Evidence map›Paper›PMID 10611304›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Rapamycin-modulated transcription defines the subset of nutrient-sensitive signaling pathways directly controlled by the Tor proteins.

J S Hardwick, F G Kuruvilla, J K Tong, A F Shamji, S L Schreiber

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 273 papers.

0numbers the graph read from it
0cells of the map it votes in
273citing papers in PubMed
12.4field-weighted citation impact, top 1% 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

273 citing papers in PubMed, 519 citations in OpenAlex.

  1. Article
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  17. Role of eIF5A in Mitochondrial Function.International journal of molecular sciences · 2022
    Review
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  20. Review

213 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 2 institutions in 1 country.

J S HardwickHoward Hughes Medical Institute, Harvard Center for Genomics Research, Department of Chemistry, Harvard University, 12 Oxford Street, Cambridge, MA 02138, USA.
F G Kuruvilla
J K Tong
A F Shamji
S L Schreiber
Harvard University · USHoward Hughes Medical Institute · US

Funding

CONTROLLING SIGNAL TRANSDUCTION WITH SYNTHETIC LIGANDSR01GM052067 · NIGMS · HARVARD UNIVERSITY · PI SCHREIBER, STUART L · 1995 to 2002
$945k
NIGMS NIH HHS GM-52067
6 · The paper itself

Abstract

The immunosuppressant rapamycin inhibits Tor1p and Tor2p (target of rapamycin proteins), ultimately resulting in cellular responses characteristic of nutrient deprivation through a mechanism involving translational arrest. We measured the immediate transcriptional response of yeast grown in rich media and treated with rapamycin to investigate the direct effects of Tor proteins on nutrient-sensitive signaling pathways. The results suggest that Tor proteins directly modulate the glucose activation and nitrogen discrimination pathways and the pathways that respond to the diauxic shift (including glycolysis and the citric acid cycle). Tor proteins do not directly modulate the general amino acid control, nitrogen starvation, or sporulation (in diploid cells) pathways. Poor nitrogen quality activates the nitrogen discrimination pathway, which is controlled by the complex of the transcriptional repressor Ure2p and activator Gln3p. Inhibiting Tor proteins with rapamycin increases the electrophoretic mobility of Ure2p. The work presented here illustrates the coordinated use of genome-based and biochemical approaches to delineate a cellular pathway modulated by the protein target of a small molecule.

Indexed as

Phosphatidylinositol 3-KinasesPrionsSaccharomyces cerevisiae ProteinsCell Cycle ProteinsCitric Acid CycleCulture MediaFungal ProteinsGene Expression ProfilingGlucoseGlutathione PeroxidaseGlycolysisNitrogenNucleic Acid HybridizationOligonucleotide Array Sequence AnalysisPhosphotransferases (Alcohol Group Acceptor)Repressor ProteinsCell Cycle ProteinsCulture MediaFungal ProteinsGlucoseGlutathione PeroxidaseNitrogenPhosphatidylinositol 3-KinasesPhosphotransferases (Alcohol Group Acceptor)PrionsRepressor ProteinsSaccharomyces cerevisiae ProteinsSirolimusTOR1 protein, S cerevisiaeTOR2 protein, S cerevisiaeURE2 protein, S cerevisiae

Identifiers

PMID10611304
PMCPMC24739
OpenAlexW2126415488

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.