Evidence map›Paper›PMID 8670806›Full record

ArticleThe EMBO journal1996

The 'destruction box' of cyclin A allows B-type cyclins to be ubiquitinated, but not efficiently destroyed.

A Klotzbücher, E Stewart, D Harrison, T Hunt

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Histone deacetylase 3 regulates cyclin A stability.The Journal of biological chemistry · 2013
    Article
  5. A brief history of error.Nature cell biology · 2011
    Article
  6. Article
  7. Targeting proteins for degradation.Nature chemical biology · 2009
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome degradation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  13. Review
  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

4 authors at 1 institution in 1 country.

A KlotzbücherCNRS UPR 41, University de Rennes I, France.
E Stewart
D Harrison
T Hunt
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The destruction of mitotic cyclins by programmed proteolysis at the end of mitosis is an important element in cell cycle control. This proteolysis depends on a conserved motif of nine residues known as the 'destruction box', which is located 40-50 residues from the N-terminus. The sequences of the A- and B-type destruction boxes are slightly different, which might account for the differences in timing of their destruction. When the cyclin A-type destruction box was substituted for the normal one in cyclin B1 or B2, however, the resulting constructs were unexpectedly stable, although the converse substitution of B-type destruction boxes in cyclin A permitted normal degradation. We compared the ubiquitination of various cyclin constructs, and found that whereas mutation of the highly conserved residues in the destruction box strongly reduced the level of ubiquitinated intermediates, the stable destruction box 'swap' constructs did form such adducts. Thus, while ubiquitination is probably necessary for cyclin destruction, it is not sufficient. We also found that poly-ubiquitinated cyclin derivatives are still bound to p34cdc2, which is not detectably ubiquitinated itself, raising the questions of how cyclin and cdc2 dissociate from one another, and at what stage, in the process of degradation.

Indexed as

Amino Acid SequenceBase SequenceCDC2 Protein KinaseCyclinsEnzyme ActivationMolecular Sequence DataOligodeoxyribonucleotidesProtein BindingRecombinant Fusion ProteinsUbiquitinsCDC2 Protein KinaseCyclinsOligodeoxyribonucleotidesRecombinant Fusion ProteinsUbiquitins

Identifiers

PMID8670806
PMCPMC450246
OpenAlexW1959249887

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.