Assistant Professor Nathan N. Alder
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Assistant Professor Nathan N. Alder
Dept. Molecular & Cell Biology
U3125
University of Connecticut
Storrs, CT 06268
Telephone:
Fax: 860-486-4331
E-Mail: nathan.alder@uconn.edu
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Education: Ph.D., University of California, Davis; Postdoctoral study, Texas A&M University
Research Interests: Analysis of the structure, function, and biogenesis of membrane proteins using multiple techniques, primarily fluorescence spectroscopy, and employing yeast as a model system; mitochondrial protein trafficking and assembly; high-resolution fluorescence-based mapping of membrane proteins and analysis of conformational dynamics.
Selected Publications:
Alder, N.N., Jensen, R.E., and Johnson, A.E. Fluorescence mapping of mitochondrial TIM23 complex reveals a water-facing, substrate-interacting helix surface. Cell (In press).
Alder, N.N., Sutherland, J., Buhring, A.I., Jensen, R.E., and Johnson A.E. (2008). Quaternary structure of the mitochondrial TIM23 complex reveals dynamic association between Tim23p and other subunits. Molecular Biology of the Cell 19, 159-170.
Davis, A.J., Alder, N.N., Jensen, R.E., and Johnson, A.E. (2007). The Tim9p/10p and Tim8p/13p complexes bind to specific sites on Tim23p during mitochondrial protein import. Molecular Biology of the Cell 18, 475-486.
Alder, N.N., Shen, Y., Brodsky, J.L., Hendershot, L.M., and Johnson, A.E. (2005). The molecular mechanisms underlying BiP-mediated gating of the Sec61 translocon of the endoplasmic reticulum. The Journal of Cell Biology 168, 389-399.
Alder, N.N. and Johnson, A.E. (2004). Cotranslational membrane protein biogenesis at the endoplasmic reticulum. The Journal of Biological Chemistry 279, 22787-22790.
Alder, N.N. and Theg, S.M. (2003). Energy use by biological protein transport pathways. Trends in Biochemical Sciences 28, 442-451.
Alder, N.N. and Theg, S.M. (2003). Energetics of protein transport across biological membranes: a study of the thylakoid ΔpH/cpTat pathway. Cell 112, 231-242.
Alder, N.N. and Theg, S.M. (2003). Protein transport via the cpTat pathway displays cooperativity and is stimulated by transport-incompetent substrate. FEBS Letters 540, 96-100.
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