Aberrant hippocampal spine morphology and impaired memory formation in neuronal platelet-derived growth factor beta-receptor lacking mice

Hippocampus ◽  
2011 ◽  
Vol 22 (6) ◽  
pp. 1371-1378 ◽  
Author(s):  
Norifumi Shioda ◽  
Shigeki Moriguchi ◽  
Takeshi Oya ◽  
Yoko Ishii ◽  
Jie Shen ◽  
...  
Keyword(s):  
Growth Factor ◽  
Memory Formation ◽  
Platelet Derived Growth Factor ◽  
Spine Morphology ◽  
Impaired Memory ◽  
Beta Receptor ◽  
Growth Factor Beta

scholarly journals Direct interaction between Shc and the platelet-derived growth factor beta-receptor.

1994 ◽  
Vol 269 (21) ◽  
pp. 15337-15343
Author(s):  
K. Yokote ◽  
S. Mori ◽  
K. Hansen ◽  
J. McGlade ◽  
T. Pawson ◽  
...  
Keyword(s):  
Growth Factor ◽  
Direct Interaction ◽  
Platelet Derived Growth Factor ◽  
Beta Receptor ◽  
Growth Factor Beta

scholarly journals Inhibition of glioma cell growth by a truncated platelet-derived growth factor-beta receptor.

1994 ◽  
Vol 269 (33) ◽  
pp. 21215-21222
Author(s):  
L.M. Strawn ◽  
E. Mann ◽  
S.S. Elliger ◽  
L.M. Chu ◽  
L.L. Germain ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cell Growth ◽  
Glioma Cell ◽  
Platelet Derived Growth Factor ◽  
Beta Receptor ◽  
Growth Factor Beta

A Novel Monoclonal Antibody Dependent on Domain 5 of the Platelet-Derived Growth Factor Beta Receptor Inhibits Ligand Binding and Receptor Activation

1993 ◽  
Vol 8 (4) ◽  
pp. 253-265 ◽  
Author(s):  
Vanitha Ramakrishnan ◽  
Maria-Amelia Escobedo ◽  
Larry J Fretto ◽  
Joseph J Seroogy ◽  
James E Tomlinson ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Growth Factor ◽  
Ligand Binding ◽  
Receptor Activation ◽  
Platelet Derived Growth Factor ◽  
Beta Receptor ◽  
Growth Factor Beta

scholarly journals Interactions between SH2 domains and tyrosine-phosphorylated platelet-derived growth factor beta-receptor sequences: analysis of kinetic parameters by a novel biosensor-based approach.

1993 ◽  
Vol 13 (6) ◽  
pp. 3567-3576 ◽  
Author(s):  
G Panayotou ◽  
G Gish ◽  
P End ◽  
O Truong ◽  
I Gout ◽  
...  
Keyword(s):  
Growth Factor ◽  
Kinetic Parameters ◽  
Protein Tyrosine Kinase ◽  
Platelet Derived Growth Factor ◽  
Phosphatidylinositol 3 Kinase ◽  
High Association ◽  
Sh2 Domains ◽  
Beta Receptor ◽  
Growth Factor Beta ◽  
Phosphatidylinositol 3

The interaction between SH2 domains and phosphotyrosine-containing sequences was examined by real-time measurements of kinetic parameters. The SH2 domains of the p85 subunit of the phosphatidylinositol 3-kinase as well as of other signaling molecules were expressed in bacteria as glutathione S-transferase fusion proteins. Phosphotyrosine-containing peptides, corresponding to two autophosphorylation sites on the human platelet-derived growth factor beta-receptor that are responsible for phosphatidylinositol 3-kinase binding, were synthesized and used as capturing molecules, immobilized on a biosensor surface. The association and dissociation rate constants for binding to both sites were determined for intact p85 and the recombinant SH2 domains. High association rates were found to be coupled to very fast dissociation rates for all interactions studied. A binding specificity was observed for the two SH2 domains of p85, with the N-terminal SH2 binding with high affinity to the Tyr-751 site but not to the Tyr-740 site, and the C-terminal SH2 interacting strongly with both sites. This approach should be generally applicable to the study of the specificity inherent in the assembly of signaling complexes by activated protein-tyrosine kinase receptors.

Ligand-based computational modelling of platelet-derived growth factor beta receptor leading to new angiogenesis inhibitory leads

2017 ◽  
Vol 71 ◽  
pp. 170-179 ◽  
Author(s):  
Rua’a A. Al-Aqtash ◽  
Malek A. Zihlif ◽  
Hana Hammad ◽  
Zeyad D. Nassar ◽  
Jehad Al Meliti ◽  
...  
Keyword(s):  
Growth Factor ◽  
Computational Modelling ◽  
Platelet Derived Growth Factor ◽  
Beta Receptor ◽  
Growth Factor Beta
Sign in / Sign up

Export Citation Format

Share Document