ArticleeLife2014
Identification of human TERT elements necessary for telomerase recruitment to telomeres.
Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
67 citing papers in PubMed.
- Human RPA is an essential telomerase processivity factor for maintaining telomeres.Science (New York, N.Y.) · 2025Article
- TERT translocation to mitochondria: Exploring its role in mitochondrial homeostasis.PLoS genetics · 2025Article
- TRF1 and TRF2 form distinct shelterin subcomplexes at telomeres.Cell reports · 2025Article
- Discovery and characterization of a novel telomerase alternative splicing isoform that protects lung cancer cells from chemotherapy induced cell death.Scientific reports · 2025Article
- 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
- Recent progress in human telomerase structure and its therapeutic targeting.Frontiers in molecular biosciences · 2025Review
- Clinical mutations in the TERT and TERC genes coding for telomerase components induced oxidative stress, DNA damage at telomeres and cell apoptosis besides decreased telomerase activity.Human molecular genetics · 2024Article
- Telomere maintenance and the DNA damage response: a paradoxical alliance.Frontiers in cell and developmental biology · 2024Article
- Pot1b -/- tumors activate G-quadruplex-induced DNA damage to promote telomere hyper-elongation.Nucleic acids research · 2023Article
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- TCAB1 prevents nucleolar accumulation of the telomerase RNA to facilitate telomerase assembly.Cell reports · 2023Article
- Interaction hub critical for telomerase recruitment and primer-template handling for catalysis.Life science alliance · 2023Article
- Exercise regulates shelterin genes and microRNAs implicated in ageing in Thoroughbred horses.Pflugers Archiv : European journal of physiology · 2022Article
- Telomerase structural biology comes of age.Current opinion in structural biology · 2022Review
- DNA and RNA Binding Proteins: From Motifs to Roles in Cancer.International journal of molecular sciences · 2022Review
- Structural basis of human telomerase recruitment by TPP1-POT1.Science (New York, N.Y.) · 2022Article
- Structural biology of human telomerase: progress and prospects.Biochemical Society transactions · 2021Review
- Arabidopsis retains vertebrate-type telomerase accessory proteins via a plant-specific assembly.Nucleic acids research · 2021Article
- 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
- TPP1 mutagenesis screens unravel shelterin interfaces and functions in hematopoiesis.JCI insight · 2021Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
Human chromosomes terminate in telomeres, repetitive DNA sequences bound by the shelterin complex. Shelterin protects chromosome ends, prevents recognition by the DNA damage machinery, and recruits telomerase. A patch of amino acids, termed the TEL-patch, on the OB-fold domain of the shelterin component TPP1 is essential to recruit telomerase to telomeres. In contrast, the site on telomerase that interacts with the TPP1 OB-fold is not well defined. In this study, we identify separation-of-function mutations in the TEN-domain of human telomerase reverse transcriptase (hTERT) that disrupt the interaction of telomerase with TPP1 in vivo and in vitro but have very little effect on the catalytic activity of telomerase. Suppression of a TEN-domain mutation with a compensatory charge-swap mutation in the TEL-patch indicates that their association is direct. Our findings define the interaction interface required for telomerase recruitment to telomeres, an important step towards developing modulators of this interaction as therapeutics for human disease.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.