Drew C. Tilley

2Jon T Sack
2Vladimir Yarov-Yarovoy
1Sebastian Fletcher-Taylor
1Maryam Zamanian
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Electrically excitable cells, such as neurons, exhibit tremendous diversity in their firing patterns, a consequence of the complex collection of ion channels present in any specific cell. Although numerous methods are capable of measuring cellular electrical signals, understanding which types of ion channels give rise to these signals remains a significant(More)
  • Kanchan Gupta, Maryam Zamanian, Chanhyung Bae, Mirela Milescu, Dmitriy Krepkiy, Drew C Tilley +4 others
  • 2015
Tarantula toxins that bind to voltage-sensing domains of voltage-activated ion channels are thought to partition into the membrane and bind to the channel within the bilayer. While no structures of a voltage-sensor toxin bound to a channel have been solved, a structural homolog, psalmotoxin (PcTx1), was recently crystalized in complex with the extracellular(More)
Membrane proteins are critical functional molecules in the human body, constituting more than 30% of open reading frames in the human genome. Unfortunately, a myriad of difficulties in overexpression and reconstitution into membrane mimetics severely limit our ability to determine their structures. Computational tools are therefore instrumental to membrane(More)
C o m m e n t a r y All known K + channels use the same molecular architecture to achieve K + selectivity. Selectivity filters, even from distantly related K + channels, appear nearly identical in atomic resolution crystal structures; remarkably, the deviation in the coordinates of K +-coordinating backbone carbonyls is less than the uncertainty in the(More)
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