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- W2328486584 abstract "IN A MAJOR ADVANCE toward understanding a key biomolecule, scientists have solved the structure of the catalytic subunit of telomerase, the enzyme that maintains the length and integrity of telomeres, the DNA sequences at the ends of chromosomes. Telomerase activity usually declines as a natural part of aging, limiting cell division, but it reactivates in cancer, allowing cancer cells to continue dividing. Elizabeth Blackburn, a biochemistry professor at the University of California, San Francisco, and one of the codiscoverers of telomerase, says, “The new structure of the protein portion of the ribonucleoprotein enzyme telomerase is an important step along the way to the ultimate understanding of this enzyme and its potential exploitation for medical purposes.” Telomerase is a potential drug target for treating cancer and some other diseases, and for mitigating effects of aging. Telomerase consists of a catalytic protein subunit (telomerase reverse transcriptase, or TERT) and an RNA component that provid..." @default.
- W2328486584 created "2016-06-24" @default.
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- W2328486584 date "2008-09-08" @default.
- W2328486584 modified "2023-09-26" @default.
- W2328486584 title "TELOMERASE COMPONENT’S STRUCTURE SOLVED" @default.
- W2328486584 doi "https://doi.org/10.1021/cen-v086n036.p007" @default.
- W2328486584 hasPublicationYear "2008" @default.
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