Agency
National Institute of Health (NIH)
Institute
National Heart, Lung, and Blood Institute (NHLBI)
Type
Research Project (R01)
Project #
5R01HL046451-03
Application #
2222934
Study Section
Pharmacology A Study Section (PHRA)
Project Start
1994-06-01
Project End
1998-03-31
Budget Start
1996-06-01
Budget End
1998-03-31
Support Year
3
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Columbia University (N.Y.)
Department
Pharmacology
Type
Schools of Medicine
DUNS #
167204994
City
New York
State
NY
Country
United States
Zip Code
10032
Jiang, Min; Xu, Xulin; Wang, Yuhong et al. (2009) Dynamic partnership between KCNQ1 and KCNE1 and influence on cardiac IKs current amplitude by KCNE2. J Biol Chem 284:16452-62
Xu, Xulin; Jiang, Min; Hsu, Kai-Ling et al. (2008) KCNQ1 and KCNE1 in the IKs channel complex make state-dependent contacts in their extracellular domains. J Gen Physiol 131:589-603
Xu, Xulin; Recanatini, Maurizio; Roberti, Marinella et al. (2008) Probing the binding sites and mechanisms of action of two human ether-a-go-go-related gene channel activators, 1,3-bis-(2-hydroxy-5-trifluoromethyl-phenyl)-urea (NS1643) and 2-[2-(3,4-dichloro-phenyl)-2,3-dihydro-1H-isoindol-5-ylamino]-nicotinic acid (PD3 Mol Pharmacol 73:1709-21
Tseng, Gea-Ny (2007) The phenotype of a KCNQ1 mutation depends on its KCNE partners: is the cardiac slow delayed rectifier (IKs) channel more than a KCNQ1/KCNE1 complex? Heart Rhythm 4:1542-3
Tseng, Gea-Ny; Sonawane, Kailas D; Korolkova, Yuliya V et al. (2007) Probing the outer mouth structure of the HERG channel with peptide toxin footprinting and molecular modeling. Biophys J 92:3524-40
Liu, Xian-Sheng; Zhang, Mei; Jiang, Min et al. (2007) Probing the interaction between KCNE2 and KCNQ1 in their transmembrane regions. J Membr Biol 216:117-27
Zhang, M; Liu, X-S; Diochot, S et al. (2007) APETx1 from sea anemone Anthopleura elegantissima is a gating modifier peptide toxin of the human ether-a-go-go- related potassium channel. Mol Pharmacol 72:259-68
Wu, Dong-Mei; Jiang, Min; Zhang, Mei et al. (2006) KCNE2 is colocalized with KCNQ1 and KCNE1 in cardiac myocytes and may function as a negative modulator of I(Ks) current amplitude in the heart. Heart Rhythm 3:1469-80
Wu, Dong-Mei; Lai, Ling-Ping; Zhang, Mei et al. (2006) Characterization of an LQT5-related mutation in KCNE1, Y81C: implications for a role of KCNE1 cytoplasmic domain in IKs channel function. Heart Rhythm 3:1031-40
Zhang, M; Liu, J; Jiang, M et al. (2005) Interactions between charged residues in the transmembrane segments of the voltage-sensing domain in the hERG channel. J Membr Biol 207:169-81

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