The DOI matches its Crossref record; 55 of the 55 references it cites were found in a registry or an index.
Amyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths
Open accessAbstract
One of the clinical manifestations of Alzheimer's disease is the deposition of the 39-43 residue amyloid-beta (A beta) peptide in aggregated fibrils in senile plaques. Characterization of the aggregation behavior of A beta is one of the critical issues in understanding the role of A beta in the disease process. Using solution hydrodynamics, A beta was observed to form three types of species in phosphate-buffered saline: insoluble aggregates with sedimentation coefficients of approximately 50,000 S and molecular masses of approximately 10(9) Da, "soluble aggregates" with sedimentation coefficients of approximately 30 S and masses of approximately 10(6) Da, and monomer. When starting from monomer, the aggregation kinetics of A beta 1-40 (A beta 40) and A beta 1-42 (A beta 42), alone and in combination, reveal large differences in the tendency of these peptides to aggregate as a function of pH and other solution conditions. At pH 4.1 and 7.0-7.4, aggregation is significantly slower than at pH 5 and 6. Under all conditions, aggregation of the longer A beta 42 was more rapid than A beta 40. Oxidation of Met-35 to the sulfoxide in A beta 40 enhances the aggregation rate over that of the nonoxidized peptide. Aggregation was found to be dependent upon temperature and to be strongly dependent on peptide concentration and ionic strength, indicating that aggregation is driven by a hydrophobic effect. When A beta 40 and A beta 42 are mixed together, A beta 40 retards the aggregation of A beta 42 in a concentration-dependent manner. Shorter fragments have a decreasing ability to interfere with A beta 42 aggregation. Conversely, the rate of aggregation of A beta 40 can be significantly enhanced by seeding slow aggregating solutions with preformed aggregates of A beta 42. Taken together, the inhibition of A beta 42 aggregation by A beta 40, the seeding of A beta 40 aggregation by A beta 42 aggregates, and the chemical oxidation of A beta 40 suggest that the relative abundance and rates of production of different-length A beta and its exposure to radical damage may be factors in the accumulation of A beta in plaques in vivo.
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The increased Aβ 42:40 ratio in oligodendrocytes could contribute to the high proportion of soluble aggregates [28,42,43]”
From Selective suppression of oligodendrocyte-derived amyloid beta rescues neuronal dysfunction in Alzheimer’s disease (2024) · cites this paper as [42]
Experimental — accuracy not yet measured
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
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178
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
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
Amyloid Deposits and Amyloidosis
Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,780
Isolation 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
Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471
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
Neurodegeneration induced by beta-amyloid peptides in vitro: the role of peptide assembly state
Pike, C., Burdick, D., Walencewicz, A., Glabe, C., & Cotman, C. (1993) · The Journal of Neuroscience · doi:10.1523/jneurosci.13-04-01676.1993 · Cited by 1,417
Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,359
Tanzi, R. E., McClatchey, A. I., Lamperti, E. D., Villa‐Komaroff, L., Gusella, J. F., & Neve, R. L. (1988) · Nature · doi:10.1038/331528a0 · Cited by 1,093
Hensley, K., Carney, J. M., Mattson, M. P., Aksenova, M., Harris, M., Wu, J. F., Floyd, R. A., & Butterfield, D. A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.8.3270 · Cited by 1,086
Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity
Kitaguchi, N., Takahashi, Y., Tokushima, Y., Shiojiri, S., & Ito, H. (1988) · Nature · doi:10.1038/331530a0 · Cited by 1,083
A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
Ponte, P. A., Gonzalez‐DeWhitt, P. A., Schilling, J., Miller, J., Hsu, D. K., Greenberg, B., Davis, K. L., Wallace, W., Lieberburg, I. M., Fuller, F. H., et al. (1988) · Nature · doi:10.1038/331525a0 · Cited by 1,050
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
In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity
Pike, C. J., Walencewicz, A. J., Glabe, C. G., & Cotman, C. W. (1991) · Brain Research · doi:10.1016/0006-8993(91)91553-d · Cited by 841
Barrow, C. J., Yasuda, A., Kenny, P. T. M., & Zagorski, M. G. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90106-t · Cited by 644
Vitamin E protects nerve cells from amyloid βprotein toxicity
Behl, C., Davis, J. B., Cole, G. M., & Schubert, D. A. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90837-b · Cited by 582
Aggregation and secondary structure of synthetic amyloid βA4 peptides of Alzheimer's disease
Hilbich, C., Kisters–Woike, B., Reed, J., Masters, C. L., & Beyreuther, K. T. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90881-6 · Cited by 580
Kirschner, D. A., Abraham, C. R., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.2.503 · Cited by 570
An in vivo model for the neurodegenerative effects of beta amyloid and protection by substance P.
Kowall, N. W., Beal, M. F., Busciglio, J. A., Duffy, L. K., & Yankner, B. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.16.7247 · Cited by 529
Hofrichter, J., Ross, P. D., & Eaton, W. A. (1974) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.71.12.4864 · Cited by 520
Stafford, W. F. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90316-y · Cited by 517
Kirschner, D. A., Inouye, H., Duffy, L. K., Sinclair, A. J., Lind, M., & Selkoe, D. J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6953 · Cited by 481
Physiological production of the β-amyloid protein and the mechanism of Alzheimer's disease
Selkoe, D. J. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90008-a · Cited by 423
pH-dependent structural transitions of Alzheimer amyloid peptides
Fraser, P. E., Nguyen, J. T., Surewicz, W. K., & Kirschner, D. A. (1991) · Biophysical Journal · doi:10.1016/s0006-3495(91)82154-3 · Cited by 380
Secondary structure of amyloid beta peptide correlates with neurotoxic activity in vitro.
Simmons, L. K., May, P. C., Tomaselli, K. J., Rydel, R. E., Fuson, K. S., Brigham, E. F., Wright, S., Lieberburg, I. M., Becker, G. W., & Brems, D. N. (1994) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10007-2 · Cited by 371
Mathematical theory of sedimentation analysis
(1962) · Journal of the Franklin Institute · doi:10.1016/0016-0032(62)90836-0 · Cited by 332
Jarrett, J. T., & Lansbury, P. T. (1992) · Biochemistry · doi:10.1021/bi00164a008 · Cited by 325
Halverson, K. J., Fraser, P. E., Kirschner, D. A., & Lansbury, P. T. (1990) · Biochemistry · doi:10.1021/bi00463a003 · Cited by 292
Fraser, P. E., Nguyen, J. T., Inouye, H., Surewicz, W. K., Selkoe, D. J., Podlisny, M. B., & Kirschner, D. A. (1992) · Biochemistry · doi:10.1021/bi00159a011 · Cited by 250
Inouye, H., Fraser, P., & Kirschner, D. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81393-6 · Cited by 239
Intracellular accumulation and resistance to degradation of the Alzheimer amyloid A4/beta protein.
Knauer, M. F., Soreghan, B., Burdick, D., Kosmoski, J., & Glabe, C. G. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.16.7437 · Cited by 233
Zagorski, M. G., & Barrow, C. J. (1992) · Biochemistry · doi:10.1021/bi00139a028 · Cited by 188
Turnell, W. G., & Finch, J. T. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90532-o · Cited by 181
Mathematical theory of sedimentation analysis
Holde, K. E. V. (1963) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(63)90266-2 · Cited by 156
Kinetics of aggregation of synthetic β-amyloid peptide
Tomski, S. J., & Murphy, R. M. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90735-f · Cited by 149
Gorevic, P. D., Munoz, P. C., Casey, T. T., DiRaimondo, C. R., Stone, W. J., Prelli, F. C., Rodrigues, M. M., Poulik, M. D., & Frangione, B. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.20.7908 · Cited by 149
Lansbury, P. T. (1992) · Biochemistry · doi:10.1021/bi00145a001 · Cited by 145
Cleavage at the amino and carboxyl termini of Alzheimer's amyloid-beta by cathepsin D
Ladror, U. S., Snyder, S. W., Wang, G. T., Holzman, T. F., & Krafft, G. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32325-6 · Cited by 128
Self-citationÖtvös, L., Szendrei, G. I., Lee, V. M.-Y., & Mantsch, H. H. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb19893.x · Cited by 122
Spencer, R. G. S., Halverson, K. J., Auger, M., McDermott, A. E., Griffin, R. G., & Lansbury, P. T. (1991) · Biochemistry · doi:10.1021/bi00107a004 · Cited by 96
Shen, C. L., Scott, G., Merchant, F., & Murphy, R. M. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81312-2 · Cited by 93
Solvent effects on beta protein toxicity in vivo
Waite, J., Cole, G. M., Frautschy, S. A., Connor, D. J., & Thal, L. J. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90062-3 · Cited by 82
[5] The measurement of cooperative protein self-assembly by turbidity and other techniques
Andreu, J. M., & Timasheff, S. N. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)30007-7 · Cited by 81
Luminescence-based sensors: microheterogeneous and temperature effects
Demas, J. N., & DeGraff, Β. A. (1993) · Sensors and Actuators B Chemical · doi:10.1016/0925-4005(93)85236-4 · Cited by 57
Giordano, T., Pan, J. B., Monteggia, L. M., Holzman, T. F., Snyder, S. W., Krafft, G. A., Ghanbari, H., & Kowall, N. W. (1994) · Experimental Neurology · doi:10.1006/exnr.1994.1022 · Cited by 41
Self-citationCommentary and perspective on studies of beta amyloid neurotoxicity
Yankner, B. A. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90067-8 · Cited by 39
Caputo, C. B., Fraser, P. E., Sobel, I. R. E., & Kirschner, D. A. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90068-8 · Cited by 29
A convergent synthesis of the amyloid protein of Alzheimer's disease
Hendrix, J. C., Halverson, K. J., & Lansbury, P. T. (1992) · Journal of the American Chemical Society · doi:10.1021/ja00046a060 · Cited by 20
Hendrix, J. C., & Lansbury, P. T. (1992) · The Journal of Organic Chemistry · doi:10.1021/jo00038a034 · Cited by 11
Caputo, C. B., Sobel, I. R. E., Sygowski, L. A., Lampe, R. A., & Spreen, R. C. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1518 · Cited by 6
Research works printed but not linked: 4
- Gorevic, P. D., P. C. Munoz, T. T. Casey, C. R. Diraimondo, W. J. Stone, F. C. Prelli, M K Rodrigues, K D. Poulk, and B. Franikone. 1986. Ten to fourt residue pepqides of Alzheimer's disease protein are sufficient for amyloid fibril formaton and its characteristic x-ray dffraction pattern. Proc. Natl Acad Sci USA. 83:7908-7912.
- Holzman, T. F., and S. W. Snyder. 1994. Applicatons of analytical ultra- centrugation i sucture-bsed drug design. In Modern Analytical Ul- tracentifugation: Acquisition and Interpretation of Data for Biological and Synthetic Polymer Systems. T. M. Schuster, T. M. Laue, editors. Boston, Birkhauser Division, Springer-Verlag.
- Kirschner, D. A, C. R. Abraham, and D. J. Selkoe. 1986. X-ray diffractio from intraneuronal paired helical filaments and extraneuronal amyloid fibminAlzheimer disease indicates cross-beta conformation. Proc. NatiL Acad ScL U.S.A 86:503-507.
- Krafft, G. A. 1993. Perspectives on amyloid and Alzheimer's disease: a critical review. Annu. Rep. Mled Chem 28:49-58.
Cited by
Sorted by citations
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
Self-citationAβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,156
Metadata
- Authors
- Snyder, S. W., Ladror, U. S., Wade, W. S., Wang, G. T., Barrett, L. W., Matayoshi, E. D., Huffaker, H. J., Krafft, G. A., & Holzman, T. F.
- Affiliations
- Abbott (United Kingdom) (GB)
- Corresponding author
- Holzman, T.F.
- Venue
- Biophysical Journal
- Publisher
- Elsevier BV
- Published
- 1994-09
- Volume
- 67
- Issue
- 3
- Pages
- 1216-1228
- ISSN
- 0006-3495 (ISSN-L)
- PMC
- PMC1225478
- OpenAlex
- W2024559246
- Cited by
- 381
- References
- 55
- Citations by year
- 2026: 4 · 2025: 2 · 2024: 17 · 2023: 5 · 2022: 9 · 2021: 20 · 2020: 8 · 2019: 12 · 2018: 9 · 2017: 18 · 2016: 13 · 2015: 9 · 2014: 10 · 2013: 18 · 2012: 17
- FWCI
- 7.03
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biophysical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Abbott Laboratories
- National Institutes of Health (7p01ag010481-05)
- National Institute on Aging (AG10481)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta aggregation, Alzheimer's disease, Aβ40, amyloid-beta 42, peptide length, aggregation kinetics, hydrophobic effect, seeding, aggregation inhibition, pH dependence, ionic strength, amyloid plaques
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Biophysics, Humans, Kinetics, Microscopy, Electron, Molecular Sequence Data, Polymers, Protein Conformation, Solutions, Amyloid beta-Peptides, Neurofibrillary Tangles, Macromolecular Substances, Biophysical Phenomena, In Vitro Techniques
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
