E. G. Govorunova

This study identifies structural motifs in kalium channelrhodopsins (KCRs) responsible for their K+ selectivity, showing that specific mutations convert Na+ selectivity to K+ selectivity.

The paper identifies KCRs, light-gated potassium channels from a fungus-like protist, which are highly selective and fast-acting, showing potential for optogenetic control of potassium gradients in neurological and cardiac diseases.

The paper identifies and characterizes sequence motifs and ion selectivity mechanisms in channelrhodopsins from diverse algal and protist species using electrophysiological analysis and genomic data.

The paper reports the crystal structure of bromide-bound GtACR1, showing structural changes that relax constrictions in the anion tunnel, indicating a transition to a pre-activated state.

The paper identifies and characterizes two new families of anion channelrhodopsins (ACRs), including RubyACRs with highly red-shifted absorption spectra, expanding optogenetic tools for neural inhibition.

The paper identifies 19 new BCCR proteins from cryptophyte algae, revealing distinct conductance mechanisms and rapid desensitization in two subfamilies through electrophysiology and spectroscopy.

This study shows the photoactive site in GtACR1 affects chloride conductance and channel closing through electrostatic changes and distance-dependent effects.