Ligand-Induced Conformational Changes in Cyclic Nucleotide Phosphodiesterases and Cyclic Nucleotide-Dependent Protein Kinases

Methods ◽  
1998 ◽  
Vol 14 (1) ◽  
pp. 81-92 ◽  
Author(s):  
Sharron H. Francis ◽  
Der-Ming Chu ◽  
Melissa K. Thomas ◽  
Alfreda Beasley ◽  
Kennard Grimes ◽  
...  
1979 ◽  
Vol 28 (8) ◽  
pp. 1307-1312 ◽  
Author(s):  
Richard G. van Inwegen ◽  
Phyllis Salaman ◽  
Vassil St. Georgiev ◽  
Ira Weinryb

1982 ◽  
Vol 257 (19) ◽  
pp. 11609-11616 ◽  
Author(s):  
T J Torphy ◽  
W B Freese ◽  
G A Rinard ◽  
L L Brunton ◽  
S E Mayer

1969 ◽  
Vol 244 (23) ◽  
pp. 6395-6402 ◽  
Author(s):  
Eishichi Miyamoto ◽  
J.F. Kuo ◽  
Paul Greengard

2002 ◽  
Vol 7 (3) ◽  
pp. 215-222 ◽  
Author(s):  
Wei Huang ◽  
Yan Zhang ◽  
J. Richard Sportsman

Cyclic nucleotide phosphodiesterases (PDEs) catalyze the hydrolysis of the 3′-ester bond of cyclic AMP (cAMP) and cyclic GMP (cGMP), important second messengers in the transduction of a variety of extracellular signals. There is growing interest in the study of PDEs as drug targets for novel therapeutics. We describe the development of a homogeneous fluorescence polarization assay for PDEs based on the strong binding of PDE reaction products (i.e., AMP or GMP) onto modified nanoparticles through interactions with immobilized trivalent metal cations. This assay technology (IMAP) is applicable to both cAMP- and cGMP-specific PDEs. Results of the assay in 384- and 1536-well microplates are presented.


2004 ◽  
Vol 483 (2-3) ◽  
pp. 187-194 ◽  
Author(s):  
Chin-Chung Wu ◽  
Wei-Ya Wang ◽  
Reen-Yen Kuo ◽  
Fang-Rong Chang ◽  
Yang-Chang Wu

Sign in / Sign up

Export Citation Format

Share Document