References

abundant in the brain, normally hydroly-ses the bonds between ubiquitin mole-cules or between ubiquitin and other mol-ecules such as glutathione. The mutation detected by Leroy et al. leads to a de-crease in the enzyme activity of UCH-L1. However, exactly how this produces PD is currently unclear, although a change in the state of ubiquitination of a key pro-tein might be important. These results are analogous to those obtained from experiments on HD by Saudou et al. dis-cussed above. However, it is also possible that the mutated UCH-L1 itself is prone to aggregate