Evidence map›Paper›PMID 16647858›Full record

ReviewTrends in biochemical sciences2006

How a single protein complex accommodates many different H/ACA RNAs.

U Thomas Meier

Abstract readReview
In one paragraph

Review in Trends in biochemical sciences, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

  1. Review
  2. Article
  3. Exploration ofParasitology · 2024
    Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Prediction of Protein Complexes inMolecular & cellular proteomics : MCP · 2017
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

1 author.

U Thomas MeierDepartment of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA. meier@aecom.yu.edu

Funding

MOLECULAR MECHANISM OF DYSKERATOSIS CONGENITAR01HL079566 · NHLBI · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI MEIER, U THOMAS · 2004 to 2008
$2.0M
NHLBI NIH HHS R01 HL079566
6 · The paper itself

Abstract

More than 100 mammalian H/ACA RNAs form an equal number of ribonucleoproteins (RNPs) by associating with the same four core proteins. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes. Recent crystal structures of archaeal H/ACA protein complexes show how the same four proteins accommodate >100 distinct but related H/ACA RNAs and reveal that a spatial mutation cluster underlies dyskeratosis congenita, a syndrome of bone marrow failure.

Indexed as

AnimalsArchaeal ProteinsDyskeratosis CongenitaMammalsMutationProtein BindingProtein Structure, TertiaryRibonucleoproteins, Small NucleolarRibosomesRNA, Small NuclearRNA SplicingArchaeal ProteinsGAR1 protein, humanRibonucleoproteins, Small NucleolarRNA, Small Nuclear

Identifiers

PMID16647858
PMCPMC4314714

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.