Evidence map›Paper›PMID 22960705›Full record

ReviewBioarchitecture

Structural biology of the PCI-protein fold.

Andrew M Ellisdon, Murray Stewart

Open access · bronzeAbstract readReview
In one paragraph

Review in Bioarchitecture. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

29 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. PCID2 Subunit of theCurrent issues in molecular biology · 2023
    Article
  6. Article
  7. Article
  8. PCID2, a subunit of theRNA biology · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Proteasome Structure and Assembly.Journal of molecular biology · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

2 authors at 2 institutions in 2 countries.

Andrew M EllisdonDepartment of Biochemistry and Molecular Biology; Monash University; Clayton, Victoria, Australia.
Murray StewartMRC Laboratory of Molecular Biology; Cambridge, UK.
Monash University · AUMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105178939Medical Research Council U105178939Wellcome Trust
6 · The paper itself

Abstract

The PCI fold is based on a stack of α-helices topped with a winged-helix domain and is found in a range of proteins that form central parts of large complexes such as the proteasome lid, the COP9 signalosome, elongation factor eIF3, and the TREX-2 complex. Recent structural determinations have given intriguing insight into how these folds function both to facilitate the generation of larger proteinaceous assembles and also to interact functionally with nucleic acids.

Indexed as

Protein FoldingHumansModels, MolecularNucleic AcidsProteasome Endopeptidase ComplexProtein C InhibitorProtein Structure, SecondarySaccharomyces cerevisiae ProteinsNucleic AcidsProteasome Endopeptidase ComplexProtein C InhibitorSaccharomyces cerevisiae ProteinsSEM1 protein, S cerevisiaeCOP9 complexeIF3PCI foldPCI proteinproteasomeTREX-2 complex

Identifiers

PMID22960705
PMCPMC3675071
OpenAlexW2084820754

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.