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Additionally, these mutants retained the ability to learn much longer than normal worms.

Both mutants retained the global structure of the native protein (Fig. S2e).

The results showed that the Ile529Ala and Asn560Ala mutants retained the binding activity to 8C11, but they can't bind to 8H3 with the presence of 8C11 (Fig. 2B), suggesting that the epitope of 8C11 was retained, but the epitope of 8H3 was damaged in mutants Ile529Ala and Asn560Ala.

All the mutants retained the normal ATPase activity of gp96 (Fig. S2), suggesting that the mutations did not affect their native conformation.

All four mutants retained the slow-killing phenotype, although the LF82ΔompR mutant displayed attenuated virulence compared to the wild type strain (Figure 3B; P<0.0001).

Considering that GSS disease has a slower progression and a later onset compared to CJD, we investigated whether all other GSS-associated PrP mutants retained the anti-Bax function.

Remarkably, all the mutants retain the ability to activate cysteine desulfurase, even when two of them exhibit a strong decrease in iron binding, revealing a differential sensitivity of these functional features to loop-1 perturbation.

Using an erythrocyte-protection assay, we demonstrated that most of the translocation-competent mutants retain the conformational protective epitope.

The M5 and M9 mutants retain the entire ECD, while the M4, M7, and M8 mutants have deletions of nearly the entire ECD.

δCOP mutants retain the Verm and Gasp luminal proteins inside the tracheal cells at stage 15 and fail to fully expand DT tube diameter at early stage 16 (Figure 4A, B, C, D).

Importantly, these mutants retain the conserved loop region and the two TMDs.