Professor Cicerone works on development and application of spectroscopic coherent Raman imaging approaches and on dynamics of amorphous condensed matter. In the coherent Raman imaging work, his group introduced broadband (spectroscopic) coherent anti-Stokes Raman scattering (BCARS) microscopy in 2004. Since then he and his group have remained at the forefront of this field, introducing improvements such as a time-domain Kramers-Kronig transform to deal with non-causal signals for retrieving the pure Raman spectrum directly from the raw BCARS signal. The results of that work and other instrument design innovations utilizing impulsive vibrational coherence generation resulted in recognition as one of the top 10 innovations in BioPhotonics for 2014. His group has logged many imaging firsts, including the first to obtain quantitative vibrational fingerprint spectra from mammalian cells using coherent Raman imaging, and the first to identify specific structural proteins from coherent Raman imaging.His work on dynamics of amorphous condensed matter focuses on the impact of picosecond timescale spatial and temporal heterogeneity in dynamics on transport and relaxation in liquids and glasses. In 2004, he used neutron scattering to show for the first time that chemical and physical stability of proteins encapsulated in glassy sugars could be predicted by the profile of ps-timescale dynamics. Since then, he has developed a framework for calculating transport and relaxation properties of liquids and glasses over 12 orders of magnitude in time, based solely on ps-timescale dynamics, and identified the molecular origin of a relaxation process (Johari-Goldstein process) that had been observed but remained enigmatic for 50 years. He has also developed benchtop approaches accessible to pharmaceutical labs for measuring the relevant dynamics, and developed a protein stability approach for drug delivery that encapsulates proteins in nanometer-sized droplets of vitrified sugar-based glass and makes them impervious to traditional processing steps, allowing retention of ~99% of protein function or titer after all processing steps. This approach has now been used successfully in large animal trials, and has also been shown to be effective for transdermal drug delivery due to the nanometer size of the encapsulation materials.