Evidence map›Paper›PMID 22214661›Full record

ReviewCell cycle (Georgetown, Tex.)2012

Deconvoluting mTOR biology.

Jason D Weber, David H Gutmann

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 1 pooled it
7.1field-weighted citation impact, top 2% 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

50 citing papers in PubMed, 1 synthesis or guideline pooled it, 93 citations in OpenAlex.

  1. Pooled it
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  18. Actin up in the Nucleus: Regulation of Actin Structures Modulates Mesenchymal Stem Cell Differentiation.Transactions of the American Clinical and Climatological Association · 2017
    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

2 authors at 1 institution in 1 country.

Jason D WeberDepartment of Internal Medicine, Washington University School of Medicine, St. Louis, MO, USA.
David H Gutmann
Washington University in St. Louis · US

Funding

NEUROFIBROMIN REGULATION OF NEURAL STEM CELL FUNCTION IN VITRO AND IN VIVOR01NS065547 · NINDS · WASHINGTON UNIVERSITY · PI GUTMANN, DAVID H · 2010 to 2014
$1.6M
REGULATION AND ROLE OF MTOR IN NEUROFIBROMIN GROWTH CONTROLR01CA127008 · NCI · WASHINGTON UNIVERSITY · PI GUTMANN, DAVID H, PIWNICA-WORMS, DAVID · 2008 to 2011
$1.6M
NCI NIH HHS CA127008NCI NIH HHS R01 CA127008NINDS NIH HHS NS065547NINDS NIH HHS R01 NS065547
6 · The paper itself

Abstract

In metazoans, TOR is an essential protein that functions as a master regulator of cellular growth and proliferation. Over the past decade, there has been an explosion of information about this critical master kinase, ranging from the composition of the TOR protein complex to its ability to act as an integrator of numerous extracellular signals. Unfortunately, this plethora of information has also raised numerous questions regarding TOR function. Currently, the prevailing view is that mammalian TOR (mTOR) exists in at least two molecular complexes, mTORC1 and mTORC2, which are largely defined by the presence of either RAPTOR or RICTOR. However, additional co-factors have been identified for each complex, and their importance in mediating mTOR signals has been incompletely elucidated. Similarly, there are differences in mTOR function that reflect the tissue of origin. In this review, we present an alternative view to mTOR complex formation and function, which envisions mTOR regulation and signal propagation as a reflection of cell type- and basal state-dependent conditions. The re-interpretation of mTOR biology in this framework may facilitate the design of therapies most likely to effectively inhibit this central regulator of cell behavior.

Indexed as

AnimalsCentral Nervous SystemEnzyme ActivationGene Expression RegulationHumansMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesProteinsProtein TransportSignal TransductionTOR Serine-Threonine KinasesTranscription FactorsCRTC2 protein, humanMechanistic Target of Rapamycin Complex 1Multiprotein ComplexesProteinsTOR Serine-Threonine KinasesTranscription Factors

Identifiers

PMID22214661
PMCPMC3293376
OpenAlexW1992267944

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.