TMEM126A, a CD137 ligand binding protein, couples with the TLR4 signal transduction pathway in macrophages

2015 ◽  
Vol 64 (2) ◽  
pp. 244-251 ◽  
Author(s):  
Eun-Cheol Kim ◽  
Ji-Hoi Moon ◽  
Sang W. Kang ◽  
Byungsuk Kwon ◽  
Hyeon-Woo Lee
Keyword(s):  
Signal Transduction ◽  
Ligand Binding ◽  
Binding Protein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway

The mRNA 5' cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transformation of primary rodent fibroblasts

1992 ◽  
Vol 12 (3) ◽  
pp. 1234-1238
Author(s):  
A Lazaris-Karatzas ◽  
N Sonenberg
Keyword(s):  
Signal Transduction ◽  
Binding Protein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Rat Embryo ◽  
Present Evidence ◽  
P21 Ras ◽  
Embryo Fibroblasts ◽  
Common Signal

We present evidence that eIF-4E, the mRNA 5' cap-binding protein, cooperates with two immortalizing oncogenes, v-myc and E1A, to cause transformation of rat embryo fibroblasts. eIF-4E alone can transform rat embryo fibroblasts when selection is applied. The pattern of transformation by eIF-4E is similar to that of p21 Ras, raising the possibility that eIF-4E shares a common signal transduction pathway with p21 Ras.

scholarly journals The mRNA 5' cap-binding protein, eIF-4E, cooperates with v-myc or E1A in the transformation of primary rodent fibroblasts.

1992 ◽  
Vol 12 (3) ◽  
pp. 1234-1238 ◽  
Author(s):  
A Lazaris-Karatzas ◽  
N Sonenberg
Keyword(s):  
Signal Transduction ◽  
Binding Protein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Rat Embryo ◽  
Present Evidence ◽  
P21 Ras ◽  
Embryo Fibroblasts ◽  
Common Signal

We present evidence that eIF-4E, the mRNA 5' cap-binding protein, cooperates with two immortalizing oncogenes, v-myc and E1A, to cause transformation of rat embryo fibroblasts. eIF-4E alone can transform rat embryo fibroblasts when selection is applied. The pattern of transformation by eIF-4E is similar to that of p21 Ras, raising the possibility that eIF-4E shares a common signal transduction pathway with p21 Ras.

scholarly journals Regulation of the mRNA-binding Protein AUF1 by Activation of the -Adrenergic Receptor Signal Transduction Pathway

1996 ◽  
Vol 271 (14) ◽  
pp. 8493-8501 ◽  
Author(s):  
Aldo Pende ◽  
Kelli D. Tremmel ◽  
Christine T. DeMaria ◽  
Burns C. Blaxall ◽  
Wayne A. Minobe ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Adrenergic Receptor ◽  
Binding Protein ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Receptor Signal ◽  
Mrna Binding Protein ◽  
Mrna Binding

scholarly journals The Phosphate-Binding Protein of Escherichia coliIs Not Essential for Pi-Regulated Expression of thepho Regulon

2001 ◽  
Vol 183 (19) ◽  
pp. 5768-5771 ◽  
Author(s):  
Sally M. Hoffer ◽  
Jan Tommassen
Keyword(s):  
Escherichia Coli ◽  
Signal Transduction ◽  
Binding Protein ◽  
Constitutive Expression ◽  
Signal Transduction Pathway ◽  
Transduction Pathway ◽  
Phosphate Binding ◽  
Essential Component ◽  
Regulated Expression ◽  
Phosphate Binding Protein

ABSTRACT Disruption of pstS encoding the Pi-binding protein in Escherichia coli generally leads to the constitutive expression of thepho regulon. We demonstrate that Pi-controlled expression is restored when the activity of the Pitransporter PitA or PitB is increased. Apparently, PstS is not an essential component of the signal transduction pathway.

Sign in / Sign up

Export Citation Format

Share Document