(Q28240102)

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The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses

scientific article (publication date: 13 May 2005)

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9 January 2020

The tuberous sclerosis protein TSC2 is not required for the regulation of the mammalian target of rapamycin by amino acids and certain cellular stresses (English)

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9 January 2020

tuberous sclerosis

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based on heuristic

inferred from title

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based on heuristic

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1

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9 January 2020

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9 January 2020

Christopher G. Proud

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9 January 2020

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Stephen G Finn

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9 January 2020

Gareth J Browne

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9 January 2020

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16 March 2005

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9 January 2020

Journal of Biological Chemistry

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9 January 2020

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9 January 2020

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9 January 2020

18717-18727

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9 January 2020

Regulation of peptide-chain elongation in mammalian cells

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Regulation of mammalian translation factors by nutrients

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Control of protein synthesis by amino acid availability

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mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery

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Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action

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Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling

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Rapamycin inhibits hepatic stellate cell proliferation in vitro and limits fibrogenesis in an in vivo model of liver fibrosis

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Loss of Tsc1/Tsc2 activates mTOR and disrupts PI3K-Akt signaling through downregulation of PDGFR

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Target of rapamycin (TOR)-signaling and RAIP motifs play distinct roles in the mammalian TOR-dependent phosphorylation of initiation factor 4E-binding protein 1

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Management of cellular energy by the AMP-activated protein kinase system

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TSC2 mediates cellular energy response to control cell growth and survival

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Activation of AMP-activated protein kinase leads to the phosphorylation of elongation factor 2 and an inhibition of protein synthesis

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Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398

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ATP depletion increases phosphorylation of elongation factor eEF2 in adult cardiomyocytes independently of inhibition of mTOR signalling

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Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors

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Hypoxia increases the association of 4E-binding protein 1 with the initiation factor 4E in isolated rat hepatocytes

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DNA-damaging agents cause inactivation of translational regulators linked to mTOR signalling

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The p38 and MK2 kinase cascade phosphorylates tuberin, the tuberous sclerosis 2 gene product, and enhances its interaction with 14-3-3

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A novel mTOR-regulated phosphorylation site in elongation factor 2 kinase modulates the activity of the kinase and its binding to calmodulin

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10.1074/JBC.M414499200

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Consolidated OpenCitations Corpus – April 2017

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9 January 2020

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2 references

Consolidated OpenCitations Corpus – April 2017

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:15772076%20AND%20SRC:MED&resulttype=core&format=json

9 January 2020

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