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PMID: 18163952
From fig.1
PMID: 18163952
From fig.1
PMID: 18163952
From fig.1
PMID: 18163952, 9759489, 7532278, 9726434
The STAT1 and STAT2 proteins have been reported to be activated by the IFN-α/β via tyrosyl phosphorylation at critical residues, using tyrosine kinases Tyk2 and JAK1.
PMID: 18163952, 9759489, 7532278, 9726434
The STAT1 and STAT2 proteins have been reported to be activated by the IFN-α/β via tyrosyl phosphorylation at critical residues, using tyrosine kinases Tyk2 and JAK1.
PMID: 18163952, 9759489, 7532278, 9726434
The STAT1 and STAT2 proteins have been reported to be activated by the IFN-α/β via tyrosyl phosphorylation at critical residues, using tyrosine kinases Tyk2 and JAK1.
PMID: 18163952, 9759489, 7532278, 9726434
The STAT1 and STAT2 proteins have been reported to be activated by the IFN-α/β via tyrosyl phosphorylation at critical residues, using tyrosine kinases Tyk2 and JAK1.
PMID: 18163952, 8417326
After being activated (i.e. tyrosyl phosphorylated) STAT1 and STAT2 heterodimers associate with the non-STAT DNA-binding protein, IFN gene regulatory factor-9 (IRF-9/p48/ISGF3-γ)
PMID: 18163952, 8417326
After being activated (i.e. tyrosyl phosphorylated) STAT1 and STAT2 heterodimers associate with the non-STAT DNA-binding protein, IFN gene regulatory factor-9 (IRF-9/p48/ISGF3-γ)
PMID: 18163952
The resultant trimeric transcription factor, ISGF3, binds to the IFN-stimulated regulatory elements (ISREs) to induce the expression of many IFN-α/β-regulated genes.
PMID: 18163952
The resultant trimeric transcription factor, ISGF3, binds to the IFN-stimulated regulatory elements (ISREs) to induce the expression of many IFN-α/β-regulated genes.
PMID: 18163952
From fig.1
PMID: 18163952
From fig.1
PMID: 18163952
From fig.1
PMID: 18163952
From fig.1
PMID: 18163952
Only the STAT1 protein is tyrosyl phosphorylated by JAK1 and JAK2 at the ligand engaged type II IFN receptor.
PMID: 18163952, 7690989
STAT1 dimers, thus formed, migrate to the nucleus, bind to the γ-IFN-activated sequence (GAS) to drive γ-IFN-induced gene expression
PMID: 18163952, 7690989
STAT1 dimers, thus formed, migrate to the nucleus, bind to the γ-IFN-activated sequence (GAS) to drive γ-IFN-induced gene expression
PMID: 18163952, 7690989
STAT1 dimers, thus formed, migrate to the nucleus, bind to the γ-IFN-activated sequence (GAS) to drive γ-IFN-induced gene expression
PMID: 18163952, 7690989
STAT1 dimers, thus formed, migrate to the nucleus, bind to the γ-IFN-activated sequence (GAS) to drive γ-IFN-induced gene expression
PMID: 18163952, 15166220
The ligand-bound type III IFN receptor, although activated in a manner similar to the type I receptor, activates multiple STATs-STAT1, STAT2, STAT3, STAT4 and STAT5
PMID: 18163952, 15166220
The ligand-bound type III IFN receptor, although activated in a manner similar to the type I receptor, activates multiple STATs-STAT1, STAT2, STAT3, STAT4 and STAT5
PMID: 18163952, 15166220
The ligand-bound type III IFN receptor, although activated in a manner similar to the type I receptor, activates multiple STATs-STAT1, STAT2, STAT3, STAT4 and STAT5
PMID: 18163952, 15166220
The ligand-bound type III IFN receptor, although activated in a manner similar to the type I receptor, activates multiple STATs-STAT1, STAT2, STAT3, STAT4 and STAT5
PMID: 18163952, 15166220
The ligand-bound type III IFN receptor, although activated in a manner similar to the type I receptor, activates multiple STATs-STAT1, STAT2, STAT3, STAT4 and STAT5
PMID: 18163952, 15166220
The ligand-bound type III IFN receptor, although activated in a manner similar to the type I receptor, activates multiple STATs-STAT1, STAT2, STAT3, STAT4 and STAT5
PMID: 18163952, 10878008, 10523304
some studies have shown p38α is phosphorylated and activated in a type-I-IFN-dependent manner in several IFN-sensitive cell lines.
PMID: 18163952, 10878008, 10523304
some studies have shown p38α is phosphorylated and activated in a type-I-IFN-dependent manner in several IFN-sensitive cell lines.
indirect
PMID: 18163952, 15864272
The PI3K-signaling cascade also regulates IFN inducible activation of the mammalian target of rapamycin (mTOR), via Akt, which mediates the initiation of mRNA translation
indirect
PMID: 18163952, 15864272
The PI3K-signaling cascade also regulates IFN inducible activation of the mammalian target of rapamycin (mTOR), via Akt, which mediates the initiation of mRNA translation
indirect
PMID: 18163952, 15864272
The PI3K-signaling cascade also regulates IFN inducible activation of the mammalian target of rapamycin (mTOR), via Akt, which mediates the initiation of mRNA translation
PMID: 18163952, 15864272
The PI3K-signaling cascade also regulates IFN inducible activation of the mammalian target of rapamycin (mTOR), via Akt, which mediates the initiation of mRNA translation
indirect
PMID: 18163952, 15864272
The PI3K-signaling cascade also regulates IFN inducible activation of the mammalian target of rapamycin (mTOR), via Akt, which mediates the initiation of mRNA translation
indirect
PMID: 18163952, 9238507
C/EBP-β also regulates IL-6 and IL-6-induced expression of the cytokines IL-1, IL-8, tumor necrosis factor-α (TNF-α), and granulocyte colony-stimulating factor (G-CSF), as well acute phase response proteins such as α1-acid glycoprotein, α2-microglobulin, and C-reactive protein
PMID: 18163952, 9238507
C/EBP-β also regulates IL-6 and IL-6-induced expression of the cytokines IL-1, IL-8, tumor necrosis factor-α (TNF-α), and granulocyte colony-stimulating factor (G-CSF), as well acute phase response proteins such as α1-acid glycoprotein, α2-microglobulin, and C-reactive protein
PMID: 18163952, 9238507
C/EBP-β also regulates IL-6 and IL-6-induced expression of the cytokines IL-1, IL-8, tumor necrosis factor-α (TNF-α), and granulocyte colony-stimulating factor (G-CSF), as well acute phase response proteins such as α1-acid glycoprotein, α2-microglobulin, and C-reactive protein
PMID: 18163952, 9238507
C/EBP-β also regulates IL-6 and IL-6-induced expression of the cytokines IL-1, IL-8, tumor necrosis factor-α (TNF-α), and granulocyte colony-stimulating factor (G-CSF), as well acute phase response proteins such as α1-acid glycoprotein, α2-microglobulin, and C-reactive protein
PMID: 18163952, 9238507
C/EBP-β also regulates IL-6 and IL-6-induced expression of the cytokines IL-1, IL-8, tumor necrosis factor-α (TNF-α), and granulocyte colony-stimulating factor (G-CSF), as well acute phase response proteins such as α1-acid glycoprotein, α2-microglobulin, and C-reactive protein
PMID: 18163952, 9238507
C/EBP-β also regulates IL-6 and IL-6-induced expression of the cytokines IL-1, IL-8, tumor necrosis factor-α (TNF-α), and granulocyte colony-stimulating factor (G-CSF), as well acute phase response proteins such as α1-acid glycoprotein, α2-microglobulin, and C-reactive protein
PMID: 18163952, 9238507
C/EBP-β also regulates IL-6 and IL-6-induced expression of the cytokines IL-1, IL-8, tumor necrosis factor-α (TNF-α), and granulocyte colony-stimulating factor (G-CSF), as well acute phase response proteins such as α1-acid glycoprotein, α2-microglobulin, and C-reactive protein
PMID: 18163952, 8321203, 8552662, 9121452, 11238899
C/EBP-β can interact with transcription factors outside its family, such as NF-κB (84), retinoblastoma (pRb) tumor suppressor protein (85), Sp1 (86), STAT3 (87) to regulate cellular functions.
PMID: 18163952, 8321203, 8552662, 9121452, 11238899
C/EBP-β can interact with transcription factors outside its family, such as NF-κB (84), retinoblastoma (pRb) tumor suppressor protein (85), Sp1 (86), STAT3 (87) to regulate cellular functions.
PMID: 18163952, 7959007, 8756629, 8552662, 9121452
C/EBP-β binds to a variety of response elements and forms heteromeric complexes with other transcription factors, such as pRb, NF-κB, Sp1, Myb and PU.1
PMID: 18163952, 8321203, 8552662, 9121452, 11238899
C/EBP-β can interact with transcription factors outside its family, such as NF-κB (84), retinoblastoma (pRb) tumor suppressor protein (85), Sp1 (86), STAT3 (87) to regulate cellular functions.
PMID: 18163952, 7959007, 8756629, 8552662, 9121452
C/EBP-β binds to a variety of response elements and forms heteromeric complexes with other transcription factors, such as pRb, NF-κB, Sp1, Myb and PU.1
PMID: 18163952, 8321203, 8552662, 9121452, 11238899
C/EBP-β can interact with transcription factors outside its family, such as NF-κB (84), retinoblastoma (pRb) tumor suppressor protein (85), Sp1 (86), STAT3 (87) to regulate cellular functions.
PMID: 18163952, 7959007, 8756629, 8552662, 9121452
C/EBP-β binds to a variety of response elements and forms heteromeric complexes with other transcription factors, such as pRb, NF-κB, Sp1, Myb and PU.1
PMID: 18163952, 1934061
LIP dominantly inhibits the transcriptional activity of the full-length C/EBP-beta by dimerizing with it.
PMID: 18163952, 1547942
It can form heterodimers with C/EBP-α and C/EBP-β, and attenuate their transcriptional activity
PMID: 18163952, 1547942
It can form heterodimers with C/EBP-α and C/EBP-β, and attenuate their transcriptional activity
indirect
PMID: 18163952, 2112087
LPS, IL-6, IL-1, dexamethasone, and glucagon can strongly up-regulate the expression of C/EBP-β
indirect
PMID: 18163952, 2112087
LPS, IL-6, IL-1, dexamethasone, and glucagon can strongly up-regulate the expression of C/EBP-β
indirect
PMID: 18163952, 2112087
LPS, IL-6, IL-1, dexamethasone, and glucagon can strongly up-regulate the expression of C/EBP-β
indirect
PMID: 18163952, 2112087
LPS, IL-6, IL-1, dexamethasone, and glucagon can strongly up-regulate the expression of C/EBP-β
indirect
PMID: 18163952, 10777554
We have shown that IFN-γ not only induces the expression of C/EBP-β but also enhances its transcriptional activity
indirect
PMID: 18163952, 2112087
LPS, IL-6, IL-1, dexamethasone, and glucagon can strongly up-regulate the expression of C/EBP-β
PMID: 18163952, 8336793, 8384717, 10635333, 11684016
Posttranscriptional modifications of C/EBP by protein kinases PKA, PKC,ribosomal S6 kinase (RSK), and extracellular signal-related kinase (ERK) appear to modulate its activity in different cells
PMID: 18163952, 8336793, 8384717, 10635333, 11684016
Posttranscriptional modifications of C/EBP by protein kinases PKA, PKC,ribosomal S6 kinase (RSK), and extracellular signal-related kinase (ERK) appear to modulate its activity in different cells
PMID: 18163952, 8336793, 8384717, 10635333, 11684016
Posttranscriptional modifications of C/EBP by protein kinases PKA, PKC,ribosomal S6 kinase (RSK), and extracellular signal-related kinase (ERK) appear to modulate its activity in different cells
PMID: 18163952, 8336793, 8384717, 10635333, 11684016
Posttranscriptional modifications of C/EBP by protein kinases PKA, PKC,ribosomal S6 kinase (RSK), and extracellular signal-related kinase (ERK) appear to modulate its activity in different cells
PMID: 18163952, 10777554, 11312260
We have shown that C/EBP-β binds to GATE and stimulates transcription
PMID: 18163952, 10777554, 11312260
We have shown that C/EBP-β binds to GATE and stimulates transcription
PMID: 18163952, 7959007, 8756629, 8552662, 9121452
C/EBP-β binds to a variety of response elements and forms heteromeric complexes with other transcription factors, such as pRb, NF-κB, Sp1, Myb and PU.1
PMID: 18163952, 7959007, 8756629, 8552662, 9121452
C/EBP-β binds to a variety of response elements and forms heteromeric complexes with other transcription factors, such as pRb, NF-κB, Sp1, Myb and PU.1
PMID: 18163952, 11004486
IL-6 induces IRF-9 gene expression through GATE using C/EBP-β
indirect
PMID: 18163952, 1888886
IL-6 induces the expression of 2-5A synthetase and MHC class I genes
indirect
PMID: 18163952, 1888886
IL-6 induces the expression of 2-5A synthetase and MHC class I genes
PMID: 18163952, 11057895
Ras activation is dependent on the recruitment of the adaptor proteins Grb and Sos to the growth factor receptors
PMID: 18163952, 11057895
Ras activation is dependent on the recruitment of the adaptor proteins Grb and Sos to the growth factor receptors
indirect
PMID: 18163952
Raf, a serine-threonine kinase, responds to Ras and phosphorylates MAP kinase kinase 1 (MEK1).
PMID: 18163952
Raf, a serine-threonine kinase, responds to Ras and phosphorylates MAP kinase kinase 1 (MEK1).
PMID: 18163952
MEK1, a dual specificity kinase, phosphorylates at the conserved threonine and tyrosine residues present in the activation loop of ERKs: ERK1 (p44) and ERK2 (p42).
PMID: 18163952
MEK1, a dual specificity kinase, phosphorylates at the conserved threonine and tyrosine residues present in the activation loop of ERKs: ERK1 (p44) and ERK2 (p42).
PMID: 18163952
ERKs1/2 are known to phosphorylate members of the AP1 family, such as Elk1, Egr1, Fos, and Jun.
PMID: 18163952
ERKs1/2 are known to phosphorylate members of the AP1 family, such as Elk1, Egr1, Fos, and Jun.
PMID: 18163952
ERKs1/2 are known to phosphorylate members of the AP1 family, such as Elk1, Egr1, Fos, and Jun.
PMID: 18163952
ERKs1/2 are known to phosphorylate members of the AP1 family, such as Elk1, Egr1, Fos, and Jun.
PMID: 18163952
ERKs1/2 are known to phosphorylate members of the AP1 family, such as Elk1, Egr1, Fos, and Jun.
PMID: 18163952
ERKs1/2 are known to phosphorylate members of the AP1 family, such as Elk1, Egr1, Fos, and Jun.
PMID: 18163952
ERKs1/2 are known to phosphorylate members of the AP1 family, such as Elk1, Egr1, Fos, and Jun.
PMID: 18163952
ERKs1/2 are known to phosphorylate members of the AP1 family, such as Elk1, Egr1, Fos, and Jun.
indirect
PMID: 18163952, 9199317, 9668040
Raf activation by IFN-γ and IFN-β has been reported
indirect
PMID: 18163952, 9199317, 9668040
Raf activation by IFN-γ and IFN-β has been reported
indirect
PMID: 18163952, 9305638
Rho and Rac, the G proteins similar to Ras, are activated first
indirect
PMID: 18163952, 9305638
Rho and Rac, the G proteins similar to Ras, are activated first
indirect
PMID: 18163952, 9305638
Rho and Rac, the G proteins similar to Ras, are activated first
indirect
PMID: 18163952
These G-proteins then activate MAP kinase kinase kinases (MEKKs)
indirect
PMID: 18163952
These G-proteins then activate MAP kinase kinase kinases (MEKKs)
indirect
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
indirect
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
indirect
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
indirect
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
PMID: 18163952
MEKKs then activate stress responsive kinases, such as the various isoforms of p38 MAPK (α, β, γ, δ) and c-Jun N-terminal kinases (JNK), using the intermediate enzymes
SEK1/2.
indirect
PMID: 18163952, 12048245
Instead of Raf, MEKK1 was required for IFN-γ-induced ERK activation and the induction IRF-9 gene
indirect
PMID: 18163952, 12048245
Instead of Raf, MEKK1 was required for IFN-γ-induced ERK activation and the induction IRF-9 gene
indirect
PMID: 18163952, 12048245
Instead of Raf, MEKK1 was required for IFN-γ-induced ERK activation and the induction IRF-9 gene
PMID: 18163952, 10969079
This domain acts as a scaffold for the binding of MEK1 and ERK1/2, which permits the juxtaposition of the kinases and their activation.
PMID: 18163952, 7624324
MEKK1 phosphorylates MEK1 on the same residue as does Raf
indirect
PMID: 18163952, 10346818, 9689078, 10805784
MEKK1 is also required for the activation of NF-κB and c-Jun N-terminal kinases
indirect
PMID: 18163952, 10346818, 9689078, 10805784
MEKK1 is also required for the activation of NF-κB and c-Jun N-terminal kinases
indirect
PMID: 18163952, 10747925
It also plays a major role in IFN-β gene induction
indirect
PMID: 18163952, 14759369
One recent study showed that Ras induces phosphorylation of C/EBP-β and activated C/EBP-β interacts with the transcriptional
mediator complex
PMID: 18163952, 14759369
One recent study showed that Ras induces phosphorylation of C/EBP-β and activated C/EBP-β interacts with the transcriptional mediator complex
indirect
PMID: 18163952, 12050152
GATE also binds another transcriptional activator, GBF1, in response to IFN-γ
indirect
PMID: 18163952, 10657627
CRKL is tyrosine phosphorylated during IFN-treatment
indirect
PMID: 18163952
Mutation of this motif and/or interference with the ERK1/2 activation prevented the IFN-γ-induced association between GBF1 and C/EBP-β.
PMID: 18163952, 15879117
Our subsequent studies have shown that GBF1 recruitment to the IRF-9 promoter is dependent on C/EBP-β.
PMID: 18163952, 10799501
Signal induced binding of Cdc42/Rac to the CRIB causes MLK dimerization, leading to their autophosphorylation
PMID: 18163952, 10799501
Signal induced binding of Cdc42/Rac to the CRIB causes MLK dimerization, leading to their autophosphorylation
PMID: 18163952, 10799501
Signal induced binding of Cdc42/Rac to the CRIB causes MLK dimerization, leading to their autophosphorylation
indirect
PMID: 18163952, 9003778, 11432832
MLKs function as MKKKs and have been implicated in the activation of JNK and SEK1 and transcription factor NF-κB
indirect
PMID: 18163952, 9003778, 11432832
MLKs function as MKKKs and have been implicated in the activation of JNK and SEK1 and transcription factor NF-κB
indirect
PMID: 18163952, 9003778, 11432832
MLKs function as MKKKs and have been implicated in the activation of JNK and SEK1 and transcription factor NF-κB
indirect
PMID: 18163952, 9003778, 11432832
MLKs function as MKKKs and have been implicated in the activation of JNK and SEK1 and transcription factor NF-κB
indirect
PMID: 18163952
co-expression of MLK3, but not MLK2, significantly stimulated the IFN-γ-induced expression of IRF-9.
PMID: 18163952, 15314150
One likely candidate is Cdk2, which phosphorylates C/EBP-β in vitro at S64 and T189
PMID: 18163952, 8755534
IFN-γ treatment has been shown to cause a decrease in Cdk2 activity
PMID: 18163952
IFN-γ treatment decreased S64 phosphorylation. Surprisingly, MLK3 caused a decrease in phosphorylation of C/EBP-β instead of its stimulation in an IFN-γ dependent manner.