case western reserve university


Welcome to the Zagorski Lab


“Structure Dependent Inhibition of b-Fibrillogenesis by Melatonin,” M. Pappolla, P. Bozner, C. Soto, M. Zagorski, H. Shao, N. K. Robakis, B. Frangione, and J. Ghiso, J. Biol. Chem., 1998, 273, 7185-7188. [download PDF]

“Amyloid Aggregation Inhibitors,” M. G. Zagorski, IDrugs, 1998, 1, 17-18.38.

“Solution Structure Model of Residues 1-28 of the Amyloid b-Peptide When Bound to Micelles,” K. J. Marcinowski, H. Shao, E. L. Clancy, and M. G. Zagorski, J. Am. Chem. Soc., 1998, 120, 11082-11091. [download PDF]

“Solution Structures of Micelle-Bound Amyloid Ab-(1-40) and Ab-(1-42) Peptides of Alzheimer's Disease,” H. Shao, S.-C. Jao, K. Ma, and M. G. Zagorski, J. Mol. Biol., 1999, 285, 755-773. [download PDF]

“The Molecular Mechanism of Amyloidosis in Alzheimer's Disease,” M. G. Zagorski, in “The Biology-Chemistry Interface,” eds., R. Cooper and J. K. Snyder, Marcel Dekker, 1999, 14, 397-430.

“Methodological and Chemical Factors Affecting Ab Peptide Amyloidogenicity,” M. G. Zagorski, J. Yang, H. Shao, K. Ma, H. Zeng, and A. Hong, in Amyloid and Other Protein Deposition, ed. R. Wetzel, Methods Enzymology, 1999, 309, 189-204.

“Dual Anti-amyloidogenic and Antioxidant Properties of Melatonin: A New Therapy for Alzheimer's Disease?”, M. A. Pappolla, Y.-J. Chyan, P. Bozner, C. Soto, H. Shao, R. J. Reiter, G. Brewer, N. K. Robakis, M. G. Zagorski, B. Frangione, and J. Ghiso, in “Alzheimer's Disease and Related Disorders”, eds., K. Iqbal, D. F. Swaab, and H. M. Wisniewski, Wiley & Sons Ltd., 1999, 661-669

“Residue Specific pKa Measurements of the b-Peptide and Mechanism of pH-Induced Amyloid Formation,” K. Ma, E. L. Clancy, Y. Zhang, D. G. Ray, K. Wollenberg, and M. G. Zagorski, J. Am. Chem.Soc.,1999,121, 8698-8706. [download PDF]

“Solution Structure of the E200K Variant of Human Prion Protein,” Y. Zhang, W. Swietnicki, M. G. Zagorski, W. K. Surewicz, and F. D. Sönnichsen, J. Biol. Chem., 2000, 275, 33650-33654. [download PDF]

“Nicotine and Amyloid Formation,” H. Zeng, Y. Zhang, L.-J. Peng, H. Shao, N. K. Menon, J. Yang, A. R. Salomon, R. P. Friedland, and M. G. Zagorski, Biol. Psychiat., 2001, 49, 248-257. [download PDF]

“Melatonin Reverses the Profibrillogenic Activity of Apolipoprotein E4 on the Alzheimer Amyloid Ab Protein,” B. Poeggeler, L. Miravelle, M. G. Zagorski, T. Wisniewski, Y.-J. Chyan, Y. Zhang, H. Shao, T. Bryant-Thomas, R. Vidal, B. Frangione, J. Ghiso, and M. Pappolla, Biochemistry, 2001, 40, 14995-15001. [download PDF]

“Methionine 35 Oxidation Reduces Fibril Assembly of the Amyloid Ab-(1-42) Peptide of Alzheimer's Disease,” L. Hou, I. Kang, R. E. Marchant, and M. G. Zagorski, J. Biol. Chem., 2002, 277, 40173-40176. [download PDF]

“Intramolecular Quenching of Tryptophan Fluorescence by the Peptide Bond in Cyclic Hexapeptides,” P. D. Adams, Y. Chen, K. Ma, M. G. Zagorski, F. D. Sönnichsen, M. L. McLaughlin, and M. D. Barkley, J. Am. Chem. Soc., 2002, 124, 9278-9286. [download PDF]

“pH-Dependent Amyloid and Protofibril Formation by the ABri Peptide of Familial British Dementia,” R. Srinivasan, E. M. Jones, K. Liu, J. Ghiso, R. E. Marchant, and M. G. Zagorski, J. Mol. Biol., 2003, 333, 1003-1023. [download PDF]

“ABri peptide Associated with Familial British Dementia Forms Annular and Ring-Like Protofibrillar Structures,” R. Srinivasan, R. E. Marchant, and M. G. Zagorski, Amyloid: Int. J. Exp. Clin. Invest, 2004, 11, 10-13. [download PDF]

“Solution NMR Studies of the Ab(1-40) and Ab(1-42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation,” L. Hou, H. Shao, Y. Zhang, H. Li, N. K. Menon, E. B. Neuhaus, J. M. Brewer, I.-J. Byeon, D. G. Ray, M. P. Vitek, T. Iwashita, R. A. Makula, A. Przybyla, and M. G. Zagorski, J. Am. Chem. Soc., 2004, 126, 1992-2005. [download PDF]

“Sorting Out the Driving Forces for Parallel and Antiparallel Alignments in the Ab Peptide Fibril Structure,” L. Hou and M. G. Zagorski, Biophys. J., 2004, 86, 1-2. [download PDF]

“Raman Spectroscopic Characterization of Secondary Structure in Natively Unfolded Proteins: a-Synuclein,” N. C. Maiti, M. M. Apetri, M. G. Zagorski, P. R. Carey, and V. E. Anderson, J. Am. Chem. Soc., 2004, 126. 2399-2408. [download PDF]

“Secondary Structure of a-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy,” M. M. Apetri, N. C. Maiti, M. G. Zagorski, P. R. Carey, and V. E. Anderson, J. Mol. Biol., 2006, 355, 63-71. [download PDF]

“Production of Native Protofibril Structures from Aggregation of a-Synuclein in Methanol-Water Solutions,” M. M. Apetri, R. Srinivasan, V. E. Anderson, and M. G. Zagorski, J. Biol. Chem., submitted.

“NMR Reveals Anomalous Copper(II) Binding to the Amyloid Ab Peptide of Alzheimer's Disease,” L. Hou and M. G. Zagorski, J. Am. Chem. Soc., 2006, 128, 9260-9261. [download PDF]

“NMR Uncovers a Unique Binding Motif Between a-Synuclein and Tau,” M. M. Apetri, V. Lee, D. Eliezer, and M. G. Zagorski, Protein Science, submitted.