Journal
METHODS
Volume 114, Issue -, Pages 85-95Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2016.08.002
Keywords
Telomerase; Activity assay; Immunopurification; DNA affinity
Funding
- Cancer Council NSW [RG12-02]
- Cancer Institute NSW Career Development and Support Fellowship [11/CDF/3-05]
- Priority Driven Young Investigator grant - Cancer Australia
- Cure Cancer Australia Foundation
- Perpetual Trusts (Australia)
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Telomerase is the ribonucleoprotein enzyme that catalyzes the processive addition of the telomeric DNA repeat 5'-TTAGGG-3' onto chromosome ends. In addition to its fascinating biochemical and enzymatic properties, clinical interest in telomerase stems from its dysregulated expression in similar to 90% of human cancers, representing a broad spectrum of diseases. Exploiting telomerase as a therapeutic target and hence identifying and/or evaluating potential inhibitors requires quantitative measurement of its activity. This article presents procedures for measuring multiple aspects of telomerase enzymology that are relevant to both fundamental biochemistry and drug discovery: direct activity assays, DNA binding affinity, DNA dissociation, and cell-based over-expression of the active enzyme complex. (C) 2016 Elsevier Inc. All rights reserved.
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