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研究领域

Amyloid A b peptide in Alzheimer’s pathogenesis; gamete recognition

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Nussbaum J, Schilling S, Cynis H, Silva A, Swanson E, Wangsanut T, Tayler K, Wiltgen B, Hatami A, Rönicke R, Hutter-Paier B, Reymann K, Alexandru A, Jagla W, Graubner S, Glabe C, Demuth HU, Bloom GS (2012) Prion-Like Behavior and Tau-dependent Cytotoxicity of beta-Amyloid Oligomers Seeded by Pyroglutamylated beta-Amyloid. Nature Accepted for publication. Laganowsky A, Liu C, Sawaya MR, Whitelegge JP, Park J, Zhao M, Pensalfini A, Soriaga AB, Landau M, Teng PK, Cascio D, Glabe C, Eisenberg D (2012) Atomic view of a toxic amyloid small oligomer. Science 335:1228-1231. Lasagna-Reeves CA, Glabe CG, Kayed R (2011) Amyloid-{beta} Annular Protofibrils Evade Fibrillar Fate in Alzheimer Disease Brain. J Biol Chem 286:22122-22130. Kayed R, Canto I, Breydo L, Rasool S, Lukacsovich T, Wu J, Albay R, 3rd, Pensalfini A, Yeung S, Head E., March, J.L., and Glabe, CG. 2010. Conformation dependent monoclonal antibodies distinguish different replicating strains or conformers of prefibrillar Abeta oligomers. Mol Neurodegener, 5:57. Wu, JW, Breydo, L, Isas, JM, Lee, J, Kuznetsov, YG, Langen, R, Glabe, C. 2010. Fibrillar Oligomers Nucleate the Oligomerization of Monomeric Amyloid {beta} but Do Not Seed Fibril Formation. J. Biol. Chem. 285(9):6071-6079. Deshpande, A., H. Kawai, R. Metherate, C. G. Glabe, and J. Busciglio. 2009. A role for synaptic zinc in activity-dependent Abeta oligomer formation and accumulation at excitatory synapses. J Neurosci 29:4004-4015. Mina, E. W., C. Lasagna-Reeves, C. G. Glabe, and R. Kayed. 2009. Poloxamer 188 copolymer membrane sealant rescues toxicity of amyloid oligomers in vitro. J Mol Biol 391:577-585. Tomic, J. L., A. Pensalfini, E. Head, and C. G. Glabe. 2009. Soluble fibrillar oligomer levels are elevated in Alzheimer's disease brain and correlate with cognitive dysfunction. Neurobiol Dis. 35:352-358. Kayed, R., A. Pensalfini, L. Margol, Y. Sokolov, F. Sarsoza, E. Head, J. Hall, and C. Glabe. 2009. Annular protofibrils are a structurally and functionally distinct type of amyloid oligomer. J Biol Chem 284:4230-4237.

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