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Single-molecule analysis of telomerase structure and function.

Authors
Type
Published Article
Journal
Current Opinion in Chemical Biology
Publisher
Elsevier
Volume
15
Issue
6
Pages
845–852
Identifiers
DOI: 10.1016/j.cbpa.2011.10.008
Source
UCSC Aging biomedical-ucsc
License
Unknown

Abstract

The telomerase ribonucleoprotein is a specialized reverse transcriptase required to maintain protective chromosome end-capping structures called telomeres. In most cells, telomerase is not active and the natural shortening of telomeres with each round of DNA replication ultimately triggers cell growth arrest. In contrast, the presence of telomerase confers a high level of renewal capacity upon rapidly dividing cells. Telomerase is aberrantly activated in 90% of human cancers and thus represents an important target for anticancer therapeutics. However, the naturally low abundance of telomerase has hampered efforts to obtain high-resolution models for telomerase structure and function. To circumvent these challenges, single-molecule techniques have recently been employed to investigate telomerase assembly, structure, and catalysis.

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