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Aggregated protein structures, channels

Lashuel, H. A., Petre, B. M., Wall, J., Simon, M., Nowak, R. J., Walz, T., and Lansbury, P. T., Jr. (2002). Alpha-synuclein, especially the Parkinson s disease-associated mutants, forms pore-like annular and tubular protofibrils./. Mol. Biol. 322,1089-1102. LeVine, H. (1993). Thioflavine T interaction with synthetic Alzheimer s disease beta-amyloid peptides Detection of amyloid aggregation in solution. Protein Sci. 2, 404—410. Lin, H., Bhatia, R., and Lai, R. (2001). Amyloid beta protein forms ion channels Implications for Alzheimer s disease pathophysiology. FASEB J. 15, 2433-2444. Lorenzo, A., and Yankner, B. A. (1994). Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc. Natl. Acad. Sci. USA 91, 12243-12247. Luhrs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Dobeli, H., Schubert, D., and Riek, R. (2005). 3D structure of Alzheimer s amyl o id-( be la) (1—12) fibrils. Proc. Natl. Acad. Sci. USA 102, 17342-17347. [Pg.232]

Channel-forming proteins exhibit a number of structural motifs the influenza virus M2 proton channel and voltage-gated channels for K+, Na+ and Ca2+are all composed of four identical subunits that aggregate to form a central pore as shown in Fig. 5.7 an acid sensing Na+ ion channel has a similar structure but with threefold symmetry Ca2+ release channels, the divalent metal ion transporter CorA, the... [Pg.161]

Hong et al. discussed recent advances in using SSNMR to study K and H" " channels, Ca + pumps, G protein-coupled receptors, bacterial outer membrane proteins, and viral fusion proteins to elucidate their mechanisms of action at the membrane. Shi and Ladizhansky underlined that SSNMR has become a prominent method for the characterization of insoluble proteins and protein aggregates such as amyloid fibrils and membrane-lipid complexes. Im et al. developed SSNMR ensemble dynamics (SSNMR-ED) using multiple conformer models, which generates an ensemble of structures that satisfies the experimental observables without any fitting parameters. [Pg.386]


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Aggregates structure

Channel structures

Channels protein

Protein aggregates

Structure aggregation

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