Irina Pogozheva, PhD
College of Pharmacy
428 Church St
Ann Arbor, MI 48109-1065
Irina Pogozheva has experience in theoretical and experimental research of membrane proteins including ESR and other spectroscopic studies of rhodopsin, development and application of an ESR-based method for in situ measurement of NO release, application of computational methods for modeling of protein structure, conformational transitions, and protein-membrane interactions. She is co-author of 50 papers published in peer-reviewed journals, 16 meeting abstracts, and two book chapters.
Based on the experimental and computationally-derived restraints, she modeled diverse membrane proteins, including various G-protein coupled receptors (opioid, melanocortin, adrenergic, neurokinin, gonadotropin-releasing hormone, and glycoprotein hormone receptors), ABC-transporters (TAP1/TAP2), single-helical membrane proteins (cytochrome P450/cytochrome b5, cytochrome P450/cytochrome P450 reductase) and membrane-active peptides (colicin toxins, antimicrobial peptides). Models of opioid receptors were successfully used for structure-based design of opioid peptides with desired pharmacological profiles.
She also participated in design and development of databases for membrane proteins, including the OPM (Orientations of Proteins in Membranes) database, a resource that provides comprehensive information about proteins with known three-dimensional structures and their predicted orientations with respect to the lipid bilayer, and the Membranome database that provides models of transmembrane domains of single-helical membrane proteins.
For the complete list of Pogozheva’s professional and organizational activities refer to her CV.
To learn more, visit the Lomize Group web site
Theoretical analysis of protein structure, folding, evolution, and interaction with membranes
Modeling of membrane proteins, protein-protein, and protein-ligand complexes in membranes, including G-protein coupled receptors, ABC transporters, and single-helical membrane proteins
Computer-aided design of peptides with desired properties, such as receptor-selective ligands, cell-penetrating and antimicrobial peptides
Design, development, and maintenance of bioinformatics resources
Pogozheva, I.D., Tristram-Nagle, S., Mosberg, H.I., Lomize, A.L. (2013) Structural adaptation of proteins to different biological membranes. BBA-Biomembranes, 1828: 2592–2608
Lomize, M.A., Pogozheva, I.D., Joo, H., Mosberg, H.I., Lomize, A.L. (2012) OPM database and PPM web server: resources for positioning of proteins in membranes. Nucleic Acids Res. 40 (Database issue): D370-D376
Anand J.P., Purington, L.C., Pogozheva, I.D., Traynor, J.R., and Mosberg, H.I. (2012) Modulation of opioid receptor ligand affinity and efficacy using active and inactive state receptor models. Chem Biol Drug Des. 80:763-770
Janovick, J.A., Pogozheva, I.D., Mosberg, H.I., Cornea, A., and Conn, P.M. (2012) Rescue of misrouted GnRHR mutants reveals its constitutive activity. Mol. Endocrinol. 26:1179-1188 PMID:22595961
Purington LC, Sobczyk-Kojiro K, Pogozheva ID, Traynor JR, and Mosberg HI. (2011) Development and in vitro characterization of a novel bifunctional μ-agonist/δ-antagonist opioid tetrapeptide. ACS Chem Biol. 6:1375-1381.