Although Gaucher disease is a rare disorder, recent developments in novel means 
for therapeutic intervention have invigorated both academic research and 
pharmaceutical industry discovery programmes. The common mutations found in the 
lysosomal enzyme deficient in Gaucher disease, beta-glucocerebrosidase, earmark 
these proteins for destruction by the endoplasmic reticulum-localised protein 
folding machinery, resulting in enzyme insufficiency, lysosomal glycolipid 
storage and subsequent pathology. However, many of these mutants can be rescued 
from global misfolding to preserve glycolipid substrate binding and eventual 
catalysis in the lysosome, by the addition of subinhibitory concentrations of 
pharmacologically active small molecules. This novel, chaperon-mediated approach 
has benefited from insights into the molecular understanding of 
beta-glucocerebrosidase structure, drug design and development in cellular 
models for disease.