Evidence map›Paper›PMID 10893261›Full record

ArticleThe Journal of cell biology2000

The regulatory complex of Drosophila melanogaster 26S proteasomes. Subunit composition and localization of a deubiquitylating enzyme.

H Hölzl, B Kapelari, J Kellermann, E Seemüller, M Sümegi, A Udvardy, O Medalia, J Sperling, S A Müller, A Engel and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

51 citing papers in PubMed, 147 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Molecular Regulation of the Polycomb Repressive-Deubiquitinase.International journal of molecular sciences · 2020
    Review
  8. Review
  9. Review
  10. Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

11 authors at 4 institutions in 4 countries.

H HölzlMax-Planck-Institute of Biochemistry, D-82152 Martinsried, Germany.
B Kapelari
J Kellermann
E Seemüller
M Sümegi
A Udvardy
O Medalia
J Sperling
S A Müller
A Engel
W Baumeister
Max Planck Institute of Biochemistry · DEHungarian Academy of Sciences · HUUniversity of Basel · CHWeizmann Institute of Science · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Drosophila melanogaster embryos are a source for homogeneous and stable 26S proteasomes suitable for structural studies. For biochemical characterization, purified 26S proteasomes were resolved by two-dimensional (2D) gel electrophoresis and subunits composing the regulatory complex (RC) were identified by amino acid sequencing and immunoblotting, before corresponding cDNAs were sequenced. 17 subunits from Drosophila RCs were found to have homologues in the yeast and human RCs. An additional subunit, p37A, not yet described in RCs of other organisms, is a member of the ubiquitin COOH-terminal hydrolase family (UCH). Analysis of EM images of 26S proteasomes-UCH-inhibitor complexes allowed for the first time to localize one of the RC's specific functions, deubiquitylating activity. The masses of 26S proteasomes with either one or two attached RCs were determined by scanning transmission EM (STEM), yielding a mass of 894 kD for a single RC. This value is in good agreement with the summed masses of the 18 identified RC subunits (932 kD), indicating that the number of subunits is complete.

Indexed as

Proteasome Endopeptidase ComplexAnimalsDrosophila melanogasterElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelEmbryo, NonmammalianMacromolecular SubstancesMicroscopy, Electron, Scanning TransmissionModels, MolecularMolecular Sequence DataMolecular WeightPeptide HydrolasesProtein Structure, TertiarySequence Analysis, DNASequence Analysis, ProteinSequence Homology, Amino AcidATP dependent 26S proteaseMacromolecular SubstancesPeptide HydrolasesProteasome Endopeptidase ComplexThiolester HydrolasesUbiquitinsUbiquitin Thiolesterase

Identifiers

PMID10893261
PMCPMC2185576
OpenAlexW2160128169

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.