scholarly journals 2-Position Base-Modified Analogues of Adenophostin A as High-Affinity Agonists of thed-myo-Inositol Trisphosphate Receptor:  In Vitro Evaluation and Molecular Modeling

2008 ◽  
Vol 73 (5) ◽  
pp. 1682-1692 ◽  
Author(s):  
Kana M. Sureshan ◽  
Melanie Trusselle ◽  
Stephen C. Tovey ◽  
Colin W. Taylor ◽  
Barry V. L. Potter
Keyword(s):  
Molecular Modeling ◽  
Inositol Trisphosphate ◽  
In Vitro Evaluation ◽  
Inositol Trisphosphate Receptor ◽  
High Affinity ◽  
Adenophostin A ◽  
Trisphosphate Receptor

scholarly journals Biosynthesis of inositol trisphosphate receptors: selective association with the molecular chaperone calnexin

1999 ◽  
Vol 342 (1) ◽  
pp. 153-161 ◽  
Author(s):  
Suresh K. JOSEPH ◽  
Darren BOEHNING ◽  
Shaila BOKKALA ◽  
Richard WATKINS ◽  
Johan WIDJAJA
Keyword(s):  
Inositol Trisphosphate ◽  
Type I ◽  
Ip3 Receptors ◽  
Inositol Trisphosphate Receptor ◽  
Glucosidase Inhibitor ◽  
Glucosidase Inhibitors ◽  
Glycosylation Sites ◽  
Mechanism Of Interaction ◽  
Trisphosphate Receptor

A prominent labelled polypeptide having the same mobility as type-I inositol trisphosphate receptor (IP3R) was immunoprecipitated from WB-cell lysates by antibodies to calnexin, an ER integral membrane chaperone. The identity of this polypeptide was confirmed by re-immunoprecipitation of the radioactive polypeptides released from calnexin-antibody immunoprecipitates with type-I IP3R antibody. The interaction of calnexin with newly synthesized type-I IP3R was transient and inhibited by treatment of the cells with dithiothreitol or the glucosidase inhibitor N-methyldeoxynojirimicin. In similar experiments, there was no evidence for the binding of type-I IP3R to calreticulin, an ER luminal chaperone. Calnexin (but not calreticulin) associated with newly synthesized FLAG (DYKDDDDK epitope)-tagged type-III IP3R expressed in COS-7 cells. In order to further define the mechanism of interaction of nascent IP3R with chaperones, we have utilized an in vitro rabbit reticulocyte translation assay programmed with RNA templates encoding the six putative transmembrane (TM) domains of IP3Rs. In accordance with the known preference of calnexin for monoglucosylated oligosaccharide chains, calnexin antibody preferentially immunoprecipitated a proportion of glycosylated type-I translation product. Addition of glucosidase inhibitors prevented the association of calnexin with in vitro translated type-I TM construct. Using truncated RNA templates we found that calnexin did not associate with the first four TM domains but retained affinity for the construct encoding TM domains 5 and 6, which contains the glycosylation sites. We propose that calnexin is a key chaperone involved in the folding, assembly and oligomerization of newly synthesized IP3 receptors in the ER.

scholarly journals Synthesis and in vitro evaluation of new fluorinated quinoline derivatives with high affinity for PDE5: Towards the development of new PET neuroimaging probes

2017 ◽  
Vol 136 ◽  
pp. 548-560 ◽  
Author(s):  
Jianrong Liu ◽  
Aurélie Maisonial-Besset ◽  
Barbara Wenzel ◽  
Damien Canitrot ◽  
Ariane Baufond ◽  
...  
Keyword(s):  
Quinoline Derivatives ◽  
In Vitro Evaluation ◽  
High Affinity

scholarly journals Oligomerisation of the Inositol Trisphosphate Receptor Amino-Terminus

2013 ◽  
Vol 104 (2) ◽  
pp. 121a
Author(s):  
Spyros Zissimopoulos ◽  
Jason Marsh ◽  
F. Anthony Lai
Keyword(s):  
Inositol Trisphosphate ◽  
Amino Terminus ◽  
Inositol Trisphosphate Receptor ◽  
Trisphosphate Receptor

Radiosynthesis and in vitro evaluation of 2-(N-alkyl-N-1′-11C-propyl)amino-5-hydroxytetralin analogs as high affinity agonists for dopamine D-2 receptors

1999 ◽  
Vol 26 (7) ◽  
pp. 725-735 ◽  
Author(s):  
Bingzhi Shi ◽  
Tanjore K Narayanan ◽  
Zhi-Ying Yang ◽  
Bradley T Christian ◽  
Jogeshwar Mukherjee
Keyword(s):  
In Vitro Evaluation ◽  
High Affinity ◽  
D 2 Receptors
Sign in / Sign up

Export Citation Format

Share Document