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pro vyhledávání: '"Terence J. Campbell"'
Autor:
Terence J. Campbell
Publikováno v:
Interventional Cardiology and Cardiac Catheterisation ISBN: 9781351060356
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2a2d2223b149160c83b2cc5a6e7d55a2
https://doi.org/10.1201/9781351060356-22
https://doi.org/10.1201/9781351060356-22
Publikováno v:
Biophysical Journal. 92(11):3915-3929
The scorpion toxin CnErg1 binds to human ether-a-go-go related gene (hERG) K(+) channels with a 1:1 stoichiometry and high affinity. However, in contrast to other scorpion toxin-ion channel interactions, the inhibition of macroscopic hERG currents by
Autor:
Mari Kondo, Rajesh N. Subbiah, Catherine E. Clarke, Adam P. Hill, JingTing Zhao, Jamie I. Vandenberg, Terence J. Campbell
Publikováno v:
The Journal of Physiology. 573:291-304
The ether-a-go-go (EAG) family of voltage-gated K+ channels contains three subfamilies, EAG, ether-a-go-go related (ERG) and ether-a-go-go like (ELK). The human ether-a-go-go related gene (hERG) K+ channel has been of significant interest because los
Publikováno v:
The Journal of Physiology. 569:367-379
Inherited mutations or drug-induced block of voltage-gated ion channels, including the human ether-a-go-go-related gene (HERG) K+ channel, are significant causes of malignant arrhythmias and sudden death. The fourth transmembrane domain (S4) of these
Publikováno v:
Clinical and Experimental Pharmacology and Physiology. 31:906-912
SUMMARY 1. In recent years, the identification of the gene defects in a vast array of monogenic disorders has revolutionized our understanding of the basic mechanisms underlying numerous disease processes. 2. Mutations in cardiac ion channels have be
Autor:
Jamie I. Vandenberg, JingTing Zhao, Catherine E. Clarke, Rajesh N. Subbiah, David Smith, Terence J. Campbell
Publikováno v:
The Journal of Physiology. 558:417-431
The human ether-a-go-go related gene (HERG) encodes the pore forming α-subunit of the rapid delayed rectifier K+ channel which is central to the repolarization phase of the cardiac action potential. HERG K+ channels have unusual kinetics characteriz
Autor:
Louise J. Brown, Greg J. Pankhurst, W. Douglas Fairlie, Paul M. G. Curmi, Asne R. Bauskin, Dene R. Littler, S. Pankhurst, Raffaella Tonini, Stephen J. Harrop, Matthew Z. DeMaere, Michele Mazzanti, Terence J. Campbell, Samuel N. Breit
Publikováno v:
Journal of Biological Chemistry. 279:9298-9305
Most proteins adopt a well defined three-dimensional structure; however, it is increasingly recognized that some proteins can exist with at least two stable conformations. Recently, a class of intracellular chloride ion channel proteins (CLICs) has b
Autor:
Jane A. Bursill, Philip W. Kuchel, Paramjit S. Bansal, Catherine E. Clarke, Jamie I. Vandenberg, Samuel N. Breit, Margaret Sunde, Allan M. Torres, Asne R. Bauskin, Terence J. Campbell, Paul F. Alewood, David Smith
Publikováno v:
Journal of Biological Chemistry. 278:42136-42148
The HERG K+ channel has very unusual kinetic behavior that includes slow activation but rapid inactivation. These features are critical for normal cardiac repolarization as well as in preventing lethal ventricular arrhythmias. Mutagenesis studies hav
Autor:
Stefan A. Mann, Jamie I. Vandenberg, Juliane Heide, Mark Perrin, Adam P. Hill, Terence J. Campbell
Publikováno v:
Molecular pharmacology. 85(5)
The Kv11.1 potassium channel is the molecular target for the majority of drugs implicated in acquired long QT syndrome, the most common cause of drug-induced sudden cardiac death, and a common reason for drug restriction or withdrawal from the market
Autor:
Stella M. Valenzuela, T. Reztsova, Matthew Z. DeMaere, Min Ru Qiu, Asne R. Bauskin, S. Pankhurst, Paul M. G. Curmi, Terence J. Campbell, Stephen J. Harrop, Samuel N. Breit, W.D. Fairlie, Raffaella Tonini, Kristina Warton, Michele Mazzanti, Lucy Jankova, W.M. Wu
Publikováno v:
Journal of Biological Chemistry. 276:44993-45000
CLIC1 (NCC27) is a member of the highly conserved class of chloride ion channels that exists in both soluble and integral membrane forms. Purified CLIC1 can integrate into synthetic lipid bilayers forming a chloride channel with similar properties to