ArticleMolecular and cellular biochemistry2017
Identification of an RNA aptamer binding hTERT-derived peptide and inhibiting telomerase activity in MCF7 cells.
Article in Molecular and cellular biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- In-cell NMR spectra of chemically unmodified RNA at physiological temperature with extended lifetime through RNase inhibitor cocktail in living human cells.Scientific reports · 2025Article
- Review of Advances in Coating and Functionalization of Gold Nanoparticles: From Theory to Biomedical Application.Pharmaceutics · 2024Review
- Advances in Aptamers-Based Applications in Breast Cancer: Drug Delivery, Therapeutics, and Diagnostics.International journal of molecular sciences · 2022Review
- Engineered CRISPR/Cas13d Sensing hTERT Selectively Inhibits the Progression of Bladder CancerFrontiers in molecular biosciences · 2021Article
- Programmable Synthetic Protein Circuits for the Identification and Suppression of Hepatocellular Carcinoma.Molecular therapy oncolytics · 2020Article
- Centrality of telomerase in cellular life.The Indian journal of medical research · 2019Article
- Aptamers in HIV research diagnosis and therapy.RNA biology · 2018Review
- Aptamer selection and applications for breast cancer diagnostics and therapy.Journal of nanobiotechnology · 2017Review
- Activation of p53 Gene Expression and Synergistic Antiproliferative Effects of 5-Fluorouracil and β-escin on MCF7 Cells.Journal of medical signals and sensorsArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human telomerase reverse transcriptase is an essential rate-limiting component of telomerase complex. hTERT protein in association with other proteins and the human telomerase RNA (hTR) shows telomerase activity, essential for maintaining genomic integrity in proliferating cells. hTERT binds hTR through a decapeptide located in the RID2 (RNA interactive domain 2) domain of N-terminal region. Since hTERT is essential for telomerase activity, inhibitors of hTERT are of great interest as potential anti-cancer agent. We have selected RNA aptamers against a synthetic peptide from the RID2 domain of hTERT by employing in vitro selection protocol (SELEX). The selected RNAs could bind the free peptide, as CD spectra suggested conformational change in aptamer upon RID2 binding. Extracts of cultured breast cancer cells (MCF7) expressing this aptamer showed lower telomerase activity as estimated by TRAP assay. hTERT-binding RNA aptamers hold promise as probable anti-cancer therapeutic agent.
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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.