Evidence map›Paper›PMID 12529422›Full record

ArticleMolecular biology of the cell2003

N-terminal domain of yeast telomerase reverse transcriptase: recruitment of Est3p to the telomerase complex.

Katherine L Friedman, Jeremy J Heit, David M Long, Thomas R Cech

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.4field-weighted citation impact, top 8% of its field
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

34 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
  2. Article
  3. 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 · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Telomerase regulatory subunit Est3 in two Candida species physically interacts with the TEN domain of TERT and telomeric DNA.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Ribonucleoprotein multimers and their functions.Critical reviews in biochemistry and molecular biology · 2010
    Review
  19. Article
  20. Article
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

4 authors at 3 institutions in 1 country.

Katherine L FriedmanVanderbilt University, Department of Biological Sciences, Nashville, Tennessee 37235, USA. katherine.friedman@vanderbilt.edu
Jeremy J Heit
David M Long
Thomas R Cech
Howard Hughes Medical Institute · USMontana State University · USVanderbilt University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Telomerase is a reverse transcriptase that maintains chromosome ends. The N-terminal half of the catalytic protein subunit (TERT) contains three functional domains (I, II, and III) that are conserved among TERTs but not found in other reverse transcriptases. Guided by an amino acid sequence alignment of nine TERT proteins, mutations were introduced into yeast TERT (Est2p). In support of the proposed alignment, mutation of virtually all conserved residues resulted in loss-of-function or temperature sensitivity, accompanied by telomere shortening. Overexpression of telomerase component Est3p led to allele-specific suppression of the temperature-sensitive mutations in region I, suggesting that Est3p interacts with this protein domain. As predicted by the genetic results, a lethal mutation in region I resulted in loss of Est3p from the telomerase complex. We conclude that Est2p region I is required for the recruitment of Est3p to yeast telomerase. Given the phylogenetic conservation of region I of TERT, this protein domain may provide the equivalent function in all telomerases.

Indexed as

Fungal ProteinsAmino Acid SequenceConserved SequenceDNA-Binding ProteinsHot TemperatureMolecular Sequence DataPrecipitin TestsProteinsProtein Structure, TertiarySaccharomyces cerevisiae ProteinsSequence Analysis, ProteinTelomeraseYeastsDNA-Binding ProteinsEST1 protein, S cerevisiaeEST3 protein, S cerevisiaeFungal ProteinsProteinsSaccharomyces cerevisiae ProteinsTelomerase

Identifiers

PMID12529422
PMCPMC140223
OpenAlexW2033297272

What OpenQuestion holds

Textmetadata
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.