The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Aβ40-Lactam(D23/K28) Models a Conformation Highly Favorable for Nucleation of Amyloid
Abstract
Recent solid-state NMR data (1) demonstrate that Abeta(1)(-)(40) adopts a conformation in amyloid fibrils with two in-register, parallel beta-sheets, connected by a bend structure encompassing residues D(23)VGSNKG(29), with a close contact between the side chains of Asp23 and Lys28. We hypothesized that forming this bend structure might be rate-limiting in fibril formation, as indicated by the lag period typically observed in the kinetics of Abeta(1)(-)(40) fibrillogenesis. We synthesized Abeta(1)(-)(40)-Lactam(D23/K28), a congener Abeta(1)(-)(40) peptide that contains a lactam bridge between the side chains of Asp23 and Lys28. Abeta(1)(-)(40)-Lactam(D23/K28) forms fibrils similar to those formed by Abeta(1)(-)(40). The kinetics of fibrillogenesis, however, occur without the typical lag period, and at a rate approximately 1000-fold greater than is seen with Abeta(1)(-)(40) fibrillogenesis. The strong tendency toward self-association is also shown by size exclusion chromatography in which Abeta(1)(-)(40)-Lactam(D23/K28) forms oligomers even at concentrations of approximately 1-5 microM. Under the same conditions, Abeta(1)(-)(40) shows no detectable oligomers by size exclusion chromatography. Our data suggest that Abeta(1)(-)(40)-Lactam(D23/K28) could bypass an unfavorable folding step in fibrillogenesis, because the lactam linkage "preforms" a bendlike structure in the peptide. Consistent with this view Abeta(1)(-)(40) growth is efficiently nucleated by Abeta(1)(-)(40)-Lactam(D23/K28) fibril seeds.
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
Klunk, W. E., Jacob, R. F., & Mason, R. P. (1999) · Analytical Biochemistry · doi:10.1006/abio.1998.2933 · Cited by 310
Cited by
Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111
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
Self-citationNguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
On the Seeding and Oligomerization of pGlu-Amyloid Peptides (in vitro)
Schilling, S., Lauber, T., Schaupp, M., Manhart, S., Scheel, E., Böhm, G., & Demuth, H.-U. (2006) · Biochemistry · doi:10.1021/bi0612667 · Cited by 254
Inhibitors of Amyloid Toxicity Based on β-sheet Packing of Aβ40 and Aβ42
Sato, T., Kienlen-Campard, P., Ahmed, M., Liu, W., Li, H., Elliott, J. I., Aimoto, S., Constantinescu, S. N., Octave, J.-N., & Smith, S. O. (2006) · Biochemistry · doi:10.1021/bi052485f · Cited by 191
Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin
Ultsch, M., Li, B., Maurer, T., Mathieu, M., Adolfsson, O., Muhs, A., Pfeifer, A., Pihlgren, M., Bainbridge, T. W., Reichelt, M., et al. (2016) · Scientific Reports · doi:10.1038/srep39374 · Cited by 124
Atomic-level differences between brain parenchymal- and cerebrovascular-seeded Aβ fibrils
Scherpelz, K. P., Wang, S., Pytel, P., Madhurapantula, R. S., Srivastava, A. K., Sachleben, J. R., Orgel, J., Ishii, Y., & Meredith, S. C. (2021) · Scientific Reports · doi:10.1038/s41598-020-80042-5 · Cited by 12
Self-citationVisualizing the energy landscape for a molecular dynamics trajectory
Neuman, V., Wesołowski, P. A., Bojarski, K. K., Dewan, D., Schäffler, M., Smardz, P., & Wales, D. J. (2026) · The Journal of Chemical Physics · doi:10.1063/5.0310206 · Cited by 6
Metadata
- Authors
- Sciarretta, K. L., Gordon, D. J., Petkova, A. T., Tycko, R., & Meredith, S. C.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2005-03-30
- Volume
- 44
- Issue
- 16
- Pages
- 6003-6014
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1981735680
- Cited by
- 244
- References
- 1
- FWCI
- 7.30
- Type
- journal article
- Language
- en
- Open access
- closed
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
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.
