ApoE Publications List

Abstracts available for recent papers


  • Frieden, C. and Garai, K. (2012) Structural differences between apoE3 and apoE4 may be useful in developing therapeutic agents for Alzheimer's disease. PNAS (E-pub ahead of print.) [Abstract]


  • Shu, Q., Crick, S.L., Pinkner, J.S., Ford, B., Hultgren, S.J. and Frieden, C. (2012) The E. coli CsgB nucleator of curli assembles to beta-sheet oligomers that alter the CsgA fibrillization mechanism. PNAS 109, 6502-6507. [Abstract]


  • Huang, R.Y., Garai, K., Frieden, C. and Gross, M.L. (2011) Hydrogen/deuterium exchange and electron-transfer dissociation mass spectrometry determine the interface and dynamics of apolipoprotein E oligomerization. Biochemistry 50, 9273-9282. [Abstract]


  • Gau, B.C., Garai, K., Frieden, C. and Gross, M.L. (2011) Mass spectrometry-based protein footprinting characterizes the structures of oligomeric apolipoprotein E2, E3, and E4. Biochemistry 50, 8117-8126. [Abstract]


  • Garai, K., Baban, B. and Frieden, C. (2011) The self-association and stability of the APOE isoforms at low pH: Implications for APOE-lipid interactions. J Mol Biol 50, 6356-6364. [Abstract]


  • Garai, K., Baban, B. and Frieden, C. (2011) Dissociation of apolipoprotein E oligomers to monomer is required for high-affinity bidning to phospholipid vescicles. Biochemistry 50, 2550-2558. [Abstract]


  • Garai, K. and Frieden, C. (2010) The association-dissociation behavior fo the ApoE proteins: Kinetic and equilibrium Studies Biochemistry 49:9533-9541. [Abstract]


  • Garai, K., Mustafi, S.M., Baban, B. and Frieden, C. Structural differences between apolipoprotein E3 and E4 as measured by (19)F NMR. Protein Sci. 19, 66-74. (2010). [Abstract]


  • Garai, K., Mustafi, S.M., Baban, B. and Frieden, C. (2009) Structural differences between apolipoprotein E3 and E4 as measured by (19)F- NMR Protein Sci, 106, 20324-20329 [Abstract]


  • Zhang, R., Hu, X., Khant, H., Ludtke, S.J., Chiu, W., Schmeid, M.F., Frieden, C. and Lee, J.M. (2009) Interprotofiliment interactions between Alzheimer's A{beta}1-42 peptides in amyloid fibrils revealed by cryoEM. PNAS, 103, 4653-4658. [Abstract]