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Items: 1 to 20 of 102

1.

Substrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifs.

Sheridan DL, Kong Y, Parker SA, Dalby KN, Turk BE.

J Biol Chem. 2008 Jul 11;283(28):19511-20. doi: 10.1074/jbc.M801074200. Epub 2008 May 15.

3.

Molecular determinants that mediate selective activation of p38 MAP kinase isoforms.

Enslen H, Brancho DM, Davis RJ.

EMBO J. 2000 Mar 15;19(6):1301-11.

4.

Selectivity of docking sites in MAPK kinases.

Bardwell AJ, Frankson E, Bardwell L.

J Biol Chem. 2009 May 8;284(19):13165-73. doi: 10.1074/jbc.M900080200. Epub 2009 Feb 5.

5.

Docking interactions in the mitogen-activated protein kinase cascades.

Tanoue T, Nishida E.

Pharmacol Ther. 2002 Feb-Mar;93(2-3):193-202. Review.

PMID:
12191611
6.

Spatially separate docking sites on ERK2 regulate distinct signaling events in vivo.

Dimitri CA, Dowdle W, MacKeigan JP, Blenis J, Murphy LO.

Curr Biol. 2005 Jul 26;15(14):1319-24.

7.

Two hydrophobic residues can determine the specificity of mitogen-activated protein kinase docking interactions.

Bardwell AJ, Bardwell L.

J Biol Chem. 2015 Oct 30;290(44):26661-74. doi: 10.1074/jbc.M115.691436. Epub 2015 Sep 14.

8.

A conserved docking motif in MAP kinases common to substrates, activators and regulators.

Tanoue T, Adachi M, Moriguchi T, Nishida E.

Nat Cell Biol. 2000 Feb;2(2):110-6.

PMID:
10655591
9.

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.

10.
11.

Molecular recognitions in the MAP kinase cascades.

Tanoue T, Nishida E.

Cell Signal. 2003 May;15(5):455-62. Review.

PMID:
12639708
12.

Extracellular signal-regulated kinase 2 (ERK2) phosphorylation sites and docking domain on the nuclear pore complex protein Tpr cooperatively regulate ERK2-Tpr interaction.

Vomastek T, Iwanicki MP, Burack WR, Tiwari D, Kumar D, Parsons JT, Weber MJ, Nandicoori VK.

Mol Cell Biol. 2008 Nov;28(22):6954-66. doi: 10.1128/MCB.00925-08. Epub 2008 Sep 15.

13.

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.

14.

Use of docking peptides to design modular substrates with high efficiency for mitogen-activated protein kinase extracellular signal-regulated kinase.

Fernandes N, Bailey DE, Vanvranken DL, Allbritton NL.

ACS Chem Biol. 2007 Oct 19;2(10):665-73. Epub 2007 Oct 6.

15.

ERK5 is targeted to myocyte enhancer factor 2A (MEF2A) through a MAPK docking motif.

Barsyte-Lovejoy D, Galanis A, Clancy A, Sharrocks AD.

Biochem J. 2004 Aug 1;381(Pt 3):693-9.

16.

Specificity determinants in MAPK signaling to transcription factors.

Barsyte-Lovejoy D, Galanis A, Sharrocks AD.

J Biol Chem. 2002 Mar 22;277(12):9896-903. Epub 2002 Jan 10.

17.

Effect of the DEF motif on phosphorylation of peptide substrates by ERK.

Fernandes N, Allbritton NL.

Biochem Biophys Res Commun. 2009 Sep 18;387(2):414-8. doi: 10.1016/j.bbrc.2009.07.049. Epub 2009 Jul 15.

18.

Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase.

Qi H, Prabakaran S, Cantrelle FX, Chambraud B, Gunawardena J, Lippens G, Landrieu I.

J Biol Chem. 2016 Apr 1;291(14):7742-53. doi: 10.1074/jbc.M115.700914. Epub 2016 Feb 8.

19.

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.

20.

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