Evidence map›Paper›PMID 10654930›Full record

ArticleThe EMBO journal2000

Crystal structure of a fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution.

H Wang, D Boisvert, K K Kim, R Kim, S H Kim

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
8.3field-weighted citation impact, top 2% 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

73 citing papers in PubMed, 164 citations in OpenAlex.

  1. Fibrillarin: bridging ribosome biogenesis and apoptosis in cellular stress and disease.Apoptosis : an international journal on programmed cell death · 2026
    Review
  2. Review
  3. Advances in the structure and function of the nucleolar protein fibrillarin.Frontiers in cell and developmental biology · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Box C/D guide RNAs recognize a maximum of 10 nt of substrates.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

13 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

H WangDepartment of Chemistry, University of California, Berkeley, CA 94720, USA.
D Boisvert
K K Kim
R Kim
S H Kim
University of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibrillarin is a phylogenetically conserved protein essential for efficient processing of pre-rRNA through its association with a class of small nucleolar RNAs during ribosomal biogenesis. The protein is the antigen for the autoimmune disease scleroderma. Here we report the crystal structure of the fibrillarin homologue from Methanococcus jannaschii, a hyperthermophile, at 1.6 A resolution. The structure consists of two domains, with a novel fold in the N-terminal region and a methyltransferase-like domain in the C-terminal region. Mapping temperature-sensitive mutations found in yeast fibrillarin Nop1 to the Methanococcus homologue structure reveals that many of the mutations cluster in the core of the methyltransferase-like domain.

Indexed as

Ribonucleoproteins, Small NucleolarSaccharomyces cerevisiae ProteinsAmino Acid SequenceAntigens, BacterialBacterial ProteinsChromosomal Proteins, Non-HistoneCrystallography, X-RayFungal ProteinsMethanococcusMethyltransferasesModels, MolecularMolecular Sequence DataMutationNuclear ProteinsProtein Structure, SecondaryProtein Structure, TertiaryAntigens, BacterialBacterial ProteinsChromosomal Proteins, Non-HistonefibrillarinFungal ProteinsMethyltransferasesNOP1 protein, S cerevisiaeNuclear ProteinsRecombinant ProteinsRibonucleoproteins, Small NucleolarSaccharomyces cerevisiae Proteins

Identifiers

PMID10654930
PMCPMC305568
OpenAlexW2031765531

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.