(Q27641426)

1

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Christine B Breitenlechner

2

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Petra Rüger

3

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Ute Jucknischke

4

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Thorsten Schneider

5

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Dirk Bossemeyer

7

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Richard A Engh

Journal of Molecular Biology

8

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language of work or name

English

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publication date

20 June 2003

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published in

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volume

329

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page(s)

1021-34

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issue

5

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cites work

Protein kinases--the major drug targets of the twenty-first century?

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A single amino acid substitution makes ERK2 susceptible to pyridinyl imidazole inhibitors of p38 MAP kinase

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Structural basis for selective inhibition of Src family kinases by PP1

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Transcriptional regulation by cyclic AMP.

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The glycine-rich sequence of protein kinases: a multifunctional element

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Multiple pathway signal transduction by the cAMP-dependent protein kinase.

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cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes

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Phosphorylation of Akt/PKB is required for suppression of cancer cell apoptosis and tumor progression in human colorectal carcinoma

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Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP

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Expression, purification, characterization and homology modeling of active Akt/PKB, a key enzyme involved in cell survival signaling

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Crystal structures of catalytic subunit of cAMP-dependent protein kinase in complex with isoquinolinesulfonyl protein kinase inhibitors H7, H8, and H89. Structural implications for selectivity

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Crystal structure of a transition state mimic of the catalytic subunit of cAMP-dependent protein kinase

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Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential

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Crystal structure of the potent natural product inhibitor balanol in complex with the catalytic subunit of cAMP-dependent protein kinase

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Synergistic binding of nucleotides and inhibitors to cAMP-dependent protein kinase examined by acrylodan fluorescence spectroscopy

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Phosphorylation and flexibility of cyclic-AMP-dependent protein kinase (PKA) using (31)P NMR spectroscopy

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Intermolecular contacts in various crystal forms related to the open and closed conformational states of the catalytic subunit of cAMP-dependent protein kinase

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Structural aspects of protein kinase control-role of conformational flexibility

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2.2 A refined crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MnATP and a peptide inhibitor.

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An ATP-linked structural change in protein kinase A precedes phosphoryl transfer under physiological magnesium concentrations

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Crystal structure of the catalytic subunit of cAMP-dependent protein kinase complexed with MgATP and peptide inhibitor

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Non-hydrogen bond interactions involving the methionine sulfur atom.

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Interactions with aromatic rings in chemical and biological recognition

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Cloning of the C alpha catalytic subunit of the bovine cAMP-dependent protein kinase

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In vivo activation of recombinant cAPK catalytic subunit active site mutants by coexpression of the wild-type enzyme, evidence for intermolecular cotranslational phosphorylation

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Isoquinolinesulfonamides, novel and potent inhibitors of cyclic nucleotide-dependent protein kinase and protein kinase C

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Vasodilator actions of HA1077 in vitro and in vivo putatively mediated by the inhibition of protein kinase

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Crystal Structure of the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

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