Characterization of the Mouse Interleukin 3 Receptor System

1989 ◽  
pp. 87-93 ◽  
Author(s):  
ATSUSHI MIYAJIMA ◽  
HOLANDA SCHREURS ◽  
HUEY-MEI WANG ◽  
KAZUO MARUYAMA ◽  
DAN GORMAN ◽  
...  
Keyword(s):  
Receptor System ◽  
Interleukin 3

scholarly journals Characterization of three related murine interleukin-3 surface receptor proteins

1991 ◽  
Vol 266 (7) ◽  
pp. 4151-4158
Author(s):  
D A Stevens ◽  
J Schreurs ◽  
J N Ihle ◽  
W S May
Keyword(s):  
Receptor Proteins ◽  
Interleukin 3 ◽  
Surface Receptor

Characterization of a human multilineage-colony-stimulating factor cDNA clone identified by a conserved noncoding sequence in mouse interleukin-3

Gene ◽  
1987 ◽  
Vol 55 (1) ◽  
pp. 115-124 ◽  
Author(s):  
Lambert Dorssers ◽  
Herman Burger ◽  
Freek Bot ◽  
Ruud Delwel ◽  
Ad H.M.Geurts van Kessel ◽  
...  
Keyword(s):  
Cdna Clone ◽  
Noncoding Sequence ◽  
Colony Stimulating Factor ◽  
Interleukin 3 ◽  
Stimulating Factor

scholarly journals Characterization of the Mouse IFN-λ Ligand-Receptor System: IFN-λs Exhibit Antitumor Activity against B16 Melanoma

2006 ◽  
Vol 66 (8) ◽  
pp. 4468-4477 ◽  
Author(s):  
Ahmed Lasfar ◽  
Anita Lewis-Antes ◽  
Sergey V. Smirnov ◽  
Shubha Anantha ◽  
Walid Abushahba ◽  
...  
Keyword(s):  
Antitumor Activity ◽  
B16 Melanoma ◽  
Receptor System

scholarly journals Characterization of murine peritoneal macrophage receptors for fibrin(ogen) degradation products

Blood ◽  
1986 ◽  
Vol 67 (5) ◽  
pp. 1224-1228 ◽  
Author(s):  
S Rajagopalan ◽  
SV Pizzo
Keyword(s):  
Degradation Products ◽  
Peritoneal Macrophages ◽  
Receptor System ◽  
Human Fibrinogen ◽  
Murine Peritoneal Macrophage ◽  
High Affinity ◽  
Macrophage Receptors ◽  
Low Concentrations ◽  
Mouse Peritoneal Macrophages

Abstract The binding of human fibrinogen degradation fragments D1, E, X, and Y, as well as fibrin fragment D1 dimer, to mouse peritoneal macrophages was examined. A Scatchard plot of fragment D1 binding was biphasic, suggesting two classes of receptors. Fragments D1, D1 dimer, X, and Y in low concentrations bound to macrophages with high affinity (Kd = 23 to 73 X 10(-11) mol/L). Fragment E bound specifically but at a much lower level than the other fragments. Fragment D1 was able to compete for the binding of radiolabeled fragments X and Y but not radiolabeled fragment E. These studies indicate that fragments D and E are recognized by separate receptor systems but that all of the fibrinogen degradation products that contain the D domain are recognized by the same receptor system.

Structural characterization of the parathyroid hormone receptor domains determinant for ligand binding

2007 ◽  
Vol 35 (4) ◽  
pp. 721-723 ◽  
Author(s):  
D.F. Mierke ◽  
L. Mao ◽  
M. Pellegrini ◽  
A. Piserchio ◽  
J. Plati ◽  
...  
Keyword(s):  
Parathyroid Hormone ◽  
G Protein Coupled Receptors ◽  
Peptide Ligands ◽  
Receptor Complex ◽  
Receptor Model ◽  
Receptor System ◽  
Parathyroid Hormone Receptor ◽  
Contact Points ◽  
G Protein Coupled

Over the years, the association of peptide ligands to Family B GPCRs (G-protein coupled receptors) has been characterized by a number of experimental and theoretical techniques. For the PTH (parathyroid hormone) ligand–receptor system, important insight has been provided by photoaffinity labelling experiments and the elucidation of direct contact points between ligand and receptor. Our research has focused on the structural elucidation of the receptor domains shown to be involved in the binding of PTH. Employing a combination of carefully designed receptor domains, solution-state NMR carried out in the presence of membrane mimetics and extensive computer simulations, we have obtained a well-resolved model of the ligand–receptor complex for PTH. Here, we review the development of this model and highlight some inherent limitations of the methods employed and their consequences on interpretation of the ligand–receptor model.

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