Aldo Ferrari
Dr. Aldo Ferrari is a senior scientist at the Laboratory of Thermodynamics in Emerging Technologies (http://www.ltnt.ethz.ch/), at the Swiss Federal Institute of Technology Zurich, Switzerland. His scientific activity is mostly focused on the development of bio-mimetic scaffolds for tissue regeneration or healing. The group studies the differentiation of cells due to mechanical and topographical stimuli as provided by nanostructured, biocompatible surfaces. A cell assumes a certain shape (i.e. a polarity) when interacting with a specific surface in a process that is regulated by the formation of cellular adhesions. Dr. Ferrari is specifically interested in the molecular mechanisms univocally linking the substrate configuration to a related cell polarity state. Live-cell florescent imaging is widely applied in his studies to reveal the 3D shape of cells and the distribution of specific differentiation markers. Dr. Ferrari has been using Huygens since 2004. He tells us about his reasons for choosing Huygens: "Six years ago I had to choose among different software for deconvolution. I decided then to test the quality of the deconvolution obtained using different algorithms. I acquired a 3D stack of a fluorescent object with known shape and volume. After deconvolving with the different software, I rendered the object from the resulting stacks, and I compared the symmetry and the volume. The result was that Huygens deconvolution was the most valuable both in terms of symmetry and volume reconstruction. A second upstanding feature of Huygens is the co-localization platform. A unique possibility here is free cropping of images in 3D, which clearly gives an added degree of freedom to the measure of co-localization. Especially when the Pearson’s coefficient is to be measured in an organelle or a sub-compartment of the cell."
Publications:
- A. Ferrari, M. Cecchini, M. Serresi, P. Faraci, D. Pisignano, & F. Beltram. Neuronal polarity selection by topography-induced focal-adhesion control. Biomaterials 31, 4682-4694 (2010).
- A. Marmaras, U. Berge, A. Ferrari, V. Kurtcuoglu, D. Poulikakos & R. Kroschewski. A mathematical method for the 3D analysis of rotating deformable systems applied on lumen-forming MDCK cell aggregates. Cytoskeleton 67, 224-240 (2010).
- A. Ferrari, P. Faraci, M. Cecchini, & F. Beltram. The effect of alternative neuronal differentiation pathways on PC12 cell adhesion and neurite alignment to nanogratings. Biomaterials 31, 2565-2573 (2010).
- A. Ferrari, M. Cecchini, R. Deglinnocenti & F. Beltram. Directional PC12 cell migration along plastic nanotracks. IEEE Transactions on Biomedical Engineering 56, 2692-2696 (2009).
- A. Ferrari, A. Veligodskiy, U. Berge, M. S. Lucas & R. Kroschewski. ROCK-mediated contractility, tight junctions and channels contribute to the conversion of a preapical patch into an apical surface during isochoric lumen initiation. Journal of Cell Science 121, 3649-3663 (2008).
- A. Ferrari*, C. Le Clainche*, D. Schlaepfer*, M. Klingauf, A. Veligodskiy, K. Grohmanova, D. Didry, D. Le, C. Egile, M. Carlier & R. Kroschewski. IQGAP1 controls the activation of N-WASP dependent actin polymerization. Journal of Biological Chemistry 282, 426-435 (2007). *Contributed equally to this work.
- D. Zeng, A. Ferrari, J. Ulmer, A. Veligodskiy, P. Fischer, J. Spatz, J. Ventikos, D. Poulikakos & R. Kroschewski. Three-dimensional modeling of mechanical forces in the Extracellular matrix during epithelial lumen formation. Biophysical Journal 90, 4380-4391 (2006).
- S. Pantano, A. Marcello, A. Ferrari, D. Gaudiosi, A. Sabò, V. Pellegrini, F. Beltram, M. Giacca & P. Carloni. Insights on HIV-1 Tat:P/CAF bromodomain molecular recognition from in vivo experiments and molecular dynamics simulations. Proteins 62, 1062-1073 (2006).
- S. Pantano, A. Marcello, A. Sabò, A. Ferrari, V. Pellegrini, F. Beltram, M. Giacca & P. Carloni. A theoretical model of N-terminal Cyclin T1 based on FRET experiments. Journal of Theoretical Medicine 6, 73-79 (2005).
- A. Fittipaldi, A. Ferrari, M. Zoppe', C. Arcangeli, V. Pellegrini, F. Beltram & M. Giacca. Cell membrane lipid rafts mediate caveolar endocytosis of HIV-1 tat fusion proteins. Journal of Biological Chemistry 278, 34141-34149 (2003).
- A. Ferrari, C. Arcangeli, V. Pellegrini, A. Fittipaldi, M. Giacca & F. Beltram. Caveolae-mediated internalization of extracellular HIV-1 tat fusion proteins visualized in real time. Molecular Therapy 8, 284-294 (2003).
- A. Marcello, A. Ferrari, V. Pellegrini, G. Pegoraro, M. Lusic, F. Beltram & M. Giacca. Recruitment of human Cyclin T1 to nuclear bodies through a direct in vivo interaction with the promyelocytic leukemia factor. Embo Journal 22, 2156-2166 (2003).
- R. Nifosì, A. Ferrari, C. Arcangeli, V. Tozzini, V. Pellegrini & F. Beltram. Photoreversible dark state in a tristable green fluorescent protein variant. Journal of Physical Chemistry B 107, 1679-1684 (2003).
- R. A. G. Cinelli, V. Pellegrini, A. Ferrari, P. Faraci, R. Nifosì, M. Tyagi, M. Giacca & F. Beltram. Green fluorescent proteins as optically-controllable elements in bioelectronics. Applied Physics Letters 79, 3353-3355 (2001).
- S. Giannecchini, D. Matteucci, A. Ferrari, M. Pistello & M. Bendinelli. Feline immunodeficiency virus-infected cat sera associated with the development of broad neutralization resistance in vivo drive similar reversions in vitro. Journal of Virology 75, 8868-8873 (2001).
- A. Ferrari*, A. Marcello*, R. A. G. Cinelli*, A. Signorelli, M. Tyagi, V. Pellegrini, F. Beltram & M. Giacca. Visualization of in vitro direct interaction between HIV-1 Tat and human Cyclin T1 in specific subcellular compartments by resonance energy transfer. Journal of Biological Chemistry 276, 39220-39225 (2001). * Contributed equally to this work.
- R. A. G. Cinelli, A. Ferrari, V. Pellegrini, A. Signorelli, M. Tyagi, M. Giacca & F. Beltram. Engineering single-molecule fluorescence dynamics for advanced biomolecular applications. Australian Journal of Chemistry 54, 107-111 (2001).
- R. A. G. Cinelli, A. Ferrari, V. Pellegrini, M. Tyagi, M. Giacca & F. Beltram. The enhanced green fluorescent protein as a tool for the analysis of protein dynamics and localization: local fluorescence study at the single-molecule level. Photochemistry and Photobiology 71, 771-776 (2000).
