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Items: 1 to 20 of 118

1.

Docking interactions induce exposure of activation loop in the MAP kinase ERK2.

Zhou T, Sun L, Humphreys J, Goldsmith EJ.

Structure. 2006 Jun;14(6):1011-9.

2.

A bipartite mechanism for ERK2 recognition by its cognate regulators and substrates.

Zhang J, Zhou B, Zheng CF, Zhang ZY.

J Biol Chem. 2003 Aug 8;278(32):29901-12.

3.

ERK2 shows a restrictive and locally selective mechanism of recognition by its tyrosine phosphatase inactivators not shared by its activator MEK1.

Tárrega C, Ríos P, Cejudo-Marín R, Blanco-Aparicio C, van den Berk L, Schepens J, Hendriks W, Tabernero L, Pulido R.

J Biol Chem. 2005 Nov 11;280(45):37885-94.

4.
6.

Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for MAP kinase regulation.

Szedlacsek SE, Aricescu AR, Fulga TA, Renault L, Scheidig AJ.

J Mol Biol. 2001 Aug 17;311(3):557-68.

PMID:
11493009
7.

Molecular determinants of substrate recognition in hematopoietic protein-tyrosine phosphatase.

Huang Z, Zhou B, Zhang ZY.

J Biol Chem. 2004 Dec 10;279(50):52150-9.

8.
9.

A kinetic approach for the study of protein phosphatase-catalyzed regulation of protein kinase activity.

Wang ZX, Zhou B, Wang QM, Zhang ZY.

Biochemistry. 2002 Jun 18;41(24):7849-57.

PMID:
12056917
11.

Multiple regions of MAP kinase phosphatase 3 are involved in its recognition and activation by ERK2.

Zhou B, Wu L, Shen K, Zhang J, Lawrence DS, Zhang ZY.

J Biol Chem. 2001 Mar 2;276(9):6506-15.

13.

The structure of phosphorylated p38gamma is monomeric and reveals a conserved activation-loop conformation.

Bellon S, Fitzgibbon MJ, Fox T, Hsiao HM, Wilson KP.

Structure. 1999 Sep 15;7(9):1057-65.

PMID:
10508788
14.
15.

Hydrogen exchange solvent protection by an ATP analogue reveals conformational changes in ERK2 upon activation.

Lee T, Hoofnagle AN, Resing KA, Ahn NG.

J Mol Biol. 2005 Oct 28;353(3):600-12.

PMID:
16185715
16.

New insights into the catalytic activation of the MAPK phosphatase PAC-1 induced by its substrate MAPK ERK2 binding.

Zhang Q, Muller M, Chen CH, Zeng L, Farooq A, Zhou MM.

J Mol Biol. 2005 Dec 9;354(4):777-88.

PMID:
16288922
17.

Active mutants of the human p38alpha mitogen-activated protein kinase.

Diskin R, Askari N, Capone R, Engelberg D, Livnah O.

J Biol Chem. 2004 Nov 5;279(45):47040-9.

18.

Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2.

Farooq A, Chaturvedi G, Mujtaba S, Plotnikova O, Zeng L, Dhalluin C, Ashton R, Zhou MM.

Mol Cell. 2001 Feb;7(2):387-99.

19.

The third conformation of p38α MAP kinase observed in phosphorylated p38α and in solution.

Akella R, Min X, Wu Q, Gardner KH, Goldsmith EJ.

Structure. 2010 Dec 8;18(12):1571-8. doi: 10.1016/j.str.2010.09.015.

20.

Mechanism of mitogen-activated protein kinase phosphatase-3 activation by ERK2.

Zhou B, Zhang ZY.

J Biol Chem. 1999 Dec 10;274(50):35526-34.

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