The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Atomic View of a Toxic Amyloid Small Oligomer
Open accessAbstract
A Toxic Barrel: Many studies have suggested that oligomers are an important toxic species in amyloid diseases such as Alzheimer's disease. In an effort to better define these oligomers, Laganowsky et al. (p. 1228 ) identified a segment of the fibril-forming protein αB crystalline (ABC) that forms both amyloid fibrils and a relatively stable oligomer. ABC oligomers were toxic in a cell viability assay and were recognized by an amyloid-oligomer–specific antibody. A crystal structure of the oligomers showed that six peptides formed an antiparallel barrel termed a cylindrin. Amyloid oligomers are likely to be structurally polymorphic, but cylindrin-like assemblies offer a model for these elusive structures.
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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
Coot : model-building tools for molecular graphics
Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571
Phaser crystallographic software
McCoy, A. J., Grosse-Kunstleve, R. W., Adams, P. D., Winn, M. D., Storoni, L. C., & Read, R. J. (2007) · Journal of Applied Crystallography · doi:10.1107/s0021889807021206 · Cited by 20,612
Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914
Kabsch, W. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909047337 · Cited by 16,463
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111
Structural Classification of Toxic Amyloid Oligomers
Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783
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Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
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Viola, K. L., & Klein, W. L. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1386-3 · Cited by 628
The activities of amyloids from a structural perspective
Riek, R., & Eisenberg, D. S. (2016) · Nature · doi:10.1038/nature20416 · Cited by 508
Self-citationAmylin deposition in the brain: A second amyloid in Alzheimer disease?
Jackson, K., Barisone, G. A., Diaz, E., Jin, L., DeCarli, C., & Despa, F. (2013) · Annals of Neurology · doi:10.1002/ana.23956 · Cited by 340
Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer’s disease
Thal, D. R., Walter, J., Saido, T. C., & Fändrich, M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1375-y · Cited by 319
Metadata
- Authors
- Laganowsky, A., Liu, C., Sawaya, M. R., Whitelegge, J. P., Park, J., Zhao, M., Pensalfini, A., Soriaga, A. B., Landau, M., Teng, P. K., Cascio, D., Glabe, C., & Eisenberg, D.
- Venue
- Science
- Published
- 2012-03-09
- Volume
- 335
- Issue
- 6073
- Pages
- 1228-1231
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2082923159
- Cited by
- 563
- References
- 13
- FWCI
- 43.40
- Type
- journal article
- Language
- en
- Open access
- green
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- Laganowsky, A., Liu, C., Sawaya, M. R., Whitelegge, J. P., Park, J., Zhao, M., Pensalfini, A., Soriaga, A. B., Landau, M., Teng, P. K., Cascio, D., Glabe, C., & Eisenberg, D. (2012). Atomic View of a Toxic Amyloid Small Oligomer. Science. https://doi.org/10.1126/science.1213151
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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