSCLC.The oncologist · 2026Article
- Nuclear-Cytoplasmic Axis in Cancer: From Protein Mislocalization to Anticancer Drug Resistance.Oncology research · 2026Review
- Clinical characteristics and treatment of EGFR exon 19 L747 mutation in advanced NSCLC: a retrospective study.BMC cancer · 2025Article
- DEPTOR suppresses lymphomagenesis by promoting EGFR degradation via HUWE1 E3 ligase.Cell death and differentiation · 2025Article
- BRAFbioRxiv : the preprint server for biology · 2025Article
- Recent Insights on the Role of Nuclear Receptors in Alzheimer's Disease: Mechanisms and Therapeutic Application.International journal of molecular sciences · 2025Review
- Sequential tyrosine kinase inhibitor therapy for EGFR L747P-mutated lung adenocarcinoma in a renal transplant recipient: a 24-month case report.Frontiers in medicine · 2025Article
- Review
- Development of triazole-based PKC-inhibitors to overcome resistance to EGFR inhibitors in EGFR-mutant lung cancers.American journal of cancer research · 2023Article
Corrections and comments
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Authors and funding
27 authors at 2 institutions in 3 countries.
Funding
Abstract
Nuclear epidermal growth factor receptor (EGFR) has been shown to be correlated with drug resistance and a poor prognosis in patients with cancer. Previously, we have identified a tripartite nuclear localization signal (NLS) within EGFR. To comprehensively determine the functions and underlying mechanism of nuclear EGFR and its clinical implications, we aimed to explore the nuclear export signal (NES) sequence of EGFR that is responsible for interacting with the exportins. We combined in silico prediction with site-directed mutagenesis approaches and identified a putative NES motif of EGFR, which is located in amino acid residues 736-749. Mutation at leucine 747 (L747) in the EGFR NES led to increased nuclear accumulation of the protein via a less efficient release of the exportin CRM1. Interestingly, L747 with serine (L747S) and with proline (L747P) mutations were found in both tyrosine kinase inhibitor (TKI)-treated and -naïve patients with lung cancer who had acquired or de novo TKI resistance and a poor outcome. Reconstituted expression of the single NES mutant EGFR
Indexed as
Identifiers
37168336PMC10164793W4376226453What OpenQuestion holds
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.