Evidence map›Paper›PMID 7622566›Full record

ArticleThe Journal of cell biology1995

Members of the NAP/SET family of proteins interact specifically with B-type cyclins.

D R Kellogg, A Kikuchi, T Fujii-Nakata, C W Turck, A W Murray

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

65 citing papers in PubMed, 164 citations in OpenAlex.

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  15. Optimization of yeast cell cycle analysis and morphological characterization by multispectral imaging flow cytometry.Cytometry. Part A : the journal of the International Society for Analytical Cytology · 2008
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5 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

5 authors at 1 institution in 1 country.

D R KelloggDepartment of Physiology, University of California, San Francisco 94143-0444, USA.
A Kikuchi
T Fujii-Nakata
C W Turck
A W Murray
University of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclin-dependent kinase complexes that contain the same catalytic subunit are able to induce different events at different times during the cell cycle, but the mechanisms by which they do so remain largely unknown. To address this problem, we have used affinity chromatography to identify proteins that bind specifically to mitotic cyclins, with the goal of finding proteins that interact with mitotic cyclins to carry out the events of mitosis. This approach has led to the identification of a 60-kD protein called NAP1 that interacts specifically with members of the cyclin B family. This interaction has been highly conserved during evolution: NAP1 in the Xenopus embryo interacts with cyclins B1 and B2, but not with cyclin A, and the S. cerevisiae homolog of NAP1 interacts with Clb2 but not with Clb3. Genetic experiments in budding yeast indicate that NAP1 plays an important role in the function of Clb2, while biochemical experiments demonstrate that purified NAP1 can be phosphorylated by cyclin B/p34cdc2 kinase complexes, but not by cyclin A/p34cdc2 kinase complexes. These results suggest that NAP1 is a protein involved in the specific functions of cyclin B/p34cdc2 kinase complexes. In addition to NAP1, we found a 43-kD protein in Xenopus that is homologous to NAP1 and also interacts specifically with B-type cyclins. This protein is the Xenopus homolog of the human SET protein, which was previously identified as part of a putative oncogenic fusion protein (Von Lindern et al., 1992).

Indexed as

Cyclin BSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsBase SequenceCDC2 Protein KinaseCell CompartmentationCell Cycle ProteinsChromatography, AffinityChromosomal Proteins, Non-HistoneCyclinsCytoplasmDNA-Binding ProteinsHistone ChaperonesMitosisMolecular Sequence DataCDC2 Protein KinaseCell Cycle ProteinsChromosomal Proteins, Non-HistoneCLB2 protein, S cerevisiaeCyclin BCyclinsDNA-Binding ProteinsHistone ChaperonesNAP1L1 protein, humanNAP1 protein, S cerevisiaeNuclear ProteinsNucleosome Assembly Protein 1ProteinsSaccharomyces cerevisiae ProteinsSET protein, humanTranscription Factors

Identifiers

PMID7622566
PMCPMC2120524
OpenAlexW2118056303

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.