ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structure of Est3 reveals a bimodal surface with differential roles in telomere replication.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 42 citations in OpenAlex.
- Fission yeast RPA-TERT-Tpz1TPP1 complex promotes telomere extension and suppresses telomere recombination.PLoS genetics · 2026Article
- Fission yeast RPA-TERT-Tpz1bioRxiv : the preprint server for biology · 2026Article
- Cryo-electron microscopy structure of the budding yeast telomerase holoenzyme.Science (New York, N.Y.) · 2026Article
- The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- Interaction hub critical for telomerase recruitment and primer-template handling for catalysis.Life science alliance · 2023Article
- Telomerase structural biology comes of age.Current opinion in structural biology · 2022Review
- The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Cutinase Bdo_10846 Play an Important Role in the Virulence ofInternational journal of molecular sciences · 2021Article
- Insights into the structure and function of Est3 from the Hansenula polymorpha telomerase.Scientific reports · 2020Article
- Fine tuning the level of the Cdc13 telomere-capping protein for maximal chromosome stability performance.Current genetics · 2019Review
- Order in Disorder as Observed by the "Hydrophobic Cluster Analysis" of Protein Sequences.Proteomics · 2018Review
- Direct observation of nucleic acid binding dynamics by the telomerase essential N-terminal domain.Nucleic acids research · 2018Article
- The N Terminus of the OB Domain of Telomere Protein TPP1 Is Critical for Telomerase Action.Cell reports · 2018Article
- Using Separation-of-Function Mutagenesis To Define the Full Spectrum of Activities Performed by the Est1 Telomerase SubunitGenetics · 2018Article
- Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017Review
- Recombinant expression and purification of the RNA-binding LARP6 proteins from fish genetic model organisms.Protein expression and purification · 2017Article
- Fundamental mechanisms of telomerase action in yeasts and mammals: understanding telomeres and telomerase in cancer cells.Open biology · 2017Review
- Dynamic peptides of human TPP1 fulfill diverse functions in telomere maintenance.Nucleic acids research · 2016Article
- Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use.Nucleic acids research · 2016Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Telomerase is essential for continuous cellular proliferation. Substantial insights have come from studies of budding yeast telomerase, which consists of a catalytic core in association with two regulatory proteins, ever shorter telomeres 1 and 3 (Est1 and Est3). We report here a high-resolution structure of the Est3 telomerase subunit determined using a recently developed strategy that combines minimal NMR experimental data with Rosetta de novo structure prediction algorithms. Est3 adopts an overall protein fold which is structurally similar to that adopted by the shelterin component TPP1. However, the characteristics of the surface of the experimentally determined Est3 structure are substantially different from those predicted by prior homology-based models of Est3. Structure-guided mutagenesis of the complete surface of the Est3 protein reveals two adjacent patches on a noncanonical face of the protein that differentially mediate telomere function. Mapping these two patches on the Est3 structure defines a set of shared features between Est3 and HsTPP1, suggesting an analogous multifunctional surface on TPP1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.