Izhak Michaelevski

Modulation of a brain voltage-gated K+ channel by syntaxin 1A requires the physical interaction of Gbetagamma with the channel.

Direct interaction of target SNAREs with the Kv2.1 channel. Modal regulation of channel activation and inactivation gating.

Kv2.1 channel activation and inactivation is influenced by physical interactions of both syntaxin 1A and the syntaxin 1A/soluble N-ethylmaleimide-sensitive factor-25 (t-SNARE) complex with the C terminus of the channel.

Target soluble N-ethylmaleimide-sensitive factor attachment protein receptors (t-SNAREs) differently regulate activation and inactivation gating of Kv2.2 and Kv2.1: Implications on pancreatic islet cell Kv channels.

Vimentin binding to phosphorylated Erk sterically hinders enzymatic dephosphorylation of the kinase.

Interaction of syntaxin with a single Kv1.1 channel: a possible mechanism for modulating neuronal excitability.

VAMP2 interacts directly with the N terminus of Kv2.1 to enhance channel inactivation.

Formation of the full SNARE complex eliminates interactions of its individual protein components with the Kv2.1 channel.

Syntaxin modulates Kv1.1 through dual action on channel surface expression and conductance.

Rearrangements in the relative orientation of cytoplasmic domains induced by a membrane-anchored protein mediate modulations in Kv channel gating.

Axoplasm isolation from peripheral nerve.

Axonal transport proteomics reveals mobilization of translation machinery to the lesion site in injured sciatic nerve.

Signaling to transcription networks in the neuronal retrograde injury response.

Gas-phase compaction and unfolding of protein structures.