Evidence map›Paper›PMID 24466140›Full record

ArticlePloS one2014

Structure of Utp21 tandem WD domain provides insight into the organization of the UTPB complex involved in ribosome synthesis.

Cheng Zhang, Jinzhong Lin, Weixiao Liu, Xining Chen, Rongchang Chen, Keqiong Ye

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
  5. Article
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  7. Article
  8. Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. The SSU processome interactome inRNA (New York, N.Y.) · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
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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

6 authors at 2 institutions in 1 country.

Cheng ZhangInstitute of Developmental Biology and Molecular Medicine, School of Life Science, Fudan University, Shanghai, China ; National Institute of Biological Sciences, Beijing, Beijing, China.
Jinzhong LinNational Institute of Biological Sciences, Beijing, Beijing, China.
Weixiao LiuNational Institute of Biological Sciences, Beijing, Beijing, China.
Xining ChenNational Institute of Biological Sciences, Beijing, Beijing, China.
Rongchang ChenNational Institute of Biological Sciences, Beijing, Beijing, China.
Keqiong YeNational Institute of Biological Sciences, Beijing, Beijing, China.
National Institute of Biological Sciences, Beijing · CNFudan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Assembly of the eukaryotic ribosome requires a large number of trans-acting proteins and small nucleolar RNAs that transiently associate with the precursor rRNA to facilitate its modification, processing and binding with ribosomal proteins. UTPB is a large evolutionarily conserved complex in the 90S small subunit processome that mediates early processing of 18S rRNA. UTPB consists of six proteins Utp1/Pwp1, Utp6, Utp12/Dip2, Utp13, Utp18 and Utp21 and has abundant WD domains. Here, we determined the crystal structure of the tandem WD domain of yeast Utp21 at 2.1 Å resolution, revealing two open-clamshell-shaped β-propellers. The bottom faces of both WD domains harbor several conserved patches that potentially function as molecular binding sites. We show that residues 100-190 of Utp18 bind to the tandem WD domain of Utp21. Structural mapping of previous crosslinking data shows that the WD domains of Utp18 and Utp1 are organized on two opposite sides of the Utp21 WD domains. This study reports the first structure of a UTPB component and provides insight into the structural organization of the UTPB complex.

Indexed as

Amino Acid SequenceBinding SitesCrystallography, X-RayMolecular Sequence DataNuclear ProteinsProtein BindingProtein Structure, TertiaryRibosomal ProteinsRibosomesRNA, RibosomalRNA, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentYeastsNuclear ProteinsRibosomal ProteinsRNA, RibosomalRNA, Small NucleolarSaccharomyces cerevisiae ProteinsUtp21 protein, S cerevisiae

Identifiers

PMID24466140
PMCPMC3897721
OpenAlexW1979540748

What OpenQuestion holds

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LicenceCC BY
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.