Dalby KN - Search Results

1

Two rate-limiting steps in the kinetic mechanism of the serine/threonine specific protein kinase ERK2: a case of fast phosphorylation followed by fast product release.

Waas WF, Rainey MA, Szafranska AE, Dalby KN. Waas WF, et al. Among authors: dalby kn. Biochemistry. 2003 Oct 28;42(42):12273-86. doi: 10.1021/bi0348617. Biochemistry. 2003. PMID: 14567689

2

The kinetic mechanism of the dual phosphorylation of the ATF2 transcription factor by p38 mitogen-activated protein (MAP) kinase alpha. Implications for signal/response profiles of MAP kinase pathways.

Waas WF, Lo HH, Dalby KN. Waas WF, et al. Among authors: dalby kn. J Biol Chem. 2001 Feb 23;276(8):5676-84. doi: 10.1074/jbc.M008787200. Epub 2000 Nov 7. J Biol Chem. 2001. PMID: 11069918 Free article.

3

Purification of a model substrate for transcription factor phosphorylation by ERK2.

Waas WF, Dalby KN. Waas WF, et al. Among authors: dalby kn. Protein Expr Purif. 2001 Oct;23(1):191-7. doi: 10.1006/prep.2001.1491. Protein Expr Purif. 2001. PMID: 11570862

4

Transient protein-protein interactions and a random-ordered kinetic mechanism for the phosphorylation of a transcription factor by extracellular-regulated protein kinase 2.

Waas WF, Dalby KN. Waas WF, et al. Among authors: dalby kn. J Biol Chem. 2002 Apr 12;277(15):12532-40. doi: 10.1074/jbc.M110523200. Epub 2002 Jan 25. J Biol Chem. 2002. PMID: 11812784 Free article.

5

Physiological concentrations of divalent magnesium ion activate the serine/threonine specific protein kinase ERK2.

Waas WF, Dalby KN. Waas WF, et al. Among authors: dalby kn. Biochemistry. 2003 Mar 18;42(10):2960-70. doi: 10.1021/bi027171w. Biochemistry. 2003. PMID: 12627962

6

A kinetic approach towards understanding substrate interactions and the catalytic mechanism of the serine/threonine protein kinase ERK2: identifying a potential regulatory role for divalent magnesium.

Waas WF, Rainey MA, Szafranska AE, Cox K, Dalby KN. Waas WF, et al. Among authors: dalby kn. Biochim Biophys Acta. 2004 Mar 11;1697(1-2):81-7. doi: 10.1016/j.bbapap.2003.11.015. Biochim Biophys Acta. 2004. PMID: 15023352 Review.

7

Following in vitro activation of mitogen-activated protein kinases by mass spectrometry and tryptic peptide analysis: purifying fully activated p38 mitogen-activated protein kinase alpha.

Szafranska AE, Luo X, Dalby KN. Szafranska AE, et al. Among authors: dalby kn. Anal Biochem. 2005 Jan 1;336(1):1-10. doi: 10.1016/j.ab.2004.09.039. Anal Biochem. 2005. PMID: 15582552

8

Proximity-induced catalysis by the protein kinase ERK2.

Rainey MA, Callaway K, Barnes R, Wilson B, Dalby KN. Rainey MA, et al. Among authors: dalby kn. J Am Chem Soc. 2005 Aug 3;127(30):10494-5. doi: 10.1021/ja052915p. J Am Chem Soc. 2005. PMID: 16045329 Free PMC article.

9

Kinetic mechanism for p38 MAP kinase alpha. A partial rapid-equilibrium random-order ternary-complex mechanism for the phosphorylation of a protein substrate.

Szafranska AE, Dalby KN. Szafranska AE, et al. Among authors: dalby kn. FEBS J. 2005 Sep;272(18):4631-45. doi: 10.1111/j.1742-4658.2005.04827.x. FEBS J. 2005. PMID: 16156785 Free article.

We show using an untagged highly active form of p38 MAPKalpha, expressed and purified from Escherichia coli[Szafranska AE, Luo X & Dalby KN (2005) Anal Biochem336, 1-10) that at pH 7.5, 10 mm Mg2+ and 27 degrees C p38 MAPKalpha phosphorylates ATF2Delta115 throug …

We show using an untagged highly active form of p38 MAPKalpha, expressed and purified from Escherichia coli[Szafranska AE, Luo X & Da …

10

Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains.

Callaway K, Rainey MA, Dalby KN. Callaway K, et al. Among authors: dalby kn. Biochim Biophys Acta. 2005 Dec 30;1754(1-2):316-23. doi: 10.1016/j.bbapap.2005.11.002. Epub 2005 Nov 16. Biochim Biophys Acta. 2005. PMID: 16324895 Review.

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