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Items: 1 to 20 of 114

1.

Hydrophobic as well as charged residues in both MEK1 and ERK2 are important for their proper docking.

Xu Be, Stippec S, Robinson FL, Cobb MH.

J Biol Chem. 2001 Jul 13;276(28):26509-15. Epub 2001 May 14.

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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. Epub 2003 May 16.

5.

Identification of novel point mutations in ERK2 that selectively disrupt binding to MEK1.

Robinson FL, Whitehurst AW, Raman M, Cobb MH.

J Biol Chem. 2002 Apr 26;277(17):14844-52. Epub 2002 Jan 31.

6.

A docking site in MKK4 mediates high affinity binding to JNK MAPKs and competes with similar docking sites in JNK substrates.

Ho DT, Bardwell AJ, Abdollahi M, Bardwell L.

J Biol Chem. 2003 Aug 29;278(35):32662-72. Epub 2003 Jun 3.

7.

A conserved docking site in MEKs mediates high-affinity binding to MAP kinases and cooperates with a scaffold protein to enhance signal transmission.

Bardwell AJ, Flatauer LJ, Matsukuma K, Thorner J, Bardwell L.

J Biol Chem. 2001 Mar 30;276(13):10374-86. Epub 2000 Dec 28.

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Identification of a cytoplasmic-retention sequence in ERK2.

Rubinfeld H, Hanoch T, Seger R.

J Biol Chem. 1999 Oct 22;274(43):30349-52.

11.

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. Epub 2005 Sep 7.

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Quantitative analysis of ERK2 interactions with substrate proteins: roles for kinase docking domains and activity in determining binding affinity.

Burkhard KA, Chen F, Shapiro P.

J Biol Chem. 2011 Jan 28;286(4):2477-85. doi: 10.1074/jbc.M110.177899. Epub 2010 Nov 22.

14.

Negative regulation of MAPKK by phosphorylation of a conserved serine residue equivalent to Ser212 of MEK1.

Gopalbhai K, Jansen G, Beauregard G, Whiteway M, Dumas F, Wu C, Meloche S.

J Biol Chem. 2003 Mar 7;278(10):8118-25. Epub 2002 Dec 27.

15.

A constitutively active and nuclear form of the MAP kinase ERK2 is sufficient for neurite outgrowth and cell transformation.

Robinson MJ, Stippec SA, Goldsmith E, White MA, Cobb MH.

Curr Biol. 1998 Oct 22;8(21):1141-50.

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18.

Mitogen-activated protein kinase feedback phosphorylation regulates MEK1 complex formation and activation during cellular adhesion.

Eblen ST, Slack-Davis JK, Tarcsafalvi A, Parsons JT, Weber MJ, Catling AD.

Mol Cell Biol. 2004 Mar;24(6):2308-17.

19.

Involvement of the activation loop of ERK in the detachment from cytosolic anchoring.

Wolf I, Rubinfeld H, Yoon S, Marmor G, Hanoch T, Seger R.

J Biol Chem. 2001 Jul 6;276(27):24490-7. Epub 2001 Apr 27. Retraction in: J Biol Chem. 2017 May 26;292(21):8853.

20.

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