|2016 Cranefield Award|
Francesco Tombola "The Hv1 proton channel responds to mechanical stimuli." Journal of General Physiology 148:405-418 DOI: 10.1085/jgp.201611672
|2015 Cranefield Award|
László Csanády became a PhD student of Professor David C. Gadsby at The Rockefeller University in 1995, following completion of medical studies at Semmelweis University, Budapest. Under the guidance of Dr. Gadsby he became involved in studying structure-function of the CFTR chloride channel, which still remains one of his major research focuses. After completion of his doctoral work he returned to Hungary in 2000, and joined the Department of Medical Biochemistry at Semmelweis University where he continues to work as an Associate Professor. Research effort in his group is focused on structure and function of the CFTR chloride channel and of the TRPM2 cation channel, and is currently funded by grants from HHMI and the Hungarian Academy of Sciences.
2014 Cranefield Award
Matthew C. Trudeau received his PhD in 1998 from the University of Wisconsin. His thesis work, with Dr. Gail A. Robertson, focused on the voltage-gated human ether-á-go-go–related gene (hERG) potassium channel and related channels, including the role of hERG in acquired and inherited cardiac arrhythmia and mechanisms of hERG channel inactivation and closing (deactivation). As a postdoctoral fellow, with Dr. William N. Zagotta at the University of Washington, Dr. Trudeau studied retinal rod cyclic nucleotide–gated (CNG) channels, including their role in an inherited form of vision loss, their unusual 3:1 subunit stoichiometry, and their modulation by Ca2+-calmodulin. These studies involved a combination of protein chemistry, electrophysiology, and advanced fluorescence imaging methods that Dr. Trudeau would later apply to hERG in his own laboratory at the University of Maryland. He was given the Cranefield Award for a paper that investigated the unusually slow deactivation kinetics of hERG channels, a property critical for delayed entry of potassium and membrane repolarization during the cardiac action potential. The paper addressed a controversy regarding the molecular mechanism by which the N-terminal eag domain of hERG regulates deactivation. The authors used patch-clamp recording and spectral FRET analysis to determine which regions of hERG interact with the eag domain to regulate deactivation in functional channels at the plasma membrane.
2013 Cranefield Award
Baron Chanda's primary research interest is to understand the mechanisms of electrical signaling by membrane proteins such as ion channels. Baron graduated from the University of Delhi and earned his Masters degree from the University of Pune, India. He obtained his Ph.D. at the National Center for Biological Sciences in India where he gained experience in membrane protein biochemistry, fluorescence spectroscopy and basic electrophysiology. In 2000, he moved to UCLA to conduct postdoctoral research with Dr. Francisco Bezanilla involving elucidating the mechanisms of voltage-dependent structural changes in sodium and potassium channels. Baron's work at UCLA also led to development of new fluorescence methods to study membrane protein dynamics. He is currently an Associate Professor (as of July 2012) in the Department of Physiology at University of Wisconsin-Madison. His current research focuses on combining spectroscopic and structural methods with electrophysiology and protein thermodynamics to study voltage- and ligand-activated ion channels. His long-term interest is to understand the biophysical underpinnings of conformational coupling between protein domains. He received this award for the paper "Estimating the voltage-dependent free energy change of ion channels using the median voltage for activation" (JGP 2012: 139(1), 3-17).
2011 Cranefield Award
Rikard Blunck currently holds a faculty position at the Université de Montréal, Canada. He received his PhD in physics from the University of Kiel, Germany, and did his postdoctoral work at the University of California at Los Angeles in the laboratory of F. Bezanilla. His research interests are directed towards understanding structure function relations of voltage-gated potassium channels and pore forming toxins. He is using voltage-clamp fluorometry to investigate conformational changes of these membrane proteins and link them to their function. He received the award for the development of a technique to monitor fluorescence changes of proteins reconstituted in planar lipid bilayer. He and his coworkers used the technique to determine the pore forming mechanism of the toxin Cry1Aa of Bacillus thuringiensis. This work was published in JGP under the title “Rapid topology probing using fluorescence spectroscopy in planar lipid bilayer: the pore-forming mechanism of the toxin Cry1Aa of Bacillus thuringiensis.” (JGP 136 no. 5 497-513.)