Evidence map›Paper›PMID 21051362›Full record

ArticleNucleic acids research2011

Direct involvement of the TEN domain at the active site of human telomerase.

Julie Jurczyluk, Amanda S Nouwens, Jessica K Holien, Timothy E Adams, George O Lovrecz, Michael W Parker, Scott B Cohen, Tracy M Bryan

Abstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed.

  1. Article
  2. Article
  3. Telomerase structural biology comes of age.Current opinion in structural biology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Structural Biology of Telomerase.Cold Spring Harbor perspectives in biology · 2019
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Single-Molecule Studies of Telomeres and Telomerase.Annual review of biophysics · 2017
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Julie JurczylukChildren's Medical Research Institute, Westmead, NSW 2145, Australia.
Amanda S Nouwens
Jessica K Holien
Timothy E Adams
George O Lovrecz
Michael W Parker
Scott B Cohen
Tracy M Bryan

Funding

Wellcome Trust GR066727MA
6 · The paper itself

Abstract

Telomerase is a ribonucleoprotein that adds DNA to the ends of chromosomes. The catalytic protein subunit of telomerase (TERT) contains an N-terminal domain (TEN) that is important for activity and processivity. Here we describe a mutation in the TEN domain of human TERT that results in a greatly increased primer K(d), supporting a role for the TEN domain in DNA affinity. Measurement of enzyme kinetic parameters has revealed that this mutant enzyme is also defective in dNTP polymerization, particularly while copying position 51 of the RNA template. The catalytic defect is independent of the presence of binding interactions at the 5'-region of the DNA primer, and is not a defect in translocation rate. These data suggest that the TEN domain is involved in conformational changes required to position the 3'-end of the primer in the active site during nucleotide addition, a function which is distinct from the role of the TEN domain in providing DNA binding affinity.

Indexed as

Catalytic DomainCell LineDNADNA PrimersHumansModels, MolecularMutationNucleotidesProtein Structure, TertiaryTelomeraseTemplates, GeneticDNADNA PrimersNucleotidesTelomeraseTERT protein, human

Identifiers

PMID21051362
PMCPMC3061064

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.