Disruption of 3-phosphoinositide-dependent kinase 1 (PDK1) signaling by the anti-tumorigenic and anti-proliferative agent n-alpha-tosyl-l-phenylalanyl chloromethyl ketone (Q40816988)

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scientific article published on 18 January 2001

Language	Label	Description	Also known as
English	Disruption of 3-phosphoinositide-dependent kinase 1 (PDK1) signaling by the anti-tumorigenic and anti-proliferative agent n-alpha-tosyl-l-phenylalanyl chloromethyl ketone	scientific article published on 18 January 2001

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Disruption of 3-phosphoinositide-dependent kinase 1 (PDK1) signaling by the anti-tumorigenic and anti-proliferative agent n-alpha-tosyl-l-phenylalanyl chloromethyl ketone (English)

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

author name string

Ballif BA

1

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Shimamura A

2

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Pae E

3

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Blenis J

4

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

language of work or name

0 references

publication date

18 January 2001

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Europe PubMed Central

PubMed publication ID

24 September 2017

number of pages

10

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based on heuristic

inferred from page(s)

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

24 September 2017

276

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Europe PubMed Central

PubMed publication ID

24 September 2017

15

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

12466-12475

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

Intracellular signalling: PDK1--a kinase at the hub of things

1 reference

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AKT/PKB and other D3 phosphoinositide-regulated kinases: kinase activation by phosphoinositide-dependent phosphorylation

1 reference

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Cellular signaling: pivoting around PDK-1.

1 reference

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The protein kinase family: conserved features and deduced phylogeny of the catalytic domains

1 reference

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Three protein kinase structures define a common motif

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Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha

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3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro

1 reference

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Phosphorylation and activation of p70s6k by PDK1

1 reference

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Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1

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Regulation of protein kinase C zeta by PI 3-kinase and PDK-1

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Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)

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Primary structure, tissue distribution, and expression of mouse phosphoinositide-dependent protein kinase-1, a protein kinase that phosphorylates and activates protein kinase Czeta

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Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2

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Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway

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Ribosomal S6 kinase 1 (RSK1) activation requires signals dependent on and independent of the MAP kinase ERK.

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90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-phosphoinositide-dependent protein kinase-1.

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Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase

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Sphingosine is a novel activator of 3-phosphoinositide-dependent kinase 1.

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Phosphorylation of Ser-241 is essential for the activity of 3-phosphoinositide-dependent protein kinase-1: identification of five sites of phosphorylation in vivo

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The role of 3-phosphoinositide-dependent protein kinase 1 in activating AGC kinases defined in embryonic stem cells

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Dual Role of Phosphatidylinositol-3,4,5-trisphosphate in the Activation of Protein Kinase B

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Effect of phosphoinositide-dependent kinase 1 on protein kinase B translocation and its subsequent activation

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p70 S6 kinase is regulated by protein kinase Czeta and participates in a phosphoinositide 3-kinase-regulated signalling complex

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

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A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1.

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Dual role of pseudosubstrate in the coordinated regulation of protein kinase C by phosphorylation and diacylglycerol

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Ribosomal S6 kinase signaling and the control of translation

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The 70 kDa S6 kinase: regulation of a kinase with multiple roles in mitogenic signalling

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Tumorigenesis in Mouse Skin: Inhibition by Synthetic Inhibitors of Proteases

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The effect of epsilon amino caproic acid and other inhibitors of proteolysis upon the response of human peripheral blood lymphocytes to phytohemagglutinin

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Suppression of phorbol ester-enhanced radiation-induced malignancy in vitro by protease inhibitors is independent of protein kinase C.

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N-acetylcysteine blocks apoptosis induced by N-alpha-tosyl-L-phenylalanine chloromethyl ketone in transformed T-cells

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The serine protease inhibitors, tosylphenylalanine chloromethyl ketone and tosyllysine chloromethyl ketone, potently inhibit pp70s6k activation

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Rsk1 mediates a MEK-MAP kinase cell survival signal

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Rapamycin-FKBP specifically blocks growth-dependent activation of and signaling by the 70 kd S6 protein kinases

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Evidence for two catalytically active kinase domains in pp90rsk

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Structural and functional analysis of pp70S6k

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PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2.

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N-alpha-Tosyl-L-lysine chloromethyl ketone and N-alpha-tosyl-L-phenylalanine chloromethyl ketone inhibit protein kinase C.

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Identifiers

10.1074/JBC.M009939200

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

24 September 2017

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