Evidence map›Paper›PMID 12972604›Full record

ArticleMolecular and cellular biology2003

Comprehensive structure-function analysis of the core domain of human telomerase RNA.

Hinh Ly, Elizabeth H Blackburn, Tristram G Parslow

Abstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing 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

39 citing papers in PubMed.

  1. Article
  2. Review
  3. A structurally conserved human andProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  4. Article
  5. New perspectives on telomerase RNA structure and function.Wiley interdisciplinary reviews. RNA · 2018
    Review
  6. Review
  7. Article
  8. Article
  9. Structural conservation in the template/pseudoknot domain of vertebrate telomerase RNA from teleost fish to human.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Pyrimidine motif triple helix in the Kluyveromyces lactis telomerase RNA pseudoknot is essential for function in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Article
  18. Review
  19. Architecture of human telomerase RNA.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

3 authors.

Hinh LyDepartment of Pathology, University of California, San Francisco, California 94143, USA.
Elizabeth H Blackburn
Tristram G Parslow

Funding

THE FUNCTION OF TELOMERASE AND TELOMERESR01GM026259 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI BLACKBURN, ELIZABETH H · 1985 to 2014
$8.9M
GAG PROTEIN/RNA INTERACTIONS IN THE HIV LIFECYCLER01AI040317 · NIAID · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI PARSLOW, TRISTRAM G. · 1996 to 2005
$1.9M
STRUCTURE BASED STUDIES OF RNA BINDING PROTEINS FROM HIVR01AI036636 · NIAID · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI PARSLOW, TRISTRAM G. · 1995 to 2005
$1.8M
UCSF AIDS RESEARCH TRAINING PROGRAMT32AI007395 · NIAID · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI LEVY, JAY A · 1990 to 2004
$743k
STRUCTURE AND FUNCTION OF TELOMERESR37GM026259 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BLACKBURN, ELIZABETH H · 1989 to 1998
–
NIAID NIH HHS AI07395NIAID NIH HHS AI36636NIAID NIH HHS AI40317NIAID NIH HHS R01 AI036636NIAID NIH HHS R01 AI040317NIAID NIH HHS T32 AI007395NIGMS NIH HHS GM26259NIGMS NIH HHS R01 GM026259NIGMS NIH HHS R37 GM026259
6 · The paper itself

Abstract

Telomerase is a cellular reverse transcriptase that uses part of its integral RNA (called TER) as the template to synthesize telomeric DNA repeats. Vertebrate TERs are thought to share a conserved, highly structured core domain that includes the templating sequence and a pseudoknot, but not all features of the predicted core structure have been verified directly or shown to affect telomerase enzymatic activity. Here, we report a systematic mutational analysis of the core domain (residues 1 to 210) of human telomerase RNA (hTER). Our data confirm that optimal hTER activity requires the integrity of four short helices (P2a.1, P2a, P2b, and P3) which create the proposed pseudoknot and that features of both the primary sequence and secondary structure in P2b and P3 contribute to optimal function. At least part of the long-range P1 pairing is also required, despite the lack of a known P1 counterpart in rodent TERs. Among the predicted single-stranded regions, we found that J2b/3, portions of J2a/3, and residues in and around the template make sequence-specific contributions to telomerase function. Additionally, we provide evidence that naturally occurring hTER sequence polymorphisms found in some patients with aplastic anemia can inhibit telomerase activity by disrupting critical structures within the hTER core domain.

Indexed as

Anemia, AplasticBase PairingBase SequenceBinding SitesCell LineConsensus SequenceHumansMutationPolymorphism, GeneticProtein Structure, TertiaryRNAStructure-Activity RelationshipTelomeraseTemplates, GeneticRNATelomerasetelomerase RNA

Identifiers

PMID12972604
PMCPMC193926

What OpenQuestion holds

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Registered trials

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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.