Gennaro Esposito
Gennaro Esposito
affiliation: Università di Udine
research area(s): Chemical Biology, Molecular Biology
Course: Biomedical and Biotechnological Sciences
University/Istitution: Università di Udine
Rino (Gennaro) Esposito was born on Sept. 19th 1953 in Naples where he received his education and got the degree in Chemistry cum laude in 1979. From 1980 to 1982 he was a chemistry teacher and worked at the NMR spectroscopy laboratory of the Chemistry Institute of Naples University. From Sept. 1982 to Jan. 1990 he became researcher at the NMR laboratory of Assoreni-Eniricerche, (Monterotondo - Rome), a research corporate of ENI, the former Italian government oil company. In Feb. 1990 he joined the University of Udine, first as a permanent researcher in Biophysics (May 1990-Aug. 2000) and later, from Sept. 2000, as an associate professor of Applied Physics of the Faculty of Medicine, a position that he still keeps. He is the research leader of the Biophysics laboratory of the Dipartimento di Scienze e Mediche e Biologiche in the field of NMR spectroscopy and biophysics methodology for the study of biopolymers, in collaboration with Dr. Alessandra Corazza, prof. Federico Fogolari and prof. Paolo Viglino. He is also in charge for the mass spectrometry laboratory of MATI Centre of Excellence. Besides home lab work, Rino Esposito did often scientific activity abroad (Jun./Dec. 1983 and Mar. 1985/Sept. 1986 at the NMR lab of the Biochemistry Department of Oxford University, UK; Jul./Dec. 1987 at the NMR lab of the School of Pharmacy of London University, UK; Aug. 1993/Jul. 1994 at the NMR lab of Lausanne University, CH; Jul.-Aug. 2001 at LEDS of University J. Fourier, Grenoble, F). He was invited speaker at a few national and international conferences and has been lecturing several times at schools, workshops and meetings on NMR spectroscopy techniques. As unit-responsible leading scientist, he received several research grants from National Research Council, University Ministry, European Union, Health Ministry.
The main subject of scientific interest of the biophysics lab has always been the structural and functional characterization of biopolymers such as proteins, immunoactive peptides and oligonucleotides, coupled to the setup of novel NMR and biophysical methodology.
As for protein biophysics, over the last years the lab was involved in structural and functional determinations on small heat shock proteins (such as murine HSP25 and αB-crystallin) transcription factors (such as the thyroid transcription factor 1 (TTF1) homeodomain and the Pax-8 Paired Box domain) elastic matrix components (such as the trimeric C1q-like domain of EMILIN1 responsible for cell adhesion and migration). Most of the efforts, however, were focussed on the structure and function of amyloidogenic proteins such as β2-microglobulin and variants thereof, apolipoprotein A-I, human lysozyme amyloidogenic mutants, acylphosphatase from E. coli and S. sulfataricus, Alzheimer A-beta peptide derivatives. In the methodology category, recent work addressed the paramagnetic perturbation of the NMR spectra of proteins to determine the exposed molecular surface, the scalar coupling determination from HSQC TOCSY spectra for structural inferences and the evaluation of thermodynamic parameters from isotope exchange experiments.
Recently, from functional proteomics activity by mass spectrometry, the lab has also started investigations in metabonomics by a combined NMR and mass spectrometry approach.
Rino Esposito is coauthor of more than 100 publications in international peer-reviewed journals and about 200 printed communications in proceedings of national and international conferences. In 28/17 peer-reviewed articles he was first/second author, whereas in 18 articles he was corresponding (last) author. His publications received some 1,700 citations with a H-index of 24 (Scholar Search/Harzing’s Publish or Perish assessments, with self-citations excluded). His three most-quoted publications received 143, 133 and 94 citations (Esposito et al., Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation. Protein Sci., 9, 831-845, 2000; Esposito et al., A high resolution 1H NMR study of the solution structure of Alamethicin. Biochemistry, 26, 1043-1050, 1987; Esposito et al., The solution structure of human β2-microglobulin reveals the prodromes of its amyloid transition. Protein Sci., 11, 487-499, 2002). The total impact factor of the publications is about 330.

The five most recent publications excluding reviews are:

Fogolari. F., Corazza A., Varani N., Rotter M., Gümral D. Codutti L. Rennella E., Viglino P., Bellotti V., Esposito G.
Molecular dynamics simulation of b2-microglobulin in denaturing and stabilizing conditions
Proteins 79, 986-1001, 2011.

Rennella E., Corazza A., Giorgetti S., Fogolari F., Viglino P., Porcari R., Verga L., Stoppini M., Bellotti V. and Esposito G.
Folding and Fibrillogenesis: Clues from β2-microglobulin
J. Mol. Biol. 401, 286-297, 2010.

Verdone G., Corazza A., Colebrooke S. A., Cicero D., Eliseo T., Boyd J., Doliana R., Fogolari F., Viglino P., Colombatti A., Campbell I. D. and Esposito G.
NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1
J. Biomolec. NMR 43, 79-96, 2009.

Codutti L., van Ingen H., Vascotto C., Fogolari F., Corazza A., Tell G., Quadrifoglio F., Viglino P., Boelens R. and Esposito G.
The solution structure of DNA-free Pax-8 Paired Box domain accounts for redox regulation of transcriptional activity in Pax protein family
J. Biol Chem. 283, 33321-33328, 2008.

Esposito G., Ricagno S., Corazza A., Rennella E., Gümral D., Mimmi M.C., Betto E., Pucillo C.E.M., Fogolari F., Viglino P., Raimondi S., Giorgetti S., Bolognesi B., Merlini G., Stoppini M., Bolognesi M. and Bellotti V.
The controlling roles of Trp60 and Trp95 in β2-microglobulin function, folding and amyloid aggregation properties
J. Mol. Biol. 378, 885-895, 2008.
Project Title:
New methods for studying amyloidogenic proteins
A novel method has been devised and successfully tested to perform efficient isotope exchange measurements as a function of temperature or other external variables. The extracted information provides a very detailed, residue-based picture of the folding landscape of an investigated protein. The method should be applied to amyloidogenic proteins such as β2-microglobulin and related variants to identify the determinants of fibrillogenesis.