PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis. - sprookjes - yvandenbroek - TriplyDB

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

http://www.wikidata.org/entity/Q33306700

about

An integrative computational systems biology approach identifies differentially regulated dynamic transcriptome signatures which drive the initiation of human T helper cell differentiation PRR5L degradation promotes mTORC2-mediated PKC-δ phosphorylation and cell migration downstream of Gα12 Regulation of TOR by small GTPases Spatial regulation of the mTORC1 system in amino acids sensing pathway Targeting mTOR: prospects for mTOR complex 2 inhibitors in cancer therapy Feature Article: mTOR complex 2-Akt signaling at mitochondria-associated endoplasmic reticulum membranes (MAM) regulates mitochondrial physiology mTOR signaling in growth control and disease Characterization of Rictor phosphorylation sites reveals direct regulation of mTOR complex 2 by S6K1 Sirolimus and Everolimus Pathway: Reviewing Candidate Genes Influencing Their Intracellular Effects Autophagy signal transduction by ATG proteins: from hierarchies to networks Cutting through the complexities of mTOR for the treatment of stroke Targeting disease through novel pathways of apoptosis and autophagy Shedding new light on neurodegenerative diseases through the mammalian target of rapamycin Judicious Toggling of mTOR Activity to Combat Insulin Resistance and Cancer: Current Evidence and Perspectives TBCK influences cell proliferation, cell size and mTOR signaling pathway Protor-2 interacts with tristetraprolin to regulate mRNA stability during stress La-related Protein 1 (LARP1) Represses Terminal Oligopyrimidine (TOP) mRNA Translation Downstream of mTOR Complex 1 (mTORC1)RTP801 is induced in Parkinson's disease and mediates neuron death by inhibiting Akt phosphorylation/activation Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress mTOR signaling at a glance Regulation of proline-rich Akt substrate of 40 kDa (PRAS40) function by mammalian target of rapamycin complex 1 (mTORC1)-mediated phosphorylation.Insulin stimulates adipogenesis through the Akt-TSC2-mTORC1 pathway.Dynamic switch of negative feedback regulation in Drosophila Akt-TOR signaling.TOR-dependent control of autophagy: biting the hand that feeds Mechanisms involved in the enhancement of mammalian target of rapamycin signalling and hypertrophy in skeletal muscle of myostatin-deficient mice.mTOR signaling in lymphangioleiomyomatosis Hepatitis C virus NS5A activates the mammalian target of rapamycin (mTOR) pathway, contributing to cell survival by disrupting the interaction between FK506-binding protein 38 (FKBP38) and mTOR Mitochondria are required for pro-ageing features of the senescent phenotype.PRAS40 regulates protein synthesis and cell cycle in C2C12 myoblasts.Regulation of Akt during torpor in the hibernating ground squirrel, Ictidomys tridecemlineatus.The evolution of the TOR pathway and its role in cancer.mTOR signaling for biological control and cancer.Regulation of mTORC1 and its impact on gene expression at a glance.PRAS40 is an integral regulatory component of erythropoietin mTOR signaling and cytoprotection Rab-family GTPase regulates TOR complex 2 signaling in fission yeast Nuclear PRAS40 couples the Akt/mTORC1 signaling axis to the RPL11-HDM2-p53 nucleolar stress response pathway.mTOR direct interactions with Rheb-GTPase and raptor: sub-cellular localization using fluorescence lifetime imaging.Lentivirus-mediated knockdown of eukaryotic translation initiation factor 3 subunit D inhibits proliferation of HCT116 colon cancer cells Inhibition of autoimmune Chagas-like heart disease by bone marrow transplantation Rab small GTPase emerges as a regulator of TOR complex 2

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PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

http://www.wikidata.org/entity/Q33306700

description

2007 nî lūn-bûn

@nan

2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@ast

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@en

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@nl

type

label

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@ast

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@en

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@nl

prefLabel

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@ast

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@en

PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

@nl

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JOURNAL.PONE.0001217

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PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis

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Adiel Cohen

http://www.w3.org/2001/XMLSchema#string

Klaus D Molle

http://www.w3.org/2001/XMLSchema#string

Man Lyang Kim

http://www.w3.org/2001/XMLSchema#string

Michael N Hall

http://www.w3.org/2001/XMLSchema#string

Paul Jenö

http://www.w3.org/2001/XMLSchema#string

Pazit Polak

http://www.w3.org/2001/XMLSchema#string

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Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton

PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase

MAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 binding

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

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

Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive

STIM is a Ca2+ sensor essential for Ca2+-store-depletion-triggered Ca2+ influx

Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control

Identification of a proline-rich Akt substrate as a 14-3-3 binding partner

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e1217

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scholarly article

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10.1371/JOURNAL.PONE.0001217

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11

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2

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Kathrin Thedieck

Cécile ARRIEUMERLOU

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2007-11-21T00:00:00Z

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5817762

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18030348

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2075366

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