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A conformational transition in the adenylyl cyclase catalytic site yields different binding modes for ribosyl-modified
and unmodified nucleotide inhibitors

Wang, Jenna L. and Guo, Jian-Xin and Zhang, Qi-Yuan and Wu, Jay J.-Q. and Seifert, Roland and Lushington, Gerald H. (2007) A conformational transition in the adenylyl cyclase catalytic site yields different binding modes for ribosyl-modified
and unmodified nucleotide inhibitors.
Bioorganic & Medicinal Chemistry 15 (8), pp. 2993-3002.

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Abstract

Abstract—Adenylyl cyclases (ACs) are promising pharmacological targets for treating heart failure, cancer, and psychosis. Ribosesubstituted nucleotides have been reported as a potent family of AC inhibitors. In silico analysis of the docked conformers of such nucleotides in AC permits assembly of a consistent, intuitive QSAR model with strong correlation relative to measured pKi values. Energy ...

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Item Type:Article
Date:April 2007
Institutions:Chemistry and Pharmacy > Institute of Pharmacy > Pharmacology and Toxicology (Prof. Schlossmann formerly Prof. Seifert)
Identification Number:
ValueType
10.1016/j.bmc.2007.02.014DOI
Subjects:500 Science > 570 Life sciences
600 Technology > 610 Medical sciences Medicine
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Unknown
Owner: Ute Lange
Deposited On:28 Jan 2008 15:11
Last Modified:13 Mar 2014 10:20
Item ID:2666
Owner Only: item control page

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