158 related articles for article (PubMed ID: 10521408)
1. Identification of a cytoplasmic-retention sequence in ERK2.
Rubinfeld H; Hanoch T; Seger R
J Biol Chem; 1999 Oct; 274(43):30349-52. PubMed ID: 10521408
[TBL] [Abstract][Full Text] [Related]
2. Identification of a C-terminal region that is required for the nuclear translocation of ERK2 by passive diffusion.
Shibayama S; Shibata-Seita R; Miura K; Kirino Y; Takishima K
J Biol Chem; 2002 Oct; 277(40):37777-82. PubMed ID: 12149268
[TBL] [Abstract][Full Text] [Related]
3. 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; 276(27):24490-7. PubMed ID: 11328824
[TBL] [Abstract][Full Text] [Related]
4. Nuclear shuttling of mitogen-activated protein (MAP) kinase (extracellular signal-regulated kinase (ERK) 2) was dynamically controlled by MAP/ERK kinase after antigen stimulation in RBL-2H3 cells.
Furuno T; Hirashima N; Onizawa S; Sagiya N; Nakanishi M
J Immunol; 2001 Apr; 166(7):4416-21. PubMed ID: 11254696
[TBL] [Abstract][Full Text] [Related]
5. 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; 8(21):1141-50. PubMed ID: 9799732
[TBL] [Abstract][Full Text] [Related]
6. Biochemical and biological functions of the N-terminal, noncatalytic domain of extracellular signal-regulated kinase 2.
Eblen ST; Catling AD; Assanah MC; Weber MJ
Mol Cell Biol; 2001 Jan; 21(1):249-59. PubMed ID: 11113199
[TBL] [Abstract][Full Text] [Related]
7. 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; 277(17):14844-52. PubMed ID: 11823456
[TBL] [Abstract][Full Text] [Related]
8. Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides substrate specificity and retains ERK2 in the cytoplasm.
Zúñiga A; Torres J; Ubeda J; Pulido R
J Biol Chem; 1999 Jul; 274(31):21900-7. PubMed ID: 10419510
[TBL] [Abstract][Full Text] [Related]
9. 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; 276(28):26509-15. PubMed ID: 11352917
[TBL] [Abstract][Full Text] [Related]
10. Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity.
Bardwell AJ; Abdollahi M; Bardwell L
Biochem J; 2003 Mar; 370(Pt 3):1077-85. PubMed ID: 12529172
[TBL] [Abstract][Full Text] [Related]
11. Role of non-phosphorylated activation loop residues in determining ERK2 dephosphorylation, activity, and subcellular localization.
Bendetz-Nezer S; Seger R
J Biol Chem; 2007 Aug; 282(34):25114-22. PubMed ID: 17597065
[TBL] [Abstract][Full Text] [Related]
12. 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; 278(32):29901-12. PubMed ID: 12754209
[TBL] [Abstract][Full Text] [Related]
13. The death effector domain protein PEA-15 prevents nuclear entry of ERK2 by inhibiting required interactions.
Whitehurst AW; Robinson FL; Moore MS; Cobb MH
J Biol Chem; 2004 Mar; 279(13):12840-7. PubMed ID: 14707138
[TBL] [Abstract][Full Text] [Related]
14. The N-terminal ERK-binding site of MEK1 is required for efficient feedback phosphorylation by ERK2 in vitro and ERK activation in vivo.
Xu Be; Wilsbacher JL; Collisson T; Cobb MH
J Biol Chem; 1999 Nov; 274(48):34029-35. PubMed ID: 10567369
[TBL] [Abstract][Full Text] [Related]
15. ERK2 enters the nucleus by a carrier-independent mechanism.
Whitehurst AW; Wilsbacher JL; You Y; Luby-Phelps K; Moore MS; Cobb MH
Proc Natl Acad Sci U S A; 2002 May; 99(11):7496-501. PubMed ID: 12032311
[TBL] [Abstract][Full Text] [Related]
16. Different domains of the mitogen-activated protein kinases ERK3 and ERK2 direct subcellular localization and upstream specificity in vivo.
Robinson MJ; Xu Be BE; Stippec S; Cobb MH
J Biol Chem; 2002 Feb; 277(7):5094-100. PubMed ID: 11741894
[TBL] [Abstract][Full Text] [Related]
17. Direct monitoring of the expression of the green fluorescent protein-extracellular signal-regulated kinase 2 fusion protein in transfected cells using capillary electrophoresis with laser-induced fluorescence detection.
Yoon S; Ban E; Yoo YS
J Chromatogr A; 2002 Nov; 976(1-2):87-93. PubMed ID: 12462599
[TBL] [Abstract][Full Text] [Related]
18. Two clusters of residues at the docking groove of mitogen-activated protein kinases differentially mediate their functional interaction with the tyrosine phosphatases PTP-SL and STEP.
Tárrega C; Blanco-Aparicio C; Muñoz JJ; Pulido R
J Biol Chem; 2002 Jan; 277(4):2629-36. PubMed ID: 11711538
[TBL] [Abstract][Full Text] [Related]
19. 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; 280(45):37885-94. PubMed ID: 16148006
[TBL] [Abstract][Full Text] [Related]
20. 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. PubMed ID: 18794356
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
