The DOI matches its Crossref record; 27 of the 27 references it cites were found in a registry or an index.
Stabilities and conformations of Alzheimer's β-amyloid peptide oligomers (Aβ 16 – 22 , Aβ 16–35 , and Aβ 10 – 35 ): Sequence effects
Open accessAbstract
Previously, we have studied the minimal oligomer size of an aggregate amyloid seed and the mechanism of seed growth with a multilayer β-sheet model. Under high temperature simulation conditions, our approach can test the stability of possible amyloid forms. Here, we report our study of oligomers of Alzheimer's amyloid β-peptide (Aβ) fragments 16–22, 16–35, and 10–35 (abbreviated Aβ 16–22 , Aβ 16–35 , and Aβ 10–35 , respectively). Our simulations indicate that an antiparallel β-sheet orientation is the most stable for the Aβ 16–22 , in agreement with a solid state NMR-based model [Balbach, J. J., Ishii, Y., Antzutkin, O. N., Leapman, R. D., Rizzo, N. W., et al . (2000) Biochemistry 39, 13748–13759]. A model with twenty-four Aβ 16–22 strands indicates a highly twisted fibril. Whereas the short Aβ 16–22 and Aβ 24–36 may exist in fully extended form, the linear parallel β-sheets for Aβ 16–35 appear impossible, mainly because of the polar region in the middle of the 16–35 sequence. However, a bent double-layered hairpin-like structure (called hook ) with the polar region at the turn forms parallel β-sheets with higher stability. An intra-strand salt-bridge (D23-K28) stabilizes the bent hairpin-like hook structure. The bent double-β-sheet model for the Aβ 10–35 similarly offers oligomer stability.
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CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) · Journal of Computational Chemistry · doi:10.1002/jcc.540040211 · Cited by 14,944
Simulation of activation free energies in molecular systems
Neria, E., Fischer, S., & Karplus, M. (1996) · The Journal of Chemical Physics · doi:10.1063/1.472061 · Cited by 1,322
Alzheimer’s amyloid fibrils: structure and assembly
Serpell, L. C. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00029-6 · Cited by 959
Folding dynamics and mechanism of β-hairpin formation
Muñoz, V., Thompson, P. A., Hofrichter, J., & Eaton, W. A. (1997) · Nature · doi:10.1038/36626 · Cited by 929
Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
Lorenzo, A., Razzaboni, B., Weir, G. C., & Yankner, B. A. (1994) · Nature · doi:10.1038/368756a0 · Cited by 820
Carrell, R. W., & Lomas, D. A. (1997) · The Lancet · doi:10.1016/s0140-6736(97)02073-4 · Cited by 807
Balbach, J. J., Ishii, Y., Antzutkin, O. N., Leapman, R. D., Rizzo, N. W., Dyda, F., Reed, J., & Tycko, R. (2000) · Biochemistry · doi:10.1021/bi0011330 · Cited by 703
Pike, C. J., Walencewicz‐Wasserman, A. J., Kosmoski, J., Cribbs, D. H., Glabe, C. G., & Cotman, C. W. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64010253.x · Cited by 699
Kirkitadze, M. D., Condron, M. M., & Teplow, D. B. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4970 · Cited by 682
The toxicity in vitro of β-amyloid protein
Iversen, L. L., Mortishire-Smith, R. J., Pollack, S. J., & Shearman, M. S. (1995) · Biochemical Journal · doi:10.1042/bj3110001 · Cited by 429
Cited by
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
Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., & Ishii, Y. (2015) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2991 · Cited by 818
Self-citationMonomer adds to preformed structured oligomers of Aβ-peptides by a two-stage dock–lock mechanism
Nguyen, P. H., Li, M. S., Stock, G., Straub, J. E., & Thirumalai, D. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607440104 · Cited by 355
Gsponer, J., Haberthür, U., & Caflisch, A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0835307100 · Cited by 264
Interpreting the Aggregation Kinetics of Amyloid Peptides
Pellarin, R., & Caflisch, A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.05.033 · Cited by 254
Metadata
- Authors
- Ma, B., & Nussinov, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2002-10-21
- Volume
- 99
- Issue
- 22
- Pages
- 14126-14131
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2014451295
- Cited by
- 403
- References
- 27
- FWCI
- 11.76
- Type
- journal article
- Language
- en
- Open access
- green
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