Alpha-synuclein oligomerization and aggregation: A model will always be a model: This is a response to "Monitoring alpha-synuclein oligomerization and aggregation using bimolecular fluorescence complementation assays: What you see is not always what you get". Read the reply on "Alpha-Synuclein oligomerization and aggregation: All models are useful but only if we know what they model". The articles are accompanied by a Preface "How good are cellular models?".

Many different types of protein aggregates have attracted the minds and curiosity of countless armies of scientists, i.e., laboratories, in the world for more than 100 years. For example, it was in 1912 that F. Lewy reported the presence of structures, eternalized as Lewy bodies (LBs) and Lewy neurites (LNs), in the brains of patients with Parkinson's disease (Lewy 1912). Since then, tremendous efforts have been dedicated to figuring out how such deposits 'cause' Parkinson's disease. In 1997, with the identification of alpha-synuclein (aSyn) as the major protein component of LBs and LNs (Spillantini et al. 1997) gave us a culprit and, since then, numerous scientists have acted as prosecutors, trying to demonstrate the toxicity of the protein towards the 'hard-working' and particularly 'vulnerable' dopaminergic neurons from the substantia nigra. Twenty three years have passed, data have been collected, hypotheses have been tested, and the causality between LB pathology and disease is still a matter of intense debate.