Isabelle Baconguis graduated from the University of Pennsylvania with a B.A. in Biochemistry in 2005. She remained at the University of Pennsylvania for two years studying glutamate receptors. She joined the Neuroscience Graduate Program at OHSU in 2007. During her doctoral research at the Vollum Institute, she studied acid sensing ion channels (ASICs), members of the superfamily of amiloride-sensitive and Na+-selective trimeric ion channels. Using a combination of x-ray crystallography and electrophysiology, she exploited toxin-dependent modulation of ASIC function to elaborate molecular mechanisms of gating, selectivity and ion channel block. She joined the Vollum Insitute as a Vollum fellow in 2013 and was promoted to assistant scientist in 2016.
The Baconguis lab is pursuing atomic-resolution mechanisms of sodium-selective and voltage-independent ion channels involved in a spectrum of processes ranging from synaptic transmission to regulation of salt homeostasis.
Areas of interest
- x-ray crystallography and electrophysiology
- cryo-electron microscopy (cryo-EM)
- sodium channels
- ion channels
- channel assembly, channel gating, and ion selectivity
- protein biochemistry
- structural biology
- Ph.D., Oregon Health & Science University, Portland Oregon 2013
- B.A., University of Pennsylvania, Philadelphia Pennsylvania 2005
Honors and awards
- NIH Director's Early Independence Award (2013-2018)
- Ruth L. Kirschstein National Research Service Award, NIH (2011-2013)
Baconguis I, Bohlen CJ, Goehring A, Julius D, Gouaux E. (2014) X-ray structure of acid-sensing ion channel 1-snake toxin complex reveals open state of a Na+-selective channel. Cell 156(4): 717-729.
Baconguis I, Hattori M, Gouaux E. (2013) Unanticipated parallels in architecture and mechanism between ATP-gated P2X receptors and acid sensing ion channels. Current Opinion in Structural Biology 23(2): 277-284.
Baconguis I, Gouaux E. (2012) Structural plasticity and dynamic selectivity of acid-sensing ion channel-spider toxin complexes. Nature 489(7416): 400-405.