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1 MAPKK kinase/MEKK phosphorylates and activates its downs
3 e has revealed the existence of 20 MAPKs, 10 MAPKKs and 60 MAPKKKs, implying a high level of complexi
7 of five phosphoproteins (ERK1 and 2, MEK1/2 [MAPKK], STAT3, and SAPK/JNK), and decreased levels of ph
14 pathway includes a MAPKKK (Wallenda/DLK), a MAPKK (Hemipterous/MKK7), and the Drosophila JNK homolog
16 ology to budding yeast SSK2, which encodes a MAPKK kinase that regulates the HOG1 osmosensing pathway
18 rough synergistic interaction of a MAPKKK, a MAPKK, and a MAPK molecule like MEKK2-JNKK2-JNK1 is like
19 ts T-loop, this suggests that PfPK7 is not a MAPKK orthologue, despite the fact that this enzyme is t
28 of regulatory proteins including activating MAPKKs and an abundance of deactivating phosphatases.
35 eta-activated kinase-1 (TAK1), also known as MAPKK kinase-7 (MAP3K7), is a candidate effector of mult
36 unusual enzyme that automodulates its basal, MAPKK-independent activity by several autophosphorylatio
38 tion is essential for the activation of both MAPKKs and MAPKs, protein phosphatases are likely to be
40 uced lacritin secretion was not inhibited by MAPKK inhibitor U0126, although p42/p44 MAPK was phospho
41 sphorylation and activation of MAP kinase by MAPKK and subsequent phosphorylation and activation of c
45 ts on primary CD4+ T cells as well, cleaving MAPKKs and leading to a 95% reduction in anti-CD3-induce
46 ng immunity and heavy metal stress by common MAPKK and MKP signaling components suggests pivotal role
47 trate that EDR1, a gene encoding a conserved MAPKK kinase, exerts negative regulation on HR cell deat
48 tively active form of human MAPKK-1 (denoted MAPKK-1 R4F or MAPKK-1*) phosphorylates Xenopus p42 MAPK
52 which a constitutively active form of human MAPKK-1 (denoted MAPKK-1 R4F or MAPKK-1*) phosphorylates
54 t PP2Calpha dephosphorylated and inactivated MAPKKs (MKK6 and SEK1) and a MAPK (p38) in the stress-re
59 ed MEKK2-mediated phosphorylation of the key MAPKKs that activate JNK (MAPK kinase (MKK)4 and MKK7).
60 the mitogen-activated protein kinase kinase MAPKK (MEK), by Western blot analysis, sequence identifi
63 re, constitutively active MAP kinase kinase (MAPKK) activated ERalpha in Cos1 cells as expected, but
65 uires the assumption that MAP kinase kinase (MAPKK) carries out its dual phosphorylation of p42 MAPK
66 the mitogen-activated protein kinase kinase (MAPKK) family near to their amino termini, leading to th
70 eas mitogen-activated protein kinase kinase (MAPKK) inhibitor, PD98059, had no effect on CHX-induced
71 ant interfering mutant of MAP kinase kinase (MAPKK) inhibits interleukin-3 (IL-3) activation of MAP k
73 ike mitogen-activated protein kinase kinase (MAPKK) kinase, and to function as a negative regulator o
74 the mitogen-activated protein kinase kinase (MAPKK) pathway and the phosphoinositol-3-kinase (PI-3-K)
75 that converge on the Pbs2 MAP kinase kinase (MAPKK), leading to the activation of the Hog1 MAP kinase
76 Finally, inhibition of MAP kinase kinase (MAPKK), which phosphorylates and thereby activates MAP k
79 the mitogen-activated protein kinase kinase (MAPKK)/MAPK cascade following IGF-I stimulation compared
80 fic mitogen-activated protein kinase kinase (MAPKK)/mitogen-activated protein kinase/ERK kinase (MEK)
85 but no clear orthologue of the MAPK kinase (MAPKK) family, raising the question of the mode of activ
86 kinase (MAPK) NTF6/NRK1, or an MAPK kinase (MAPKK) MEK1/NQK1, attenuated N-mediated resistance to TM
87 panel of constitutively active MAPK kinase (MAPKK) variants in discrete stomatal lineage cell types,
89 nts of the KGB-1 pathway, MEK-1 MAPK kinase (MAPKK), a homolog of mammalian MKK7, and VHP-1 MAPK phos
94 osphorylated and activated by a MAPK kinase (MAPKK), which is activated by an upstream protein kinase
95 vating kinase found in SMCs was MAPK kinase (MAPKK)-1, although MAPKK-2 was present in comparable amo
99 R1 (mitogen-activated protein kinase kinase, MAPKK) prevents the activation of the downstream ERK-A (
101 bind to an overlapping set of MAPK-kinases (MAPKK) in live cells and dictate the localisation of the
102 However, the role of MAP kinase kinases (MAPKKs) and their functional organization within fibrobl
103 e and threonine sites by MAP kinase kinases (MAPKKs) is thought to be the sole activation mechanism.
104 reviously identified the MAP kinase kinases (MAPKKs) MKK3 and MKK6 as the primary regulators of p38 p
105 te mitogen-activated protein kinase kinases (MAPKKs) that propagate prosurvival signals in macrophage
106 ct mitogen-activated protein kinase kinases (MAPKKs), each of which has a distinct functional identit
108 e LF-dependent cleavage of the MAPK kinases (MAPKKs) and disrupted signaling to downstream MAPK targe
111 r that cleaves and inactivates MAPK kinases (MAPKKs) in host cells and has been proposed as a therape
113 l phosphorylation catalyzed by MAPK kinases (MAPKKs), the MAPK p38beta is exceptional and is capable
115 of MPK3/MPK6 or their upstream MAPK kinases (MAPKKs; or MKKs), MKK4/MKK5, resulted in shortened pedic
118 ing in roots using inhibitors of a mammalian MAPKK blocked auxin-activated transgene expression in BA
119 ause it was still capable of inhibiting MAPK/MAPKK-1 stimulation by FCS in phorbol ester-pretreated c
120 nine, and 10 genes encoding distinct MAPKs, MAPKKs, and MAPKKKs, respectively, were silenced using v
121 Among the plants silenced for various MAPKs, MAPKKs, and MAPKKKs, those in which GmMAPK4 homologs (Gm
122 be forced to functionally replace the mating MAPKK Ste7, but only if the proper set of recruitment in
124 mitogen-activated protein kinase kinase/MEK/MAPKK 1-4 and 6, but not mitogen-activated protein kinas
125 acologic inhibition of MAPK/ERK kinase (MEK; MAPKK) using a specific MEK inhibitor, CI-1040, induced
130 spite the fact that this enzyme is the most 'MAPKK-like' enzyme encoded in the P. falciparum genome.
137 sphorylation reaction exceeded the amount of MAPKK-1* present, which would not be possible if the pho
138 identify the emergence of a concentration of MAPKK that provides the best response with respect to ra
139 cascade, while over- and under-expression of MAPKK relative to this concentration have qualitatively
140 expression of constitutively active forms of MAPKK has previously been shown to transform nonmalignan
141 in cell-cycle entry from G(0), the level of MAPKK activity was observed to affect the kinetics of pr
142 hibition of the MAPK pathway at the level of MAPKK, by expression of a dominant-negative mutant or by
143 sion of a constitutively activated mutant of MAPKK does not replace IL-3, but renders cells able to p
144 blasts, but the effect of down-regulation of MAPKK on tumorigenesis and angiogenesis in a well establ
148 tions in defining the functional identity of MAPKKs by asking whether we can use recruitment interact
149 e I IFN receptor chain confirmed the role of MAPKKs and IRF7 in Tat-mediated modulation of ISGs and e
150 uman monocytoid line MonoMac 6 as sources of MAPKKs and visualization of the extent of cleavage after
152 The captured LF was exposed to an optimized MAPKK-based peptide substrate, which it hydrolyzed into
153 orm of human MAPKK-1 (denoted MAPKK-1 R4F or MAPKK-1*) phosphorylates Xenopus p42 MAPK in vitro.
154 use recruitment interactions to force other MAPKK catalytic domains to play the functional role of t
156 be the binding and translocation of the Pbs2 MAPKK to the plasma membrane, and specifically to sites
162 dition, treatment of cells with the specific MAPKK inhibitor PD 98059 during a synchronous S phase ar
163 ase kinase (MAPKKKK, Ste20), MAPKKK (Ste11), MAPKK (Ste7), and transcription factor (Ste12) to promot
164 n kinase kinase kinase-Ste11 (MAPKKK-Ste11), MAPKK-Ste7, and MAPK-Kss1 mediate pheromone-induced mati
172 JNK1 activation by MEKK2 was mediated by the MAPKK JNK kinase 2 (JNKK2) rather than by JNKK1 through
173 icity of JNK activation is determined by the MAPKK JNKK1, which interacts with the MAPKKK MEKK1 and J
176 myocytes, the stimulation of p38 MAPK by the MAPKK, MKK6, activates the transcription factor, NF-kapp
177 ugh activation of MEK (MAPK/erk kinase), the MAPKK (mitogen-activated protein kinase kinase) that fun
181 nated protein kinase (TOPK), a member of the MAPKK protein family, is highly expressed in human color
184 APK became bisphosphorylated depended on the MAPKK-1* concentration, behavior that is predicted by th
185 tein kinase (MAPK) pathway that recruits the MAPKK kinase YODA (YDA) and MAPK 6 (MPK6) to the cortica
187 t signal strength, dependence on both of the MAPKKs for signaling, phosphorylation site preferences b
189 sphorylation site preferences by each of the MAPKKs, and both activation and inhibition resulting fro
191 h a signaling cascade consisting of Ras, the MAPKKs MKK4 and MEK1, the MAPKs SAPKs and ERKs, and the
192 ever, inactivation of the gene encoding this MAPKK by homologous recombination suggested the existenc
197 APK limits the ubiquitination of an upstream MAPKK and thereby prevents spurious activation of a seco
200 phosphorylation is regulated by the upstream MAPKK, Pbs2, which in turn is regulated by the MAPKKK, S
201 leaves and suppressing expression of various MAPKK and MAPK genes by virus-induced gene silencing, we
202 s, rather than a processive mechanism, where MAPKK carries out both phosphorylations before dissociat
203 p42 MAPK by a distributive mechanism, where MAPKK dissociates from MAPK between the first and second
205 uggest that cytoplasmic localization of Wis1 MAPKK by its NES is important for stress signaling to th
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