Dalby KN - Search Results

1

Activated ERK2 is a monomer in vitro with or without divalent cations and when complexed to the cytoplasmic scaffold PEA-15.

Kaoud TS, Devkota AK, Harris R, Rana MS, Abramczyk O, Warthaka M, Lee S, Girvin ME, Riggs AF, Dalby KN. Kaoud TS, et al. Among authors: dalby kn. Biochemistry. 2011 May 31;50(21):4568-78. doi: 10.1021/bi200202y. Epub 2011 May 4. Biochemistry. 2011. PMID: 21506533 Free PMC article.

2

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

3

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

4

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.

5

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

6

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.

7

Properties and regulation of a transiently assembled ERK2.Ets-1 signaling complex.

Callaway KA, Rainey MA, Riggs AF, Abramczyk O, Dalby KN. Callaway KA, et al. Among authors: dalby kn. Biochemistry. 2006 Nov 21;45(46):13719-33. doi: 10.1021/bi0610451. Biochemistry. 2006. PMID: 17105191

8

Regulation of protein phosphorylation within the MKK1-ERK2 complex by MP1 and the MP1*P14 heterodimer.

Brahma A, Dalby KN. Brahma A, et al. Among authors: dalby kn. Arch Biochem Biophys. 2007 Apr 1;460(1):85-91. doi: 10.1016/j.abb.2006.11.031. Epub 2007 Jan 4. Arch Biochem Biophys. 2007. PMID: 17254543 Free PMC article.

9

Expanding the repertoire of an ERK2 recruitment site: cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding.

Abramczyk O, Rainey MA, Barnes R, Martin L, Dalby KN. Abramczyk O, et al. Among authors: dalby kn. Biochemistry. 2007 Aug 14;46(32):9174-86. doi: 10.1021/bi7002058. Epub 2007 Jul 21. Biochemistry. 2007. PMID: 17658891 Free PMC article.

10

The anti-apoptotic protein PEA-15 is a tight binding inhibitor of ERK1 and ERK2, which blocks docking interactions at the D-recruitment site.

Callaway K, Abramczyk O, Martin L, Dalby KN. Callaway K, et al. Among authors: dalby kn. Biochemistry. 2007 Aug 14;46(32):9187-98. doi: 10.1021/bi700206u. Epub 2007 Jul 21. Biochemistry. 2007. PMID: 17658892

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