Evidence map›Paper›PMID 12730131›Full record

ArticleGenes & development2003

A role for a novel 'trans-pseudoknot' RNA-RNA interaction in the functional dimerization of human telomerase.

Hinh Ly, Lifeng Xu, Melissa A Rivera, Tristram G Parslow, Elizabeth H Blackburn

Abstract read
In one paragraph

Article in Genes & development, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Ribonucleoprotein multimers and their functions.Critical reviews in biochemistry and molecular biology · 2010
    Review
  5. RNA conformation in catalytically active human telomerase.Journal of the American Chemical Society · 2010
    Article
  6. Article
  7. Article
  8. Article
  9. Functional analysis of the pseudoknot structure in human telomerase RNA.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Telomeres and telomerase.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004
    Review
  16. Tetrahymena telomerase is active as a monomer.Molecular biology of the cell · 2003
    Article
  17. Article
  18. Article
  19. 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

5 authors.

Hinh LyDepartments of Pathology Microbiology, and Immunology, and Department of Biochemistry and Biophysics, University of California, San Francisco, California 94143, USA.
Lifeng Xu
Melissa A Rivera
Tristram G Parslow
Elizabeth H Blackburn

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

The integral RNA (hTER) of the human telomerase ribonucleoprotein has a conserved secondary structure that contains a potential pseudoknot. Here we examine the role of an intermolecular hTER-hTER interaction in the previously reported functional dimerization of telomerase. We provide evidence that the two conserved, complementary sequences of one stem of the hTER pseudoknot domain can pair intermolecularly in vitro, and that formation of this stem as part of a novel "trans-pseudoknot" is required for telomerase to be active in its dimeric form. Such RNA-RNA interaction mirrors a known property of retroviral reverse transcriptases, which use homodimeric viral genomic RNA substrates.

Indexed as

DimerizationHumansMutationRNATelomeraseRNATelomerase

Identifiers

PMID12730131
PMCPMC196051

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.