ArticleNucleic acids research2015
Identification of human telomerase assembly inhibitors enabled by a novel method to produce hTERT.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- High-Throughput Screening Tool to Identify Small Molecule Inhibitors of Telomerase.ACS chemical biology · 2025Article
- Telomeres and telomerase in Sarcoma disease and therapy.International journal of medical sciences · 2024Review
- Telomerase as a therapeutic target in glioblastoma.Neuro-oncology · 2021Review
- How RNAi machinery enters the world of telomerase.Cell cycle (Georgetown, Tex.) · 2019Review
- AGO2 promotes telomerase activity and interaction between the telomerase components TERT and TERC.EMBO reports · 2019Article
- Comprehensive analysis of telomerase inhibition by gallotannin.Oncotarget · 2018Article
- New prospects for targeting telomerase beyond the telomere.Nature reviews. Cancer · 2016Review
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Telomerase is the enzyme that maintains the length of telomeres. It is minimally constituted of two components: a core reverse transcriptase protein (hTERT) and an RNA (hTR). Despite its significance as an almost universal cancer target, the understanding of the structure of telomerase and the optimization of specific inhibitors have been hampered by the limited amount of enzyme available. Here, we present a breakthrough method to produce unprecedented amounts of recombinant hTERT and to reconstitute human telomerase with purified components. This system provides a decisive tool to identify regulators of the assembly of this ribonucleoprotein complex. It also enables the large-scale screening of small-molecules capable to interfere with telomerase assembly. Indeed, it has allowed us to identify a compound that inhibits telomerase activity when added prior to the assembly of the enzyme, while it has no effect on an already assembled telomerase. Therefore, the novel system presented here may accelerate the understanding of human telomerase assembly and facilitate the discovery of potent and mechanistically unique inhibitors.
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Registered trials
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