Stephanie Cologna

ColognaPhD, Texas A&M University

Assistant Professor, Department of Chemistry, College of Liberal Arts & Sciences

Office: 5414 SES

Lab:

Phone: (312) 413-2762

email: cologna@uic.edu

Web Site: Stephanie Cologna Laboratory Page

 

Research Interests:

Stephanie joined the Department of Chemistry at UIC in the summer of 2015.  Her laboratory is focused on using mass spectrometry to further understand human diseases.  Current areas of interest include proteomic studies including identification and quantification of protein proteoforms in different human disease models.  Furthermore, her laboratory is investigating the relationship between lipid heterogeneity and neurodegeneration in the brain.  To support these efforts, a significant portion of Dr. Cologna’s laboratory is dedicated to method development and integrating new technologies related to mass spectrometry analysis of biomolecules.

 

Publications:

Cologna, S.M., Crutchfield, C.A., Searle, B.C., Blank, P.S., Toth, C.L., Ely, A.M., Picache, J.A., Backlund, P.S., Wassif, C.A., Porter, F.D., & Yergey, A.L. An efficient approach to evaluate reporter ion behavior from MALDI-MS/MS data for quantification studies using isobaric tags. J. Proteome Res., 14 (2015) 4169-4178.

Cologna, S.M., Cluzeau, C.V.M., Yanjanin, N.M., Blank, P.S., Dail, M.K., Siebel, S., Toth, C.L., Wassif, C.A., Lieberman, A.P., & Porter, F.D. Human and mouse neuro-inflammation markers in Niemann-Pick disease, type C1. J. Inherited Metab. Dis., 37 (2014) 83-92.

Cologna, S.M., Jiang, X.-S., Backlund, P.S., Cluzeau, C.V.M., Dail, M.K., Yanjanin, N.M., Siebel, S., Toth, C.L., Jun, H.-S., Wassif, C.A., Yergey, A.L., & Porter, F.D. Quantitative proteomic analysis of Niemann-Pick disease, type C1 cerebellum identifies protein biomarkers and provides pathological insight. PLoS One, 7 (2012) e47845.

Cologna, S.M., Russell, W.K., Lim, P.J., Vigh, G., & Russell, D.H. Combining isoelectric point fractionation, liquid chromatography and mass spectrometry to increase peptide detection and protein identification. J. Amer. Soc. Mass Spectrometry, 21 (2010) 1612-1619.