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PMID: 15075353, 12086290, 11177775
COX-2 is an enzyme that converts arachidonic acid into proinflammatory prostaglandins.
indirect
PMID: 15075353, 12010565, 11817610, 11040455, 10517187
MMP-13 is a TNF-{alpha}-induced collagenase that has been implicated in proinflammatory, angiogenic, and destructive processes within the joint of patients with rheumatoid arthritis.
PMID: 15075353, 12767518, 12060661, 14516792, 12937622, 12852754, 12874238
pharmacological inhibitors of p38MAPK prevent the expression of TNF-{alpha}, COX-2, MMP-13, and other proinflammatory proteins.
indirect
PMID: 15075353, 10330172, 10751406, 11279239, 9703499
TTP is a zinc-finger protein that promotes the degradation of TNF-{alpha} transcripts.
indirect
PMID: 15075353, 9703499
In macrophages, its induction by lipopolysaccharide (LPS) appears to prevent the pathological overexpression of this proinflammatory cytokine.
PMID: 15075353, 9703499
In macrophages, its induction by lipopolysaccharide (LPS) appears to prevent the pathological overexpression of this proinflammatory cytokine.
indirect
PMID: 15075353, 9703499
In macrophages, its induction by lipopolysaccharide (LPS) appears to prevent the pathological overexpression of this proinflammatory cytokine.
indirect
PMID: 15075353, 10921895, 11762949
LPS-activated macrophages derived from wild-type and TIA-1–/– mice express similar amounts of TNF-{alpha} transcripts, macrophages lacking TIA-1 produce significantly more TNF-{alpha} protein than wild-type controls.
indirect
PMID: 15075353, 10921895, 11762949
LPS-activated macrophages derived from wild-type and TIA-1–/– mice express similar amounts of TNF-{alpha} transcripts, macrophages lacking TIA-1 produce significantly more TNF-{alpha} protein than wild-type controls.
PMID: 15075353, 12767518, 12060661, 14516792, 12937622, 12852754, 12874238
pharmacological inhibitors of p38MAPK prevent the expression of TNF-{alpha}, COX-2, MMP-13, and other proinflammatory proteins.
PMID: 15075353, 10557102, 10655230, 10882126, 11106749
Stress-induced translational arrest is characterized by the activation of one or more members of a family of serine/threonine kinases [e.g., double-stranded RNA-dependent protein kinase R (PKR), PKR-like endoplasmic reticulum kinase (PERK), GCN2.
PMID: 15075353, 10557102, 10655230, 10882126, 11106749
Stress-induced translational arrest is characterized by the activation of one or more members of a family of serine/threonine kinases [e.g., double-stranded RNA-dependent protein kinase R (PKR), PKR-like endoplasmic reticulum kinase (PERK), GCN2.
PMID: 15075353, 10557102, 10655230, 10882126, 11106749
Stress-induced translational arrest is characterized by the activation of one or more members of a family of serine/threonine kinases [e.g., double-stranded RNA-dependent protein kinase R (PKR), PKR-like endoplasmic reticulum kinase (PERK), GCN2.
PMID: 15075353, 11909525
These kinases phosphorylate eukaryotic initiation factor 2{alpha} (eIF2{alpha}), a component of the ternary complex that loads tRNAiMet onto the small ribosomal subunit to initiate protein synthesis
PMID: 15075353, 11909525
These kinases phosphorylate eukaryotic initiation factor 2{alpha} (eIF2{alpha}), a component of the ternary complex that loads tRNAiMet onto the small ribosomal subunit to initiate protein synthesis
PMID: 15075353, 11909525
These kinases phosphorylate eukaryotic initiation factor 2{alpha} (eIF2{alpha}), a component of the ternary complex that loads tRNAiMet onto the small ribosomal subunit to initiate protein synthesis
PMID: 15075353, 11438658
Phosphorylation of eIF2{alpha} inhibits protein translation by reducing the availability of an active ternary complex.
PMID: 15075353, 11546803
In extracts of 293 cells, calf intestinal alkaline phosphatase-induced dephosphorylation of recombinant TTP increases its affinity for AREs.
PMID: 15075353, 11546803, 11533235
One of the candidate substrates for p38MAPK is TTP.
PMID: 15075353
We found that MK2-induced phosphorylation of TTP results in the assembly of 14-3-3:TTP complexes, which are actively excluded from SGs.
PMID: 15075353
We identified serine residues 52 and 178 as sites that are phosphorylated following p38MAPK/MK2 activation to create 14-3-3-binding sites.
PMID: 15075353, 12010565, 11817610, 11040455, 10517187
MMP-13 is a TNF-{alpha}-induced collagenase that has been implicated in proinflammatory, angiogenic, and destructive processes within the joint of patients with rheumatoid arthritis.
PMID: 15075353, 12767518, 12060661, 14516792, 12937622, 12852754, 12874238
pharmacological inhibitors of p38MAPK prevent the expression of TNF-{alpha}, COX-2, MMP-13, and other proinflammatory proteins.
PMID: 15075353
TIA-1 interacts with specific components of the initiation complex that are assembled at the 5'-end of the transcript.