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Structure-based alignment of TRP channels enables comparison of structural changes, ion permeation pathways and ligand-binding sites and reveals over-representation of structures that represent non-conducting states.

An anion-selective ligand gated channel acts as a presynaptic auto-receptor to modulate vesicle release and neuronal excitation.

The transmembrane helices forming the pore determine the conductance of the selectivity filter through allosteric interactions.

TRPM2 is simply a ligand gated channel and does not to possess enzymatic activity, even though it shows sequence similarity to Nudix hydrolases.

The animal phylogeny of glutamate receptors indicates that vertebrate types do not account for all receptor classes originated during evolution, neither are they the pinnacle of a linear evolutive process.

The Hrd1-centric endoplasmic reticulum associated degradation system is regulated by interplay between the system's components.

The structure of the calcium channel Orai in an open conformation reveals a dilated pore and gives insight into mechanisms of ion permeation and calcium selectivity.

Hemoglobin affinity and cooperativity reveal mechanistic insights in how the relation between physiology and evolutionary variations shape a protein's molecular property.

The TRPV1, TRPV2 and TRPV3 channels are gated on the cytosolic side of the pore, whereas structural changes in the ion selectivity filter associated with activation don't control cation access.

TMEM16F shifts its ion selectivity in response to change of intracellular Ca²⁺, membrane potential and ionic strength.