The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Reevaluation of telomerase inhibition by quadruplex ligands and their mechanisms of action
Open accessAbstract
Quadruplex ligands are often considered as telomerase inhibitors. Given the fact that some of these molecules are present in the clinical setting, it is important to establish the validity of this assertion. To analyze the effects of these compounds, we used a direct assay with telomerase-enriched extracts. The comparison of potent ligands from various chemical families revealed important differences in terms of effects on telomerase initiation and processivity. Although most quadruplex ligands may lock a quadruplex-prone sequence into a quadruplex structure that inhibits the initiation of elongation by telomerase, the analysis of telomerase-elongation steps revealed that only a few molecules interfered with the processivity of telomerase (i.e., inhibit elongation once one or more repeats have been incorporated). The demonstration that these molecules are actually more effective inhibitors of telomeric DNA amplification than extension by telomerase contributes to the already growing suspicion that quadruplex ligands are not simple telomerase inhibitors but, rather, constitute a different class of biologically active molecules. We also demonstrate that the popular telomeric repeat amplification protocol is completely inappropriate for the determination of telomerase inhibition by quadruplex ligands, even when PCR controls are included. As a consequence, the inhibitory effect of many quadruplex ligands has been overestimated.
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Cites
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Quadruplex DNA: sequence, topology and structure
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Inhibition of telomerase by G-quartet DMA structures
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Inhibition of Human Telomerase by a G-Quadruplex-Interactive Compound
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The POT1-TPP1 telomere complex is a telomerase processivity factor.
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Targeting telomeres and telomerase
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Self-citationTelomestatin, a Novel Telomerase Inhibitor from Streptomyces anulatus
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Cited by
DNA secondary structures: stability and function of G-quadruplex structures
Bochman, M. L., Paeschke, K., & Zakian, V. A. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3296 · Cited by 1,446
G-quadruplex structures: in vivo evidence and function
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A hitchhiker's guide to G-quadruplex ligands
Monchaud, D., & Teulade-Fichou, M.-P. (2008) · Org. Biomol. Chem. · doi:10.1039/b714772b · Cited by 788
Self-citation1,10-Phenanthroline: A versatile building block for the construction of ligands for various purposes
Bencini, A., & Lippolis, V. (2010) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2010.04.008 · Cited by 615
Rodriguez, R., Müller, S., Yeoman, J. A., Trentesaux, C., Riou, J.-F., & Balasubramanian, S. (2008) · Journal of the American Chemical Society · doi:10.1021/ja805615w · Cited by 517
Metadata
- Authors
- De Cian, A., Cristofari, G., Reichenbach, P., De Lemos, E., Monchaud, D., Teulade-Fichou, M.-P., Shin-ya, K., Lacroix, L., Lingner, J., & Mergny, J.-L.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2007-10-30
- Volume
- 104
- Issue
- 44
- Pages
- 17347-17352
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1980382899
- Cited by
- 292
- References
- 28
- FWCI
- 13.65
- Type
- journal article
- Language
- en
- Open access
- green
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- De Cian, A., Cristofari, G., Reichenbach, P., De Lemos, E., Monchaud, D., Teulade-Fichou, M.-P., Shin-ya, K., Lacroix, L., Lingner, J., & Mergny, J.-L. (2007). Reevaluation of telomerase inhibition by quadruplex ligands and their mechanisms of action. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0707365104
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