The molecular basis for the inhibition of phosphodiesterase-4D by three natural resveratrol analogs. Isolation, molecular docking, molecular dynamics simulations, binding free energy, and bioassay-Reference-Cited by-同舟云学术

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The molecular basis for the inhibition of phosphodiesterase-4D by three natural resveratrol analogs. Isolation, molecular docking, molecular dynamics simulations, binding free energy, and bioassay

Published:2013-10 Issue:10 Volume:1834 Page:2089-2096
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Zhao Peng,Chen Shang-Ke,Cai Ying-Hong,Lu Xiao,Li Zhe,Cheng Yuen-Kit,Zhang Cuixian,Hu Xiaopeng,He Xixin,Luo Hai-Bin

Funder

Natural Science Foundation of China

Guangdong Natural Science Foundation

Fundamental Research Funds for the Central Universities

Guangdong Provincial Key Laboratory of Construction Foundation

Guangdong Science Foundation

Science Foundation of Department of Education in Guangdong Province

Scientific Research foundation for Returned Overseas Chinese Scholars of Ministry of Education

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference34 articles.

1. Cyclic nucleotide phosphodiesterase (PDE) superfamily: a new target for the development of specific therapeutic agents;Lugnier;Pharmacol. Therapeut.,2006

2. Cyclic nucleotide phosphodiesterases: molecular regulation to clinical use;Bender;Pharmacol. Rev.,2006

3. Overview of PDEs and their regulation;Omori;Circ. Res.,2007

4. Biochemistry and physiology of cyclic nucleotide phosphocliesterases: essential components in cyclic nucleotide signaling;Conti;Annu. Rev. Biochem.,2007

5. Crystal structures of phosphodiesterases and implications on substrate specificity and inhibitor selectivity;Ke;Curr. Top. Med. Chem.,2007

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