The cytoplasmic tail is then inserted into the mitochondrial outer membrane.

It consists of three parts; a cytoplasmic tail, a transmembrane region and an extracellular part.

Finally there is a transmembrane domain, and the C-terminal cytoplasmic tail.

It is presumed through a direct association with the cytoplasmic tail of beta-integrin.

This connection requires tryptophan and negatively charged amino acids in the ligand's cytoplasmic tail.

PfRH2b also binds aldolase with its cytoplasmic tail.

The signal for endosomal targeting resides in the cytoplasmic tail of the invariant chain.

This cytoplasmic tail provides docking sites for numerous signaling intermediates.

The intracellular cytoplasmic tail of this protein contains two highly conserved domains which may be involved in CD93 function.

This negative regulator becomes localized to the cytoplasmic tail of LRP-5/6.