The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Fibril structure of amyloid-β(1–42) by cryo–electron microscopy
Open accessAbstract
Elucidating pathological fibril structure: Amyloid-β (Aβ) is a key pathological contributor to Alzheimer's disease. Gremer et al. used cryoelectron microscopy data to build a high-quality de novo atomic model of Aβ fibrils (see the Perspective by Pospich and Raunser). The complete structure reveals all 42 amino acids (including the entire N terminus) and provides a structural basis for understanding the effect of several disease-causing and disease-preventing mutations. The fibril consists of two intertwined protofilaments with an unexpected dimer interface that is different from those proposed previously. The structure has implications for the mechanism of fibril growth and will be an important stepping stone to rational drug design. Science , this issue p. 116 ; see also p. 45
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PHENIX : a comprehensive Python-based system for macromolecular structure solution
Adams, P. D., Afonine, P. V., Bunkóczi, G., Chen, V. B., Davis, I. W., Echols, N., Headd, J. J., Hung, L.-W., Kapral, G. J., Grosse-Kunstleve, R. W., et al. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444909052925 · Cited by 23,716
Overview of the CCP 4 suite and current developments
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The amyloid hypothesis of Alzheimer's disease at 25 years
Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164
Towards automated crystallographic structure refinement with phenix.refine
Afonine, P. V., Grosse-Kunstleve, R. W., Echols, N., Headd, J. J., Moriarty, N. W., Mustyakimov, M., Terwilliger, T. C., Urzhumtsev, A., Zwart, P. H., & Adams, P. D. (2012) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444912001308 · Cited by 5,511
The amyloid state and its association with protein misfolding diseases.
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Cryo-EM structures of tau filaments from Alzheimer’s disease
Fitzpatrick, A. W. P., Falcon, B., He, S., Murzin, A. G., Murshudov, G., Garringer, H. J., Crowther, R. A., Ghetti, B., Goedert, M., & Scheres, S. H. W. (2017) · Nature · doi:10.1038/nature23002 · Cited by 2,061
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Fu, H., Hardy, J., & Duff, K. E. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0221-2 · Cited by 585
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Metadata
- Authors
- Gremer, L., Schölzel, D., Schenk, C., Reinartz, E., Labahn, J., Ravelli, R. B. G., Tusche, M., Lopez-Iglesias, C., Hoyer, W., Heise, H., Willbold, D., & Schröder, G. F.
- Venue
- Science
- Published
- 2017-10-06
- Volume
- 358
- Issue
- 6359
- Pages
- 116-119
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2753860285
- Cited by
- 1,041
- References
- 7
- FWCI
- 66.61
- Type
- journal article
- Language
- en
- Open access
- bronze
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- CoChat. (2026). Citation check: Fibril structure of amyloid-β(1–42) by cryo–electron microscopy. https://app.cochat.ai/papers/10.1126/science.aao2825
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- Gremer, L., Schölzel, D., Schenk, C., Reinartz, E., Labahn, J., Ravelli, R. B. G., Tusche, M., Lopez-Iglesias, C., Hoyer, W., Heise, H., Willbold, D., & Schröder, G. F. (2017). Fibril structure of amyloid-β(1–42) by cryo–electron microscopy. Science. https://doi.org/10.1126/science.aao2825
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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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