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MAPK1 — TNFRSF1A
Pathways - manually collected, often from reviews:
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Velarde et al., Am J Physiol 1999
:
BK ( 10 ( -8 ) M ) promoted the association of
p60 ( src ) with the adapter protein growth factor receptor binding protein-2 and also
induced a significant increase in
MAPK activity
Jupp et al., Biochem J 2001
(MAP Kinase Signaling System) :
Conversely, only activation of the
TNFR1 could
stimulate mitogen activated protein kinase ( MAPK ) or p38
MAPK activities in a time dependent manner
Ryden et al., J Biol Chem 2002
:
Use of receptor-specific TNF-alpha mutants showed that activation of
MAPK is entirely
mediated by the
TNFR1 receptor
Mohamed et al., Biochem J 2002
(MAP Kinase Signaling System) :
TNFR1 stimulated p42/44
MAPK and p38 MAPK activities were insensitive to pharmacological caspase inhibition or CrmA
Jupp et al., Biochem J 2003
(MAP Kinase Signaling System) :
TNFR1 activates mitogen activated protein kinase (
MAPK ) and p38MAPK
Itatsu et al., Liver Int 2009
(Cholangiocarcinoma) :
These data suggest that
TNF-alpha/TNF-R1 interaction
leads to the phosphorylation of Erk1/2 and
p38MAPK and nuclear translocation of NF-kappaB, which is closely associated with the production and activation of MMP-9 in cultured CC cells of HuCTT-1 and CCKS-1
Winston et al., J Immunol 1995
:
Activation of
p42mapk/erk2 following engagement of tumor necrosis factor receptor
CD120a ( p55 ) in mouse macrophages ... Collectively, the results from these experiments indicate that cross linking of
CD120a ( p55 ), but not that of CD120b ( p75 ), was both necessary and
sufficient for the activation of
p42mapk/erk2 in mouse macrophages
Riches et al., Immunobiology 1996
:
We have investigated the upstream kinases that mediate the
activation of
p42mapk/erk2 following cross linking of
CD120a ( p55 ) in mouse macrophages