The in vivo CLSM is a relatively new but very promising approach for corneal examination in LSDs. This technique has a big advantage to be non-invasive, thus enabling dynamic studies in the same individuals over time. The corneal involvement has been demonstrated by using in vivo CLSM in patients with other LSDs, like Fabry disease, Tangier disease and cystinosis. On the basis of our in vivo CLSM finding about corneal involvement in NPC1 disease, we performed the present study to further clarify whether the regression of cellular inclusions could be achieved by combined Cyclo/ALLO/miglustat INCB18424 therapy. It is widely known that one of the most pronounced side effects of miglustat treatment in Gaucher and NPC1 patients is the peripheral neuropathy. Immune mechanisms have been proposed to play an important role in the development of peripheral neuropathy in the cornea. Thus, the increased number of DCs can be considered as a part of mechanisms suggesting immune-mediated contribution to the neuropathy. This pronounced increase can be attributed to some extent to be part of natural progression of disease. In the future, in vivo dynamic assessment of central corneal inflammatory cells density may provide new insights for management of side effects and, probably, serve as an indicator of miglustat-caused neuropathy’s severity following long-term therapy. To date, very often ophthalmologic findings and the relationship between ocular and extraocular symptoms are neglected in the global evaluation of the LSD-patients. Nevertheless, the ocular involvement can alternatively reflect other more generalized defects in LSDs. Keeping in mind the evidence that in vivo CLSM allows the early recognition of morphological changes in the cornea during the progression of disease or treatment course, we believe that this technique has the potential to become an additional clinical tool for reliable diagnosis and evaluation of treatment options in NPC1 disorder. The inherit difficulty of expression and purification of membrane proteins has drastically hindered studies of these important players of cellular functions. In the past decade, there has been a leap in the effort of solving crystal structures of membrane proteins. As of Jun. 2011, there are almost 300 unique structures of membrane proteins in the protein data bank. The availability of an increasing number of protein structures has set the stage for studies of the dynamic life cycles of membrane proteins, starting from the folding and assembly of nascent polypeptide chains in the membrane that leads to functional proteins. Specifically, the assembly process of obligate homo-oligomeric membrane proteins remains elusive. Obligate oligomers exist and function exclusively in their oligomeric form. However, it was not clear how multiple subunits, after their co-translational membrane insertion, assemble into the final functional state. Toward answering these questions, we chose an Escherichia coli inner membrane protein AcrB as a model system to study its oligomerization. AcrB is an obligate homo-trimer.