Society of
|
2019 Cranefield Award Stephan A. Pless for "Molecular determinants for agonist recognition and discrimination in P2X2 receptors" Journal of General Physiology 151 (7) 898-911; doi: doi.org/10.1085/jgp.201912347 2018 Cranefield Award Anne E. Carlson for "PLC and IP3-evoked Ca2+ release initiate the fast block to polyspermy in Xenopus laevis eggs" Journal of General Physiology 150 (9): 1239–1248.doi: doi.org/10.1085/jgp.201812069 2017 Cranefield Award Randy Stockbridge for "Mechanism of single- and double-sided inhibition of dual topology fluoride channels by synthetic monobodies" Journal of General Physiology 149 (4): 511-522. doi: 10.1085/jgp.201611747 |
|
2016 Cranefield Award Francesco Tombola for "The Hv1 proton channel responds to mechanical stimuli." Journal of General Physiology 148 (5): 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. |
|
2013 Cranefield Award
Matthew C. Trudeau for "Direct interaction of eag domains and cyclic nucleotide–binding homology domains regulate deactivation gating in hERG channels" Journal of General Physiology 142 (4): 351-366. doi: 10.1085/jgp.201310995. |
|
2011 Cranefield Award
Baron Chanda for "Estimating the voltage-dependent free energy change of ion channels using the median voltage for activation" Journal of General Physiology 139 (1): 3-17. doi: 10.1085/jgp.201110722 Dr. 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. |
|
2010 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.) |
|
SGP Cranefield Student and Postdoc Awards | Paul F. Cranefield Award