Evidence map›Paper›PMID 7925276›Full record

ArticleThe EMBO journal1994

Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis.

J R Lamb, W A Michaud, R S Sikorski, P A Hieter

Abstract read
In one paragraph

Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.

0numbers the graph read from it
0cells of the map it votes in
98citing papers in PubMed
–field-weighted citation impact
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

98 citing papers in PubMed.

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  17. Article
  18. A Wee1 checkpoint inhibits anaphase onset.The Journal of cell biology · 2013
    Article
  19. Article
  20. Structural insights into anaphase-promoting complex function and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011
    Review

38 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

4 authors.

J R LambDepartment of Molecular Biology and Genetics, Johns Hopkins University, School of Medicine, Baltimore, MD 21205.
W A Michaud
R S Sikorski
P A Hieter

Funding

TRANSPOSITION OF TN7P01CA016519 · NCI · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 1985 to 2010
$21.4M
NCI NIH HHS CA16519
6 · The paper itself

Abstract

Cdc16p, Cdc23p and Cdc27p are all essential proteins required for cell cycle progression through mitosis in Saccharomyces cerevisiae. All three proteins contain multiple tandemly repeated 34 amino acid tetratricopeptide repeats (TPRs). Using two independent assays, two-hybrid analysis in vivo and co-immunoprecipitation in vitro, we demonstrate that Cdc16p, Cdc23p and Cdc27p self associate and interact with one another to form a macromolecular complex. A temperature sensitive mutation in the most highly conserved TPR domain of Cdc27p results in a greatly reduced ability to interact with Cdc23p, but has no effect on interactions with wild-type Cdc27p or Cdc16p. The specificity of this effect indicates that TPRs can mediate protein-protein interactions and that this mutation may define an essential interaction for cell cycle progression in yeast. The conservation of at least two of the three proteins from yeast to man suggests that this protein complex is essential for mitosis in a wide range of eukaryotes.

Indexed as

Cell Cycle ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnaphase-Promoting Complex-CyclosomeAntibodies, FungalApc3 Subunit, Anaphase-Promoting Complex-CyclosomeApc6 Subunit, Anaphase-Promoting Complex-CyclosomeBase Sequencebeta-GalactosidaseDNA Mutational AnalysisEukaryotic CellsFungal ProteinsGenetic VectorsMacromolecular SubstancesMitosisMolecular Sequence DataAnaphase-Promoting Complex-CyclosomeAntibodies, FungalApc3 Subunit, Anaphase-Promoting Complex-CyclosomeApc6 Subunit, Anaphase-Promoting Complex-Cyclosomebeta-GalactosidaseCDC16 protein, S cerevisiaeCDC27 protein, S cerevisiaeCell Cycle ProteinsFungal ProteinsMacromolecular SubstancesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesUbiquitin-Protein Ligases

Identifiers

PMID7925276
PMCPMC395359

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.