The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
On the nucleation of amyloid β‐protein monomer folding
Open accessAbstract
Neurotoxic assemblies of the amyloid β‐protein (Aβ) have been linked strongly to the pathogenesis of Alzheimer's disease (AD). Here, we sought to monitor the earliest step in Aβ assembly, the creation of a folding nucleus, from which oligomeric and fibrillar assemblies emanate. To do so, limited proteolysis/mass spectrometry was used to identify protease‐resistant segments within monomeric Aβ(1–40) and Aβ(1–42). The results revealed a 10‐residue, protease‐resistant segment, Ala21–Ala30, in both peptides. Remarkably, the homologous decapeptide, Aβ(21–30), displayed identical protease resistance, making it amenable to detailed structural study using solution‐state NMR. Structure calculations revealed a turn formed by residues Val24–Lys28. Three factors contribute to the stability of the turn, the intrinsic propensities of the Val‐Gly‐Ser‐Asn and Gly‐Ser‐Asn‐Lys sequences to form a β‐turn, long‐range Coulombic interactions between Lys28 and either Glu22 or Asp23, and hydrophobic interaction between the isopropyl and butyl side chains of Val24 and Lys28, respectively. We postulate that turn formation within the Val24–Lys28 region of Aβ nucleates the intramolecular folding of Aβ monomer, and from this step, subsequent assembly proceeds. This model provides a mechanistic basis for the pathologic effects of amino acid substitutions at Glu22 and Asp23 that are linked to familial forms of AD or cerebral amyloid angiopathy. Our studies also revealed that common C‐terminal peptide segments within Aβ(1–40) and Aβ(1–42) have distinct structures, an observation of relevance for understanding the strong disease association of increased Aβ(1–42) production. Our results suggest that therapeutic approaches targeting the Val24–Lys28 turn or the Aβ(1–42)‐specific C‐terminal fold may hold promise.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538
Amyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Self-citationIsolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209
Self-citationAmyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Self-citationAllan Butterfield, D. (2002) · Free Radical Research · doi:10.1080/1071576021000049890 · Cited by 786
Grabowski, T. J., Cho, H. S., Vonsattel, J. P. G., Rebeck, G. W., & Greenberg, S. M. (2001) · Annals of Neurology · doi:10.1002/ana.1009 · Cited by 523
Cited by
Amyloid β-Protein Assembly and Alzheimer Disease
Roychaudhuri, R., Yang, M., Hoshi, M. M., & Teplow, D. B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.r800036200 · Cited by 615
Self-citationStabilization of neurotoxic Alzheimer amyloid-β oligomers by protein engineering
Sandberg, A., Luheshi, L. M., Söllvander, S., Pereira de Barros, T., Macao, B., Knowles, T. P. J., Biverstål, H., Lendel, C., Ekholm-Petterson, F., Dubnovitsky, A., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1001740107 · Cited by 358
Weggen, S., & Beher, D. (2012) · Alzheimer's Research & Therapy · doi:10.1186/alzrt107 · Cited by 192
Structure-based inhibitors of amyloid beta core suggest a common interface with tau
Griner, S. L., Seidler, P., Bowler, J., Murray, K. A., Yang, T. P., Sahay, S., Sawaya, M. R., Cascio, D., Rodriguez, J. A., Philipp, S., et al. (2019) · eLife · doi:10.7554/elife.46924 · Cited by 121
Lin, Y.-S., Bowman, G. R., Beauchamp, K. A., & Pande, V. S. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2011.12.002 · Cited by 111
Metadata
- Authors
- Lazo, N. D., Grant, M. A., Condron, M. C., Rigby, A. C., & Teplow, D. B.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2005-06
- Volume
- 14
- Issue
- 6
- Pages
- 1581-1596
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2000659036
- Cited by
- 331
- References
- 12
- FWCI
- 10.77
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: On the nucleation of amyloid β‐protein monomer folding. https://app.cochat.ai/papers/10.1110/ps.041292205
- The paper
- Lazo, N. D., Grant, M. A., Condron, M. C., Rigby, A. C., & Teplow, D. B. (2005). On the nucleation of amyloid β‐protein monomer folding. Protein Science. https://doi.org/10.1110/ps.041292205
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
