Evidence map›Paper›PMID 1387709›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1992

Karyoplasmic interaction selection strategy: a general strategy to detect protein-protein interactions in mammalian cells.

E R Fearon, T Finkel, M L Gillison, S P Kennedy, J F Casella, G F Tomaselli, J S Morrow, C Van Dang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 95 citations in OpenAlex.

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  11. Computational approaches to protein-protein interaction.Journal of structural and functional genomics · 2003
    Article
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  14. Intracellular antibody-caspase-mediated cell killing: an approach for application in cancer therapy.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
  15. Article
  16. Reporter gene vectors and assays.Molecular biotechnology · 1999
    Review
  17. Article
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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

8 authors at 2 institutions in 1 country.

E R FearonDepartment of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
T Finkel
M L Gillison
S P Kennedy
J F Casella
G F Tomaselli
J S Morrow
C Van Dang
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We describe a strategy and reagents for study of protein-protein interactions in mammalian cells, termed the karyoplasmic interaction selection strategy (KISS). With this strategy, specific protein-protein interactions are identified by reconstitution of the functional activity of the yeast transcriptional activator GAL4 and the resultant transcription of a GAL4-regulated reporter gene. Reconstitution of GAL4 function results from specific interaction between two chimeric proteins: one contains the DNA-binding domain of GAL4; the other contains a transcriptional activation domain. Transcription of the reporter gene occurs if the two chimeric proteins can form a complex that reconstitutes the DNA-binding and transcriptional activation functions of GAL4. Using the KISS system, we demonstrate specific interactions for sequences from three different pairs of proteins that complex in the cytoplasm. In addition, we demonstrate that reporter genes encoding cell surface or drug-resistance markers can be specifically activated as a result of protein-protein interactions. With these selectable markers, the KISS system can be used to screen specialized cDNA libraries to identify novel protein interactions.

Indexed as

Hybrid CellsSaccharomyces cerevisiae ProteinsTranscription FactorsAmino Acid SequenceAnimalsCHO CellsCricetinaeCytoplasmDNA-Binding ProteinsFlow CytometryFungal ProteinsHerpes Simplex Virus Protein Vmw65Macromolecular SubstancesMolecular Sequence DataProtein BindingRecombinant ProteinsDNA-Binding ProteinsFungal ProteinsGAL4 protein, S cerevisiaeHerpes Simplex Virus Protein Vmw65Macromolecular SubstancesRecombinant ProteinsSaccharomyces cerevisiae ProteinsTranscription FactorsViral Proteins

Identifiers

PMID1387709
PMCPMC49834
OpenAlexW2135440692

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.