Crossref
journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract
Telomeres are multifunctional elements that shield chromosome ends from degradation and end-to-end fusions, prevent activation of DNA damage checkpoints, and modulate the maintenance of telomeric DNA by telomerase. A major protein component of human telomeres has been identified and cloned. This factor, TRF, contains one Myb-type DNA-binding repeat and an amino-terminal acidic domain. Immunofluorescent labeling shows that TRF specifically colocalizes with telomeric DNA in human interphase cells and is located at chromosome ends during metaphase. The presence of TRF along the telomeric TTAGGG repeat array demonstrates that human telomeres form a specialized nucleoprotein complex.
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Dates
| Type | When |
|---|---|
| Created | 18 years, 10 months ago (Oct. 27, 2006, 2:19 p.m.) |
| Deposited | 1 year, 7 months ago (Jan. 12, 2024, 4:47 p.m.) |
| Indexed | 1 week, 6 days ago (Aug. 19, 2025, 6:12 a.m.) |
| Issued | 29 years, 8 months ago (Dec. 8, 1995) |
| Published | 29 years, 8 months ago (Dec. 8, 1995) |
| Published Print | 29 years, 8 months ago (Dec. 8, 1995) |
@article{Chong_1995, title={A Human Telomeric Protein}, volume={270}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.270.5242.1663}, DOI={10.1126/science.270.5242.1663}, number={5242}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Chong, Laura and van Steensel, Bas and Broccoli, Dominique and Erdjument-Bromage, Hediye and Hanish, John and Tempst, Paul and de Lange, Titia}, year={1995}, month=dec, pages={1663–1667} }