The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Surfactant properties of Alzheimer's A beta peptides and the mechanism of amyloid aggregation.
Open accessAbstract
The major proteinaceous component of amyloid deposits associated with Alzheimer's disease is a self-assembling 40-42-residue peptide, known as A beta, which is generated by the proteolytic processing of the amyloid precursor protein (Kang, J., Lemaire, H. G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K. H., Multhaup, G., Beyreuther, K., and Muller-Hill, B. (1987) Nature 325, 733-736; Haass, C., Hung, A. Y., Schlossmacher, M. G., Oltersdorf, T., Teplow, D. B., and Selkoe, D. J. (1993) Ann. N. Y. Acad. Sci. 695, 109-116; Estus, S., Golde, T. E., and Younkin S. G. (1992) Ann. N. Y. Acad. Sci. 674, 138-148) and is implicated as one of the causal factors in the pathology of the disease. A beta is now shown to display properties commonly associated with surfactants or detergents, which form micelles in solution. Increasing concentrations of A beta lower the surface tension of water up to a critical concentration, above which little further decrease in surface tension is observed. At concentrations above this critical concentration, increasing amounts of non-covalent aggregates of A beta are observed. A beta aggregation is also correlated with the formation of a hydrophobic environment that excludes water. The extent of this hydrophobic environment, as reflected by the partitioning of hydrophobic fluorescent probes, is much higher for the longer A beta 1-42 isoform, which may be more intimately associated with Alzheimer's disease pathology than A beta 1-40. Although the solution structure of A beta is not yet known, these results suggest that the structure of A beta has the same type of axial amphipathic organization as detergent molecules and that the same principles that govern micelle formation may also apply to A beta aggregation and amyloid fibril self-assembly.
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
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides
Yankner, B. A., Duffy, L. K., & Kirschner, D. A. (1990) · Science · doi:10.1126/science.2218531 · Cited by 1,975
Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774
Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014
Self-citation
Cited by
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009
Structural Classification of Toxic Amyloid Oligomers
Glabe, C. G. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800016200 · Cited by 783
Self-citationNecula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680
Self-citationCommon mechanisms of amyloid oligomer pathogenesis in degenerative disease
Glabe, C. G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.04.017 · Cited by 569
Self-citationWeldon, D. T., Rogers, S. D., Ghilardi, J. R., Finke, M. P., Cleary, J. P., O’Hare, E., Esler, W. P., Maggio, J. E., & Mantyh, P. W. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-06-02161.1998 · Cited by 348
β-Amyloid Activates the O⨪2 Forming NADPH Oxidase in Microglia, Monocytes, and Neutrophils
Della Bianca, V., Dusi, S., Bianchini, E., Dal Prà, I., & Rossi, F. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.22.15493 · Cited by 324
Amyloid β-protein oligomers and Alzheimer’s disease
Hayden, E. Y., & Teplow, D. B. (2013) · Alzheimer's Research & Therapy · doi:10.1186/alzrt226 · Cited by 276
Intracellular Mechanisms of Amyloid Accumulation and Pathogenesis in Alzheimer's Disease
Glabe, C. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:137 · Cited by 222
Self-citationMethylene Blue Inhibits Amyloid Aβ Oligomerization by Promoting Fibrillization
Necula, M., Breydo, L., Milton, S., Kayed, R., van der Veer, W. E., Tone, P., & Glabe, C. G. (2007) · Biochemistry · doi:10.1021/bi700411k · Cited by 213
Self-citationCan a Bacterial Endotoxin be a Key Factor in the Kinetics of Amyloid Fibril Formation?
Asti, A., & Gioglio, L. (2014) · Journal of Alzheimer's Disease · doi:10.3233/jad-131394 · Cited by 180
Kuo, Y.-M., Webster, S., Emmerling, M. R., De Lima, N., & Roher, A. E. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(98)00014-3 · Cited by 122
Human apolipoprotein A–I binds amyloid-β and prevents Aβ-induced neurotoxicity
Paula-Lima, A. C., Tricerri, M. A., Brito-Moreira, J., Bomfim, T. R., Oliveira, F. F., Magdesian, M. H., Grinberg, L. T., Panizzutti, R., & Ferreira, S. T. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.12.003 · Cited by 121
Tseng, B. P., Esler, W. P., Clish, C. B., Stimson, E. R., Ghilardi, J. R., Vinters, H. V., Mantyh, P. W., Lee, J. P., & Maggio, J. E. (1999) · Biochemistry · doi:10.1021/bi990718v · Cited by 119
Yang, A. J., Chandswangbhuvana, D., Shu, T., Henschen, A., & Glabe, C. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20650 · Cited by 108
Self-citationPy, N. A., Bonnet, A. E., Bernard, A., Marchalant, Y., Charrat, E., Checler, F., Khrestchatisky, M., Baranger, K., & Rivera, S. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00247 · Cited by 76
Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.
Iljina, M., Garcia, G. A., Dear, A. J., Flint, J., Narayan, P., Michaels, T. C. T., Dobson, C. M., Frenkel, D., Knowles, T. P. J., & Klenerman, D. (2016) · Scientific Reports · doi:10.1038/srep28658 · Cited by 68
Potentiation of beta-folding of β-amyloid peptide 25–35 by aluminum salts
Bondy, S. C., & Truong, A. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00307-9 · Cited by 39
Lambert, M., Velasco, P., Viola, K., & Klein, W. (2009) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152709787601876 · Cited by 29
Metadata
- Authors
- Soreghan, B., Kosmoski, J., & Glabe, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-11
- Volume
- 269
- Issue
- 46
- Pages
- 28551-28554
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1503503847
- Cited by
- 267
- References
- 5
- FWCI
- 5.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
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.
