Discovery of LRE1 as a specific and allosteric inhibitor of soluble adenylyl cyclase

被引:0
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作者
Lavoisier Ramos-Espiritu
Silke Kleinboelting
Felipe A Navarrete
Antonio Alvau
Pablo E Visconti
Federica Valsecchi
Anatoly Starkov
Giovanni Manfredi
Hannes Buck
Carolina Adura
Jonathan H Zippin
Joop van den Heuvel
J Fraser Glickman
Clemens Steegborn
Lonny R Levin
Jochen Buck
机构
[1] Weill Cornell Medical College,Department of Pharmacology
[2] The High-Throughput Screening and Spectroscopy Resource Center,Department of Biochemistry
[3] The Rockefeller University,Department of Veterinary and Animal Science
[4] University of Bayreuth,Department of Dermatology
[5] University of Massachusetts,undefined
[6] Brain and Mind Research Institute,undefined
[7] Weill Cornell Medical College,undefined
[8] Weill Cornell Medical College,undefined
[9] Helmholtz Zentrum fur Infektionsforschung,undefined
来源
Nature Chemical Biology | 2016年 / 12卷
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摘要
A high-throughput screen using a mass-spectrometry-based assay results in the identification of LRE1 as an inhibitor of HCO3−/Ca2+-regulated soluble adenylyl cyclase activity. LRE1 interacts with the HCO3− binding site (BBS) to block cAMP formation.[graphic not available: see fulltext]
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页码:838 / 844
页数:6
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