[1] Researchers were inspired to name the newly found twister motif due to its resemblance to the Egyptian hieroglyph 'twisted flax'.

[2] The active site of the twister ribozyme is centered in a double-pseudoknot, facilitating a compact fold structure through two long-range tertiary interactions, in partnership with a helical junction.

[7][1] Replacements of the pro-S nonbridging oxygen of the scissile phosphate with a thiol group leads to reduced self-cleavage rates, suggesting that the mechanism is not reliant on bound magnesium.

[6] A likely mechanism for this is the stabilization of the transition state by reducing electrostatic strain on the substrate strand from the growing negative charge during cleavage.

The twister ribozyme motif is relatively common in nature with 2,700 examples observed across bacteria, fungi, plants, and animals.