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- W2024181718 startingPage "115" @default.
- W2024181718 abstract "Telomerase is the ribonucleoprotein (RNP) reverse transcriptase responsible for synthesizing the 3' ends of linear chromosomes. It plays critical roles in tumorigenesis, cellular aging, and stem cell renewal. The past two years have seen exciting progress in determining telomerase holoenzyme architecture and the structural basis of telomerase activity. Notably, the first electron microscopy structures of telomerase were reported, of the Tetrahymena thermophila telomerase holoenzyme and a human telomerase dimer. In addition to new structures of TERT and TER domains, the first structures of telomerase protein domains beyond TERT, and their complexes with TER or telomeric single-stranded DNA, were reported. Together these studies provide the first glimpse into the organization of the proteins and RNA in the telomerase RNP." @default.
- W2024181718 created "2016-06-24" @default.
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- W2024181718 date "2014-02-01" @default.
- W2024181718 modified "2023-09-23" @default.
- W2024181718 title "Progress in structural studies of telomerase" @default.
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- W2024181718 doi "https://doi.org/10.1016/j.sbi.2014.01.008" @default.
- W2024181718 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3984607" @default.
- W2024181718 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24508601" @default.
- W2024181718 hasPublicationYear "2014" @default.
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