The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Exploring the sequence determinants of amyloid structure using position-specific scoring matrices
Open accessAbstract
Protein aggregation results in β-sheet–like assemblies that adopt either a variety of amorphous morphologies or ordered amyloid-like structures. These differences in structure also reflect biological differences; amyloid and amorphous β-sheet aggregates have different chaperone affinities, accumulate in different cellular locations and are degraded by different mechanisms. Further, amyloid function depends entirely on a high intrinsic degree of order. Here we experimentally explored the sequence space of amyloid hexapeptides and used the derived data to build Waltz, a web-based tool that uses a position-specific scoring matrix to determine amyloid-forming sequences. Waltz allows users to identify and better distinguish between amyloid sequences and amorphous β-sheet aggregates and allowed us to identify amyloid-forming regions in functional amyloids.
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Cites
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 · cited 1×
“Therefore, we modeled a set of hexapeptides from amyloid-related disease proteins into available parallel and antiparallel fibril structures and evaluated their energy using Fold”
MethodSelf-citationInclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979
Rationalization of the effects of mutations on peptide andprotein aggregation rates
Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072
Misfolded proteins partition between two distinct quality control compartments
Kaganovich, D., Kopito, R., & Frydman, J. (2008) · Nature · doi:10.1038/nature07195 · Cited by 932
Cited by
Strengthening relationships: amyloids create adhesion nanodomains in yeasts
Lipke, P. N., Garcia, M. C., Alsteens, D., Ramsook, C. B., Klotz, S. A., & Dufrêne, Y. F. (2012) · Trends in Microbiology · doi:10.1016/j.tim.2011.10.002 · Cited by 104
Kumar, S., Singh, S. K., Wang, X., Rup, B., & Gill, D. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0414-9 · Cited by 85
Proteins behaving badly: emerging technologies in profiling biopharmaceutical aggregation
Hamrang, Z., Rattray, N. J. W., & Pluen, A. (2013) · Trends in Biotechnology · doi:10.1016/j.tibtech.2013.05.004 · Cited by 75
Sharma, S., Nehru, B., & Saini, A. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.06.011 · Cited by 48
VIPdb, a genetic variant impact predictor database
Hu, Z., Yu, C., Furutsuki, M., Andreoletti, G., Ly, M., Hoskins, R., Adhikari, A. N., & Brenner, S. E. (2019) · Human Mutation · doi:10.1002/humu.23858 · Cited by 37
Metadata
- Authors
- Maurer-Stroh, S., Debulpaep, M., Kuemmerer, N., de la Paz, M. L., Martins, I. C., Reumers, J., Morris, K. L., Copland, A., Serpell, L., Serrano, L., Schymkowitz, J. W. H., & Rousseau, F.
- Venue
- Nature Methods
- Published
- 2010-02-14
- Volume
- 7
- Issue
- 3
- Pages
- 237-242
- ISSN
- 1548-7091 (ISSN-L)
- 1548-7105
- OpenAlex
- W2043876754
- Cited by
- 680
- References
- 4
- FWCI
- 17.01
- Type
- journal article
- Language
- en
- Open access
- green
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- Maurer-Stroh, S., Debulpaep, M., Kuemmerer, N., de la Paz, M. L., Martins, I. C., Reumers, J., Morris, K. L., Copland, A., Serpell, L., Serrano, L., Schymkowitz, J. W. H., & Rousseau, F. (2010). Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nature Methods. https://doi.org/10.1038/nmeth.1432
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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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