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0027936755
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A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
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(1994)
Science
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Han1
Lee2
Bibbs3
Ulevitch4
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3
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0028229012
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The stress-activated protein kinase subfamily of c-Jun kinases
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of special interest, Reports the cloning of a family of four genes encoding stress-activated protein kinases. Activation of these kinases by a great variety of agonists is likely to be independent of ERK activation.
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(1994)
Nature
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Kyriakis1
Banerjee2
Nikolaki3
Dai4
Rubie5
Ahmad6
Avruch7
Woodgett8
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4
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0028329953
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JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
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of special interest, Isolation of JNK1, a MAP kinase homolog which is activated by UV. Induction by UV results in JNK1 phosphorylation on threonyl and tyrosyl residues. JNK1 binds to and phosphorylates a GST—Jun fusion protein on the equivalents of JUN Ser63 and Ser73.
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(1994)
Cell
, vol.76
, pp. 1025-1037
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Derijard1
Hibi2
Wu3
Barrett4
Su5
Deng6
Karin7
Davis8
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0028272507
-
Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
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of special interest, Modification of Raf to contain a CAAX box results in targeting of Raf to the plasma membrane. Raf-CAAX is hyperactive, resulting in activation of endogeneous MAPK and differentiation of PC12 cells. However, Raf-CAAX is still able to be stimulated by mitogens to the same extent as wild-type Raf, implying the existence of a second mitogen-regulated signal for Raf activation.
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(1994)
Nature
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Leevers1
Paterson2
Marshall3
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7
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0028241533
-
Activation of Raf as a result of recruitment to the plasma membrane
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of special interest, Raf-CAAX is constitutively active and oncogenic. This is entirely independent of Ras activation. This paper further demonstrates that Ras functions as the temporary membrane anchor for Raf.
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(1994)
Science
, vol.264
, pp. 1463-1467
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Stokoe1
Macdonald2
Cadwallader3
Symons4
Hancock5
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0028329630
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Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues
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(1994)
EMBO J
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Zheng1
Guan2
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9
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0028308224
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Identification of 2 serine residues of MEK-1 that are differentially phosphorylated during activation by raf, and MEK kinase
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(1994)
J Biol Chem
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Yan1
Templeton2
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12
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0028141496
-
Transformation of mammalian cells by constitutively active MAP kinase kinase
-
of special interest, Replacing two regulatory series with acidic residues results in 80-fold activation. Similarly, deletion of an amino-terminal domain results in constitutive activation of MEK. Deletion of an amino-terminal domain and mutation of Ser222 to Asp in MEK transforms NIH3T3 cells and results in tumor formation in nude mice. See also [13].
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(1994)
Science
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, pp. 966-970
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Mansour1
Matten2
Hermann3
Candia4
Rong5
Fukasawa6
Vande Woude7
Ahn8
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13
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-
0028228616
-
Activation of MAP kinase kinase is necessary and sufficient for PC12 differentiation and for transformation of NIH3T3 cells
-
of special interest, Replacing two phosphorylated serines with glutamic acid results in approximately 30-fold activation of kinase activity. Microinjection of these mutants into PC12 cells resulted in nerve growth factor (NGF)-independent neutrite outgrowth. Replacing Ser218 with alanine creates a dominant interfering allele of MAPK kinase (MEK), which blocks MAPK activation and NGF-induced neurite activation, and reverts Ras transformed cells. Similar experiments to those in [12] show that constitutively active MEK mutants are oncogenic.
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(1994)
Cell
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Cowley1
Paterson2
Kemp3
Marshall4
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15
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0025120244
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Requirement for integration of signals from two distinct phosphorylation pathways for activation of MAP kinase
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(1990)
Nature
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Anderson1
Maller2
Tonks3
Sturgill4
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16
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0023766145
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Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
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(1988)
Nature
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Sturgill1
Ray2
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0027165150
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The mitogen-activated protein kinase pathway
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(1993)
J Biol Chem
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Davis1
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0027297647
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The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain
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(1993)
Cell
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Marais1
Wynne2
Treisman3
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25
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-
0028935974
-
Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
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of special interest, Isolation of human MKK3 and MKK4 (the human homolog of SEK1) cDNA clones. MKK3 phosphorylates p38 whereas MKK4 can apparently phosphorylate either p38 or JNK1.
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Science
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Derijard1
Raingeaud2
Barrett3
Wu4
Han5
Ulevitch6
Davis7
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26
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0028943245
-
Identification of a dual specificity kinase that activates the Jun kinases and p38-Mpk2
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of special interest, Cloning of the gene coding for JNKK (SEK1). Coexpression of JNKK and MEKK1 potentiates JNK activity, but does not potentiate p38 activity. This is some of the best evidence for independent activation pathways upstream of p38 and JNK.
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(1995)
Science
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Lin1
Minden2
Martinetto3
Claret4
Lange-Carter5
Mercurio6
Johnson7
Karin8
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28
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-
0028670788
-
Activation of stress-activated protein kinase by MEKK1 phosphorylation of its activator SEK1
-
of special interest, These authors created NIH3T3 cells which inducibly express MEKK. Induction of MEKK leads to fourfold activation of JNK activity, but ERK is only activated 1.5-fold. MEKK can phosphorylate SEK1 in vitro. Thus, MEKK is likely to be the physiological activator of JNK.
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(1994)
Nature
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Yan1
Dai2
Deak3
Kyriakis4
Zon5
Woodgett6
Templeton7
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0029055812
-
The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
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of outstanding interest, Elegant experiments showing that activated versions of Rac1 or Cdc42Hs or the Rho exchange proteins, Dbl or Ost, are capable of activating JNK but not ERK.
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Cell
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Coso1
Chiarello2
Yu3
Teramoto4
Crespo5
Xu6
Miki7
Gutkind8
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30
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0029070887
-
Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42HsHs
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of outstanding interest, Demonstration that activated versions of Rac1 lead to activation of SEK1 and JNK1 and to Jun's transcriptional activity. This effect is blocked by dominant-negative MEKK, suggesting that Rac1 probably signals via MEKK.
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(1995)
Cell
, vol.81
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Minden1
Lin2
Claret3
Abo4
Karin5
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0029056399
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A novel serine kinase activated by Rac1/Cdc42Hs-dependent autophosphorylation is related to PAK65 and Ste20
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EMBO J
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Martin1
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Abo4
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0029015774
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The Rho family GTPases RhoA Rac1 and CDC42Hs regulate transcriptional activation by SRF
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Cell
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Hill1
Wynne2
Treisman3
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0028144846
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c-Fos transcriptional activity stimulated by H-Ras-activated protein kinase distinct from JNK and ERK
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Nature
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Deng1
Karin2
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41
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0028338460
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Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB
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(1994)
Cell
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Ginty1
Bonni2
Greenberg3
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42
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0029055761
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Components of a new human protein kinase signal transduction pathway
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J Biol Chem
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Zhou1
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Dixon3
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47
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0028356516
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elk-1 proteins interact with MAP kinases
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(1994)
Oncogene
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Rao1
Reddy2
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48
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0027361017
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Phosphorylation of the c-Fos transrepression domain by mitogen-activated protein kinase and 90-kDa ribosomal S6 kinase
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Proc Natl Acad Sci USA
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Chen1
Abate2
Blenis3
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51
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0027253814
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FUS3 phosphorylates multiple components of the mating signal transduction cascade: evidence for STE12 and FAR1
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Mol Biol Cell
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Elion1
Satterberg2
Kranz3
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Elements of the yeast pheromone response pathway required for filamentous growth of diploids
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Science
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Liu1
Styles2
Fink3
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53
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0028670651
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Elements of a single MAP kinase cascade in Saccharomyces cerevisiae mediate two developmental programs in the same cell type: mating and invasive growth
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Genes Dev
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Roberts1
Fink2
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0028340166
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Mammalian mitogen-activated protein kinase kinase kinase (MEKK) can function in a yeast mitogen-activated protein kinase pathway downstream of protein kinase C
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Proc Natl Acad Sci USA
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Blumer1
Johnson2
Lange-Carter3
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62
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0028134981
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A MAP kinase-dependent spindle assembly checkpoint in Xenopus egg extracts
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of outstanding interest, During the checkpoint resulting from mitotic microtubule depolymerization, extracellular signal regulated kinase (ERK2) is activated. Expression of the phosphatase MKP-1 prevents this checkpoint arrest by inactivating ERK2, showing that ERK2 activity is required for checkpoint arrest.
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(1994)
Cell
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Minshull1
Sun2
Tonks3
Murray4
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63
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0027358722
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MKP-1 (3CH134), an immediate early gene product, is a dual specificity phosphatase that dephosphorylates MAP kinase in vivo
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(1993)
Cell
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Sun1
Charles2
Lau3
Tonks4
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64
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0027306121
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The human CL100 gene encodes a Tyr/Thr-protein phosphatase which potently and specifically inactivates MAP kinase and suppresses its activation by oncogenic ras in Xenopus oocyte extracts
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(1993)
Oncogene
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Alessi1
Smythe2
Keyse3
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65
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0028089986
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Inhibition of Ras-induced DNA synthesis by expression of the phosphatase MKP-1
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of special interest, MKP-1 can inhibit ERK2 activity but not JNK activity. Microinjection of MKP-1 inhibits Ras-induced serum response element transcription and Ras-induced DNA synthesis.
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Science
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, pp. 285-288
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Sun1
Tonks2
Bar-Sagi3
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0028921905
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Isolation and characterization of a novel dual specific phosphatase, HVH2, which selectively dephosphorylates the mitogen-activated protein kinase
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J Biol Chem
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Guan1
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0028170951
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Rapid deactivation of MAP kinase in PC12 cells occurs independently of induction of phosphatase MKP-1
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FEBS Lett
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Wu1
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Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
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Chen1
Martin2
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Counteractive roles of protein phosphatase 2C (PP2C) and a MAP kinase kinase homolog in the osmoregulation of fission yeast
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EMBO J
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Shiozaki1
Russell2
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79
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0028228109
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A two-component osmosensing MAP kinase cascade in yeast
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of outstanding interest, Elegant characterization of the first known eukaryotic two-component histidine kinase osmolarity sensor. Additional experiments highlight the importance of various phosphatases in regulating the Hog1 pathway.
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(1994)
Nature
, vol.369
, pp. 242-245
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Maeda1
Wurgler-Murphy2
Saito3
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