The in vivo role of PtdIns(3,4,5)P3 binding to PDK1 PH domain defined by knockin mutation. - Wikidata - wikimedia - TriplyDB

The in vivo role of PtdIns(3,4,5)P3 binding to PDK1 PH domain defined by knockin mutation.

The in vivo role of PtdIns(3,4,5)P3 binding to PDK1 PH domain defined by knockin mutation.

http://www.wikidata.org/entity/Q40561467

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PRAS40 is a target for mammalian target of rapamycin complex 1 and is required for signaling downstream of this complex Role that phosphorylation of GSK3 plays in insulin and Wnt signalling defined by knockin analysis Targeting mTOR: prospects for mTOR complex 2 inhibitors in cancer therapy AKT/PKB signaling: navigating downstream Molecular basis of physiological heart growth: fundamental concepts and new players Lipid biology of breast cancer Phosphoinositides: Key modulators of energy metabolism Mutation of the PDK1 PH Domain Inhibits Protein Kinase B/Akt, Leading to Small Size and Insulin Resistance PDK1-SGK1 Signaling Sustains AKT-Independent mTORC1 Activation and Confers Resistance to PI3Kα Inhibition Ubiquitin-specific protease 4 inhibits mono-ubiquitination of the master growth factor signaling kinase PDK1 Essential role of PDK1 in regulating endothelial cell migration Feedback inhibition of Akt signaling limits the growth of tumors lacking Tsc2 Tyrosine phosphorylation of phosphoinositide-dependent kinase 1 by the insulin receptor is necessary for insulin metabolic signaling Requirement of 3-phosphoinositide-dependent protein kinase-1 for BDNF-mediated neuronal survival Regulation of Hippo pathway by mitogenic growth factors via phosphoinositide 3-kinase and phosphoinositide-dependent kinase-1 cAMP-dependent activation of mammalian target of rapamycin (mTOR) in thyroid cells. Implication in mitogenesis and activation of CDK4.The major target of the endogenously generated reactive oxygen species in response to insulin stimulation is phosphatase and tensin homolog and not phosphoinositide-3 kinase (PI-3 kinase) in the PI-3 kinase/Akt pathway A novel inhibitor of the PI3K/Akt pathway based on the structure of inositol 1,3,4,5,6-pentakisphosphate.Cross-talk between sirtuin and mammalian target of rapamycin complex 1 (mTORC1) signaling in the regulation of S6 kinase 1 (S6K1) phosphorylation.Phosphoinositide-dependent phosphorylation of PDK1 regulates nuclear translocation.Phosphatidylinositol 4,5-bisphosphate-specific AKT1 is oncogenic.PDK1 regulates vascular remodeling and promotes epithelial-mesenchymal transition in cardiac development.Phosphatidylinositol 3-kinase: the oncoprotein.HSV activates Akt to trigger calcium release and promote viral entry: novel candidate target for treatment and suppression.A Preliminary Assessment of the Structure-Activity Relationship of Benzimidazole-Based Anti-Proliferative Agents.Multiple implications of 3-phosphoinositide-dependent protein kinase 1 in human cancer.Activated α2-macroglobulin binding to cell surface GRP78 induces T-loop phosphorylation of Akt1 by PDK1 in association with Raptor.Mechanical regulation of glycogen synthase kinase 3β (GSK3β) in mesenchymal stem cells is dependent on Akt protein serine 473 phosphorylation via mTORC2 protein.3-phosphoinositide-dependent kinase 1 controls breast tumor growth in a kinase-dependent but Akt-independent manner.Phosphoinositide-dependent kinase 1 targets protein kinase A in a pathway that regulates interleukin 4 Sialoadhesin promotes rapid proinflammatory and type I IFN responses to a sialylated pathogen, Campylobacter jejuni.PH motifs in PAR1&2 endow breast cancer growth.Computational Analysis of the Binding Specificities of PH Domains.The TSC1-TSC2 complex is required for proper activation of mTOR complex 2 Reconstitution of modular PDK1 functions on trans-splicing of the regulatory PH and catalytic kinase domains Analysis of 3-phosphoinositide-dependent kinase-1 signaling and function in ES cells.Cross talk between the Akt and p38α pathways in macrophages downstream of Toll-like receptor signaling.Mutation of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) substrate-docking site in the developing brain causes microcephaly with abnormal brain morphogenesis independently of Akt, leading to impaired cognition and disruptive behaviors.A phosphoinositide 3-kinase (PI3K)-serum- and glucocorticoid-inducible kinase 1 (SGK1) pathway promotes Kv7.1 channel surface expression by inhibiting Nedd4-2 protein.New insights into the regulation and function of serine/threonine kinases in T lymphocytes.

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P2860

The in vivo role of PtdIns(3,4,5)P3 binding to PDK1 PH domain defined by knockin mutation.

http://www.wikidata.org/entity/Q40561467

description

2004 nî lūn-bûn

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2004年の論文

@ja

2004年論文

@yue

2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

2004年论文

@zh

2004年论文

@zh-cn

name

The in vivo role of PtdIns(3,4 ...... n defined by knockin mutation.

@en

type

label

The in vivo role of PtdIns(3,4 ...... n defined by knockin mutation.

@en

prefLabel

The in vivo role of PtdIns(3,4 ...... n defined by knockin mutation.

@en

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SJ.EMBOJ.7600218

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The EMBO Journal

P1476

The in vivo role of PtdIns(3,4 ...... n defined by knockin mutation.

@en

P2093

Barry J Collins

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

Edward J McManus

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

J Simon C Arthur

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

Laura J Armit

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

Peter R Ashby

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

Victoria Murray-Tait

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P2860

Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

PDK1, the master regulator of AGC kinase signal transduction

Translocation of PDK-1 to the plasma membrane is important in allowing PDK-1 to activate protein kinase B

3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase

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

WNK1, the kinase mutated in an inherited high-blood-pressure syndrome, is a novel PKB (protein kinase B)/Akt substrate

Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1

Essential role of PDK1 in regulating cell size and development in mice

A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation.

Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA

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2071-2082

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scholarly article

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10.1038/SJ.EMBOJ.7600218

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10

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23

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Alan R. Prescott

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2004-04-29T00:00:00Z

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8589341

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15116068

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424399

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