ArticleNucleic acids research2015
The telomerase essential N-terminal domain promotes DNA synthesis by stabilizing short RNA-DNA hybrids.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 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
31 citing papers in PubMed, 41 citations in OpenAlex.
- The Missing Piece: Functional Telomerase Restored in the Beetle Model.Genome biology and evolution · 2026Article
- Structures of nucleotide-bound human telomerase at several steps of its telomeric DNA repeat addition cycle.Nature communications · 2026Article
- Functional Classification of Fusion Proteins in Sarcoma.Cancers · 2024Review
- Conformational plasticity and allosteric communication networks explain Shelterin protein TPP1 binding to human telomerase.Communications chemistry · 2023Article
- Orchestrating nucleic acid-protein interactions at chromosome ends: telomerase mechanisms come into focus.Nature structural & molecular biology · 2023Review
- Telomerase structural biology comes of age.Current opinion in structural biology · 2022Review
- Structural basis of human telomerase recruitment by TPP1-POT1.Science (New York, N.Y.) · 2022Article
- Zipper head mechanism of telomere synthesis by human telomerase.Cell research · 2021Article
- A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Composition and Function of Telomerase-A Polymerase Associated with the Origin of Eukaryotes.Biomolecules · 2020Review
- Observation of processive telomerase catalysis using high-resolution optical tweezers.Nature chemical biology · 2020Article
- Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019Review
- Single-Molecule Analysis of Reverse Transcriptase Enzymes.Cold Spring Harbor perspectives in biology · 2019Review
- Structure of Telomerase with Telomeric DNA.Cell · 2018Article
- Direct observation of nucleic acid binding dynamics by the telomerase essential N-terminal domain.Nucleic acids research · 2018Article
- A single nucleotide incorporation step limits human telomerase repeat addition activity.The EMBO journal · 2018Article
- New perspectives on telomerase RNA structure and function.Wiley interdisciplinary reviews. RNA · 2018Review
- Structure and function of the N-terminal domain of the yeast telomerase reverse transcriptase.Nucleic acids research · 2018Article
- Structural biology of telomerase and its interaction at telomeres.Current opinion in structural biology · 2017Review
- DNA-binding determinants and cellular thresholds for human telomerase repeat addition processivity.The EMBO journal · 2017Article
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 at 1 institution in 1 country.
Funding
Abstract
Telomerase is an enzyme that adds repetitive DNA sequences to the ends of chromosomes and consists of two main subunits: the telomerase reverse transcriptase (TERT) protein and an associated telomerase RNA (TER). The telomerase essential N-terminal (TEN) domain is a conserved region of TERT proposed to mediate DNA substrate interactions. Here, we have employed single molecule telomerase binding assays to investigate the function of the TEN domain. Our results reveal telomeric DNA substrates bound to telomerase exhibit a dynamic equilibrium between two states: a docked conformation and an alternative conformation. The relative stabilities of the docked and alternative states correlate with the number of basepairs that can be formed between the DNA substrate and the RNA template, with more basepairing favoring the docked state. The docked state is further buttressed by the TEN domain and mutations within the TEN domain substantially alter the DNA substrate structural equilibrium. We propose a model in which the TEN domain stabilizes short RNA-DNA duplexes in the active site of the enzyme, promoting the docked state to augment telomerase processivity.
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.