Evidence map›Paper›PMID 23728461›Full record

ReviewNature cell biology2013

Signal integration by mTORC1 coordinates nutrient input with biosynthetic output.

Christian C Dibble, Brendan D Manning

Open access · greenAbstract readReview
In one paragraph

Review in Nature cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 440 papers.

0numbers the graph read from it
0cells of the map it votes in
440citing papers in PubMed
32.0field-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

440 citing papers in PubMed, 714 citations in OpenAlex.

  1. Phase II Clinical Trial of Everolimus in a Pan-Cancer Cohort of Patients with mTOR Pathway Alterations.Clinical cancer research : an official journal of the American Association for Cancer Research · 2021
    Trial
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380 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

2 authors at 1 institution in 1 country.

Christian C DibbleDivision of Signal Transduction, Beth Israel Deaconess Medical Center, Systems Biology Department, Harvard Medical School, Boston, Massachusetts 02115, USA.
Brendan D Manning
Harvard University · US

Funding

Tuberous Sclerosis-Pathway and PathogenesisP01CA120964 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI David J. Kwiatkowski · 2007 to 2026
$35.9M
Training Program in Angiogenesis &InflammationT32HL007893 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI DVORAK, HAROLD FISHER · 1998 to 2017
$5.5M
Regulatory mechanisms and role of the PI3K-TSC-mTOR signaling network in tumorsR01CA122617 · NCI · HARVARD SCHOOL OF PUBLIC HEALTH · PI MANNING, BRENDAN D. · 2006 to 2015
$2.7M
NCI NIH HHS P01 CA120964NCI NIH HHS P01-CA120964NCI NIH HHS R01 CA122617NCI NIH HHS R01-CA122617NHLBI NIH HHS 5T32HL007893‑15NHLBI NIH HHS T32 HL007893
6 · The paper itself

Abstract

Flux through metabolic pathways is inherently sensitive to the levels of specific substrates and products, but cellular metabolism is also managed by integrated control mechanisms that sense the nutrient and energy status of a cell or organism. The mechanistic target of rapamycin complex 1 (mTORC1), a protein kinase complex ubiquitous to eukaryotic cells, has emerged as a critical signalling node that links nutrient sensing to the coordinated regulation of cellular metabolism. Here, we discuss the role of mTORC1 as a conduit between cellular growth conditions and the anabolic processes that promote cell growth. The emerging network of signalling pathways through which mTORC1 integrates systemic signals (secreted growth factors) with local signals (cellular nutrients - amino acids, glucose and oxygen - and energy, ATP) is detailed. Our expanding understanding of the regulatory network upstream of mTORC1 provides molecular insights into the integrated sensing mechanisms by which diverse cellular signals converge to control cell physiology.

Indexed as

Energy MetabolismMetabolic Networks and PathwaysSignal TransductionAmino AcidsAnimalsBiosynthetic PathwaysFoodGlucoseHumansMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesTOR Serine-Threonine KinasesAmino AcidsGlucoseMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesTOR Serine-Threonine Kinases

Identifiers

PMID23728461
PMCPMC3743096
OpenAlexW2086528604

What OpenQuestion holds

Textmetadata
LicenceTDM
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.