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Welcome to the Zagorski Lab


PUBLICATIONS


\x93Structure Dependent Inhibition of b-Fibrillogenesis by Melatonin,\x94 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]

\x93Amyloid Aggregation Inhibitors,\x94 M. G. Zagorski, IDrugs, 1998, 1, 17-18.38.

\x93Solution Structure Model of Residues 1-28 of the Amyloid b-Peptide When Bound to Micelles,\x94 K. J. Marcinowski, H. Shao, E. L. Clancy, and M. G. Zagorski, J. Am. Chem. Soc., 1998, 120, 11082-11091. [download PDF]

\x93Solution Structures of Micelle-Bound Amyloid Ab-(1-40) and Ab-(1-42) Peptides of Alzheimer's Disease,\x94 H. Shao, S.-C. Jao, K. Ma, and M. G. Zagorski, J. Mol. Biol., 1999, 285, 755-773. [download PDF]

\x93The Molecular Mechanism of Amyloidosis in Alzheimer's Disease,\x94 M. G. Zagorski, in \x93The Biology-Chemistry Interface,\x94 eds., R. Cooper and J. K. Snyder, Marcel Dekker, 1999, 14, 397-430.

\x93Methodological and Chemical Factors Affecting Ab Peptide Amyloidogenicity,\x94 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.

\x93Dual Anti-amyloidogenic and Antioxidant Properties of Melatonin: A New Therapy for Alzheimer's Disease?\x94, 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 \x93Alzheimer's Disease and Related Disorders\x94, eds., K. Iqbal, D. F. Swaab, and H. M. Wisniewski, Wiley & Sons Ltd., 1999, 661-669

\x93Residue Specific pKa Measurements of the b-Peptide and Mechanism of pH-Induced Amyloid Formation,\x94 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]

\x93Solution Structure of the E200K Variant of Human Prion Protein,\x94 Y. Zhang, W. Swietnicki, M. G. Zagorski, W. K. Surewicz, and F. D. S\xF6nnichsen, J. Biol. Chem., 2000, 275, 33650-33654. [download PDF]

\x93Nicotine and Amyloid Formation,\x94 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]

\x93Melatonin Reverses the Profibrillogenic Activity of Apolipoprotein E4 on the Alzheimer Amyloid Ab Protein,\x94 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]

\x93Methionine 35 Oxidation Reduces Fibril Assembly of the Amyloid Ab-(1-42) Peptide of Alzheimer's Disease,\x94 L. Hou, I. Kang, R. E. Marchant, and M. G. Zagorski, J. Biol. Chem., 2002, 277, 40173-40176. [download PDF]

\x93Intramolecular Quenching of Tryptophan Fluorescence by the Peptide Bond in Cyclic Hexapeptides,\x94 P. D. Adams, Y. Chen, K. Ma, M. G. Zagorski, F. D. S\xF6nnichsen, M. L. McLaughlin, and M. D. Barkley, J. Am. Chem. Soc., 2002, 124, 9278-9286. [download PDF]

\x93pH-Dependent Amyloid and Protofibril Formation by the ABri Peptide of Familial British Dementia,\x94 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]

\x93ABri peptide Associated with Familial British Dementia Forms Annular and Ring-Like Protofibrillar Structures,\x94 R. Srinivasan, R. E. Marchant, and M. G. Zagorski, Amyloid: Int. J. Exp. Clin. Invest, 2004, 11, 10-13. [download PDF]

\x93Solution NMR Studies of the Ab(1-40) and Ab(1-42) Peptides Establish that the Met35 Oxidation State Affects the Mechanism of Amyloid Formation,\x94 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]

\x93Sorting Out the Driving Forces for Parallel and Antiparallel Alignments in the Ab Peptide Fibril Structure,\x94 L. Hou and M. G. Zagorski, Biophys. J., 2004, 86, 1-2. [download PDF]

\x93Raman Spectroscopic Characterization of Secondary Structure in Natively Unfolded Proteins: a-Synuclein,\x94 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]

\x93Secondary Structure of a-Synuclein Oligomers: Characterization by Raman and Atomic Force Microscopy,\x94 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]

\x93Production of Native Protofibril Structures from Aggregation of a-Synuclein in Methanol-Water Solutions,\x94 M. M. Apetri, R. Srinivasan, V. E. Anderson, and M. G. Zagorski, J. Biol. Chem., submitted.

\x93NMR Reveals Anomalous Copper(II) Binding to the Amyloid Ab Peptide of Alzheimer's Disease,\x94 L. Hou and M. G. Zagorski, J. Am. Chem. Soc., 2006, 128, 9260-9261. [download PDF]

\x93NMR Uncovers a Unique Binding Motif Between a-Synuclein and Tau,\x94 M. M. Apetri, V. Lee, D. Eliezer, and M. G. Zagorski, Protein Science, submitted.