The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
Open accessAbstract
Observations that β-sheet proteins form amyloid fibrils under at least partially denaturing conditions has raised questions as to whether these fibrils assemble by docking of preformed β-structure or by association of unfolded polypeptide segments. By using α-helical protein apomyoglobin, we show that the ease of fibril assembly correlates with the extent of denaturation. By contrast, monomeric β-sheet intermediates could not be observed under the conditions of fibril formation. These data suggest that amyloid fibril formation from apomyoglobin depends on disordered polypeptide segments and conditions that are selectively unfavorable to folding. However, it is inevitable that such conditions often stabilize protein folding intermediates.
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Cites
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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
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Self-citationDesigning conditions for in vitro formation of amyloid protofilaments and fibrils
Chiti, F., Webster, P., Taddei, N., Clark, A., Stefani, M., Ramponi, G., & Dobson, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3590 · Cited by 1,039
Self-citationThe structural basis of protein folding and its links with human disease
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Self-citationAmyloid fibrils from muscle myoglobin
Fändrich, M., Fletcher, M. A., & Dobson, C. M. (2001) · Nature · doi:10.1038/35065514 · Cited by 799
Self-citationThe behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
Fandrich, M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf573 · Cited by 525
Polyproline II structure in a sequence of seven alanine residues
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The Amyloid State of Proteins in Human Diseases
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AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides
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FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Zandomeneghi, G., Krebs, M. R. H., McCammon, M. G., & Fändrich, M. (2004) · Protein Science · doi:10.1110/ps.041024904 · Cited by 725
Self-citationPepys, M. B. (2006) · Annual Review of Medicine · doi:10.1146/annurev.med.57.121304.131243 · Cited by 559
Prediction of Aggregation-Prone Regions in Structured Proteins
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Metadata
- Authors
- Fändrich, M., Forge, V., Buder, K., Kittler, M., Dobson, C. M., & Diekmann, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2003-12-09
- Volume
- 100
- Issue
- 26
- Pages
- 15463-15468
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2002115616
- Cited by
- 280
- References
- 35
- FWCI
- 6.11
- Type
- journal article
- Language
- en
- Open access
- green
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- Fändrich, M., Forge, V., Buder, K., Kittler, M., Dobson, C. M., & Diekmann, S. (2003). Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0303758100
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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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