The DOI matches its Crossref record; 34 of the 34 references it cites were found in a registry or an index.
Molecular basis for amyloid fibril formation and stability
Open accessAbstract
The molecular structure of the amyloid fibril has remained elusive because of the difficulty of growing well diffracting crystals. By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber. These crystals diffract to high resolution (1 Å) by electron and x-ray diffraction, enabling us to determine a detailed structure for amyloid. The structure reveals that the polypeptides form fibrous crystals composed of antiparallel β-sheets in a cross-β arrangement, characteristic of all amyloid fibers, and allows us to determine the side-chain packing within an amyloid fiber. The antiparallel β-sheets are zipped together by means of π-bonding between adjacent phenylalanine rings and salt-bridges between charge pairs (glutamic acid–lysine), thus controlling and stabilizing the structure. These interactions are likely to be important in the formation and stability of other amyloid fibrils.
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Cites
Structure validation by Cα geometry: ϕ,ψ and Cβ deviation
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Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes
Reches, M., & Gazit, E. (2003) · Science · doi:10.1126/science.1082387 · Cited by 2,530
Common core structure of amyloid fibrils by synchrotron X-ray diffraction 1 1Edited by F. E. Cohen
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Self-citationMcGaughey, G. B., Gagné, M., & Rappé, A. K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15458 · Cited by 1,160
A possible role for π‐stacking in the self‐assembly of amyloid fibrils
Gazit, E. (2002) · The FASEB Journal · doi:10.1096/fj.01-0442hyp · Cited by 1,133
Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand
Tjernberg, L. O., Näslund, J., Lindqvist, F., Johansson, J., Karlström, A. R., Thyberg, J., Terenius, L., & Nordstedt, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8545 · Cited by 963
Self-citationThe structural basis of protein folding and its links with human disease
Dobson, C. M. (2001) · Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences · doi:10.1098/rstb.2000.0758 · Cited by 932
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X-RAY DIFFRACTION STUDIES ON AMYLOID FILAMENTS
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Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing
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Cited by
The FoldX web server: an online force field
Schymkowitz, J., Borg, J., Stricher, F., Nys, R., Rousseau, F., & Serrano, L. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki387 · Cited by 2,759
“For protein aggregation no such detail is available, although recently the first ever crystal structure of an amyloid fibre was released (23).”
BackgroundProtein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
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Metadata
- Authors
- Makin, O. S., Atkins, E., Sikorski, P., Johansson, J., & Serpell, L. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-01-03
- Volume
- 102
- Issue
- 2
- Pages
- 315-320
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2161163255
- Cited by
- 657
- References
- 34
- FWCI
- 31.38
- Type
- journal article
- Language
- en
- Open access
- green
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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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