Evidence map›Paper›PMID 16980360›Full record

ArticleBiophysical journal2006

Dynamic studies of scaffold-dependent mating pathway in yeast.

Danying Shao, Wen Zheng, Wenjun Qiu, Qi Ouyang, Chao Tang

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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  11. Scaffold number in yeast signaling system sets tradeoff between system output and dynamic range.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
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  17. Mapping dynamic protein interactions in MAP kinase signaling using live-cell fluorescence fluctuation spectroscopy and imaging.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  18. Review
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 2 countries.

Danying ShaoCenter for Theoretical Biology, Peking University, Beijing, China.
Wen Zheng
Wenjun Qiu
Qi Ouyang
Chao Tang
Peking University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mating pathway in Saccharomyces cerevisiae is one of the best understood signal transduction pathways in eukaryotes. It transmits the mating signal from plasma membrane into the nucleus through the G-protein coupled receptor and the mitogen-activated protein kinase (MAPK) cascade. According to current understanding of the mating pathway, we construct a system of ordinary differential equations to describe the process. Our model is consistent with a wide range of experiments, indicating that it captures some main characteristics of the signal transduction along the pathway. Investigation with the model reveals that the shuttling of the scaffold protein and the dephosphorylation of kinases involved in the MAPK cascade cooperate to regulate the response upon pheromone induction and to help preserve the fidelity of the mating signaling. We explored factors affecting the dose-response curves of this pathway and found that both negative feedback and concentrations of the proteins involved in the MAPK cascade play crucial roles. Contrary to some other MAPK systems where signaling sensitivity is being amplified successively along the cascade, here the mating signal is transmitted through the cascade in an almost linear fashion.

Indexed as

Genes, Mating Type, FungalBiophysicsCytoplasmFungal ProteinsGTP-Binding ProteinsIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesMAP Kinase Signaling SystemModels, BiologicalModels, ChemicalModels, TheoreticalMutationPhosphorylationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsFungal ProteinsGTP-Binding ProteinsIntracellular Signaling Peptides and ProteinsMAP Kinase Kinase KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsSTE20 protein, S cerevisiae

Identifiers

PMID16980360
PMCPMC1635675
OpenAlexW2123943662

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.