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.
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
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 increased amyloid beta 42:40 ratio in oligodendrocytes could contribute to the high proportion of soluble aggregates.
“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]
The discussion section (page not provided) speculates that the Aβ42:Aβ40 ratio affects how much amyloid accumulates, and the abstract identifies soluble aggregates among the species formed in solution. The paper does not study oligodendrocytes or show that a higher ratio increases the proportion of aggregates that are soluble. (LLM, conf=0.84)
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.
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 · see citing works
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 · see citing works
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178 · see citing works
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022 · see citing works
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 · see citing works
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 · see citing works
Amyloid Deposits and Amyloidosis
Glenner, G. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198006053022305 · Cited by 1,794 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,333 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 829 · see citing works
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 636 · see citing works
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 · see citing works
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 · see citing works
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 525 · see citing works
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 522 · see citing works
Kirschner, D. A., Abraham, C., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.83.2.503 · Cited by 517 · see citing works
Stafford, W. F. (1992) · Analytical Biochemistry · doi:10.1016/0003-2697(92)90316-y · Cited by 517 · see citing works
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 · see citing works
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 422 · see citing works
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 376 · see citing works
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 · see citing works
Mathematical theory of sedimentation analysis
(1962) · Journal of the Franklin Institute · doi:10.1016/0016-0032(62)90836-0 · Cited by 332 · see citing works
Jarrett, J. T., & Lansbury, P. T. (1992) · Biochemistry · doi:10.1021/bi00164a008 · Cited by 325 · see citing works
Halverson, K. J., Fraser, P. E., Kirschner, D. A., & Lansbury, P. T. (1990) · Biochemistry · doi:10.1021/bi00463a003 · Cited by 292 · see citing works
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 248 · see citing works
Inouye, H., Fraser, P., & Kirschner, D. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81393-6 · Cited by 239 · see citing works
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 · see citing works
Zagorski, M. G., & Barrow, C. J. (1992) · Biochemistry · doi:10.1021/bi00139a028 · Cited by 188 · see citing works
Turnell, W. G., & Finch, J. T. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90532-o · Cited by 181 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Lansbury, P. T. (1992) · Biochemistry · doi:10.1021/bi00145a001 · Cited by 145 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Shen, C. L., Scott, G., Merchant, F., & Murphy, R. M. (1993) · Biophysical Journal · doi:10.1016/s0006-3495(93)81312-2 · Cited by 93 · see citing works
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 84 · see citing works
[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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Hendrix, J. C., & Lansbury, P. T. (1992) · The Journal of Organic Chemistry · doi:10.1021/jo00038a034 · Cited by 11 · see citing works
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 · see citing works
Flagged first, then by citations
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
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 · see citing works
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 · see citing works
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 · see citing works
Harper, J. D., & Lansbury, P. T. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.385 · Cited by 1,652 · see citing works
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 1,139 · see citing works
Amyloid 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 · see citing works
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015 · see citing works
Self-citationThe alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
Kelly, J. W. (1998) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(98)80016-x · Cited by 998 · see citing works
Alzheimer's amyloid fibrils: structure and assembly.
Serpell, L. (2000) · Biochimica et Biophysica Acta · doi:10.1016/s0925-4439(00)00029-6 · Cited by 922 · see citing works
Lomakin, A., Chung, D. S., Benedek, G. B., Kirschner, D. A., & Teplow, D. B. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1125 · Cited by 784 · see citing works
Turner, P. R., O’Connor, K., Tate, W. P., & Abraham, W. C. (2003) · Progress in Neurobiology · doi:10.1016/s0301-0082(03)00089-3 · Cited by 751 · see citing works
Review: Alzheimer's Amyloid β-Peptide-Associated Free Radical Oxidative Stress and Neurotoxicity
Varadarajan, S., Yatin, S., Aksenova, M., & Butterfield, D. A. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4274 · Cited by 735 · see citing works
Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90255-6 · Cited by 691 · see citing works
Hardeland, R. (2005) · Endocrine · doi:10.1385/endo:27:2:119 · Cited by 670 · see citing works
Paresce, D. M., Ghosh, R. N., & Maxfield, F. R. (1996) · Neuron · doi:10.1016/s0896-6273(00)80187-7 · Cited by 663 · see citing works
Amyloid oligomers: formation and toxicity of Aβ oligomers
Sakono, M., & Zako, T. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07568.x · Cited by 602 · see citing works
Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N., Côté, S., Simone, A. D., Doig, A. J., Faller, P., Garcı́a, A. E., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 583 · see citing works
Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers‐Nolten, I., Van Der Werf, K., Subramaniam, V., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.211 · Cited by 532 · see citing works
Hou, L., Shao, H., Zhang, Y., Li, H. L., Menon, N. K., Neuhaus, E. B., Brewer, J. M., Byeon, I. L., Ray, D. G., Vitek, M. P., et al. (2004) · Journal of the American Chemical Society · doi:10.1021/ja036813f · Cited by 525 · see citing works
Klein, W. L., Stine, W. B., & Teplow, D. B. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.010 · Cited by 487 · see citing works
Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1999) · Biochemistry · doi:10.1021/bi9904149 · Cited by 454 · see citing works
The toxicity in vitro of β-amyloid protein
Iversen, L. L., Mortishire‐Smith, R. J., Pollack, S. J., & Shearman, M. S. (1995) · Biochemical Journal · doi:10.1042/bj3110001 · Cited by 425 · see citing works
Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V., & Lee, J.-M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911281106 · Cited by 426 · see citing works
Cheng, I. H.-J., Scearce-Levie, K. A., Legleiter, J. A., Palop, J. J., Gerstein, H., Bien‐Ly, N., Puolivaöli, J., Lesné, S., Ashe, K. H., Muchowski, P. J., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701078200 · Cited by 403 · see citing works
Inhibition of amyloid-β aggregation and caspase-3 activation by the Ginkgo biloba extract EGb761
Luo, Y., Smith, J. V., Paramasivam, V., Burdick, A. J., Curry, K. J., Buford, J. P., Khan, I. A., Netzer, W. J., Xu, H., & Butko, P. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182425199 · Cited by 399 · see citing works
Chapter 7 Protein Oxidation Processes in Aging Brain
Butterfield, D. A., & Stadtman, E. R. (1997) · Advances in cell aging and gerontology · doi:10.1016/s1566-3124(08)60057-7 · Cited by 390 · see citing works
Drake, J. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00225-7 · Cited by 371 · see citing works
Aβ40 Inhibits Amyloid Deposition<i>In Vivo</i>
Kim, J., Onstead, L., Randle, S., Price, R., Smithson, L., Zwizinski, C., Dickson, D. W., Golde, T., & McGowan, E. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4849-06.2007 · Cited by 359 · see citing works
“There are several in vitro studies demonstrating that A 40 directly interferes with A 42 aggregation by delaying the A 42- mediated nucleation step at an early stage in the fibrillogenesis process (Snyder et al., 1994; Hasegawa et al., 1999; Zou et al., 2003).”
BackgroundOxidative stress in Alzheimer's disease
Chauhan, V. P. S., & Chauhan, A. (2006) · Pathophysiology · doi:10.1016/j.pathophys.2006.05.004 · Cited by 341 · see citing works
Inhibition of Alzheimer β-Fibrillogenesis by Melatonin
Pappolla, M. A., Bozner, P., Soto, C. A., Shao, H., Robakis, N. K., Zagorski, M. G., Frangione, B., & Ghiso, J. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.13.7185 · Cited by 338 · see citing works
On the nucleation of amyloid β‐protein monomer folding
Lazo, N. D., Grant, M. A., Condron, M. M., Rigby, A. C., & Teplow, D. B. (2005) · Protein Science · doi:10.1110/ps.041292205 · Cited by 330 · see citing works
Alzheimer's Aβ42 and Aβ40 peptides form interlaced amyloid fibrils
Gu, L., & Guo, Z. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12202 · Cited by 325 · see citing works
Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide.
Solomon, B., Koppel, R., Hanan, E., & Katzav-Gozansky, T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.452 · Cited by 314 · see citing works
Hu, J., Akama, K. T., Krafft, G. A., Chromy, B. A., & Eldik, L. J. V. (1998) · Brain Research · doi:10.1016/s0006-8993(97)01318-8 · Cited by 313 · see citing works
Self-citationButyrylcholinesterase in the life cycle of amyloid plaques
Guillozet-Bongaarts, A. L., Mesulam, M. M., Smiley, J. F., & Mash, D. C. (1997) · Annals of Neurology · doi:10.1002/ana.410420613 · Cited by 312 · see citing works
Standardization of measurement of β-amyloid<sub>(1-42)</sub>in cerebrospinal fluid and plasma
Vanderstichele, H., Kerschaver, E. V., Hesse, C., Davidsson, P., Buyse, M.-A., Andreasen, N., Minthon, L., Wallin, A., Blennow, K., & Vanmechelen, E. (2000) · Amyloid · doi:10.3109/13506120009146438 · Cited by 301 · see citing works
Genetics and molecular pathogenesis of sporadic and hereditary cerebral amyloid angiopathies
Révész, T., Holton, J. L., Lashley, T., Plant, G. T., Frangione, B., Rostagno, A. A., & Ghiso, J. A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0501-8 · Cited by 293 · see citing works
Lashuel, H. A., LaBrenz, S. R., Woo, L., Serpell, L. C., & Kelly, J. W. (2000) · Journal of the American Chemical Society · doi:10.1021/ja9937831 · Cited by 285 · see citing works
Allaman, I., Gavillet, M., Bélanger, M., Laroche, T., Viertl, D., Lashuel, H. A., & Magistretti, P. J. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5098-09.2010 · Cited by 277 · see citing works
Solvent effects on self-assembly of beta-amyloid peptide
Shen, C. L., & Murphy, R. M. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)79940-4 · Cited by 277 · see citing works
Prion Domain Initiation of Amyloid Formation in Vitro from Native Ure2p
Taylor, K. L., Cheng, N., Williams, R. W., Steven, A. C., & Wickner, R. B. (1999) · Science · doi:10.1126/science.283.5406.1339 · Cited by 277 · see citing works
Slow Degradation of Aggregates of the Alzheimer's Disease Amyloid β-Protein by Microglial Cells
Paresce, D. M., Chung, H., & Maxfield, F. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.29390 · Cited by 269 · see citing works
Fezoui, Y., Hartley, D. M., Harper, J. D., Khurana, R., Walsh, D. M., Condron, M. M., Selkoe, D. J., Lansbury, P. T., Fink, A. L., & Teplow, D. B. (2000) · Amyloid · doi:10.3109/13506120009146831 · Cited by 260 · see citing works
Jan, A., Hartley, D. M., & Lashuel, H. A. (2010) · Nature Protocols · doi:10.1038/nprot.2010.72 · Cited by 257 · see citing works
Structural Basis for Increased Toxicity of Pathological Aβ42:Aβ40 Ratios in Alzheimer Disease
Pauwels, K., Williams, T. L., Morris, K. L., Jonckheere, W., Vandersteen, A., Kelly, G., Schymkowitz, J., Rousseau, F., Pastore, A., Serpell, L. C., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.264473 · Cited by 253 · see citing works
Hirota, N., Mizuno, K., & Goto, Y. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1468 · Cited by 251 · see citing works
Pappolla, M. A., Chyan, Y., Pöeggeler, B., Frangione, B., Wilson, G. L., Ghiso, J. A., & Reiter, R. J. (2000) · Journal of Neural Transmission · doi:10.1007/s007020050018 · Cited by 239 · see citing works
Cooperative α‐helix formation of β‐lactoglobulin and melittin induced by hexafluoroisopropanol
Hirota, N., Goto, Y., & Mizuno, K. (1997) · Protein Science · doi:10.1002/pro.5560060218 · Cited by 241 · see citing works
Lashuel, H. A., Hartley, D. M., Petre, B. M., Wall, J. S., Simon, M. N., Walz, T., & Lansbury, P. T. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00927-6 · Cited by 237 · see citing works
Kremer, J. J., Pallitto, M. M., Sklansky, D. J., & Murphy, R. M. (2000) · Biochemistry · doi:10.1021/bi0001980 · Cited by 237 · see citing works
Peptide Aggregation in Neurodegenerative Disease
Murphy, R. M. (2002) · Annual Review of Biomedical Engineering · doi:10.1146/annurev.bioeng.4.092801.094202 · Cited by 227 · see citing works
Stéphan, A., Laroche, S., & Davis, S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-15-05703.2001 · Cited by 225 · see citing works
Modified-Peptide Inhibitors of Amyloid β-Peptide Polymerization
Findeis, M. A., Musso, G. M., Arico-Muendel, C. C., Benjamin, H. W., Hundal, A. M., Lee, J.-J., Chin, J., Kelley, M., WAKEFIELD, J. D., Hayward, N. J., et al. (1999) · Biochemistry · doi:10.1021/bi982824n · Cited by 221 · see citing works
Toxicity of Amyloid β Peptide: Tales of Calcium, Mitochondria, and Oxidative Stress
Canevari, L., Abramov, A. Y., & Duchen, M. R. (2004) · Neurochemical Research · doi:10.1023/b:nere.0000014834.06405.af · Cited by 221 · see citing works
Nicotine Inhibits Amyloid Formation by the β-Peptide
Salomon, A. R., Marcinowski, K. J., Friedland, R. P., & Zagorski, M. G. (1996) · Biochemistry · doi:10.1021/bi9617264 · Cited by 220 · see citing works
Hou, L., Kang, I., Marchant, R. E., & Zagorski, M. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200338200 · Cited by 218 · see citing works
Interactions of Amyloid β-Peptide (1−40) with Ganglioside-Containing Membranes
Matsuzaki, K., & Horikiri, C. (1999) · Biochemistry · doi:10.1021/bi982345o · Cited by 217 · see citing works
Physicochemical interactions of amyloid β-peptide with lipid bilayers
Matsuzaki, K. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.009 · Cited by 215 · see citing works
Structural studies of soluble oligomers of the alzheimer β-amyloid peptide
Huang, T. H. J., Dun-Sheng, Y., Plaskos, N. P., Go, S., Yip, C. M., Fraser, P. E., & Chakrabartty, A. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3559 · Cited by 211 · see citing works
Sousa, M. M., Du Yan, S., Fernandes, R., Guimarães, A., Stern, D., & Saraiva, M. J. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07576.2001 · Cited by 212 · see citing works
Lashuel, H. A., Lai, Z., & Kelly, J. W. (1998) · Biochemistry · doi:10.1021/bi981876+ · Cited by 206 · see citing works
Transthyretin Quaternary and Tertiary Structural Changes Facilitate Misassembly into Amyloid
Kelly, J. W., Colón, W., LAI, Z., Lashuel, H. A., MCCULLOCH, J., McCutchen, S. L., Miroy, G. J., & PETERSON, S. (1997) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60321-6 · Cited by 205 · see citing works
Kelly, J. W. (1997) · Structure · doi:10.1016/s0969-2126(97)00215-3 · Cited by 205 · see citing works
Soluble Amyloid Aβ-(1–40) Exists as a Stable Dimer at Low Concentrations
Garzon-Rodriguez, W., Sepulveda-Becerra, M., Milton, S. C. F., & Glabe, C. G. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.34.21037 · Cited by 204 · see citing works
Oligomerization and Toxicity of β-Amyloid-42 Implicated in Alzheimer's Disease
El‐Agnaf, O. M. A., Mahil, D. S., PATEL, B. P., & Austen, B. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3051 · Cited by 196 · see citing works
Characterization of Apolipoprotein J-Alzheimer's Aβ Interaction
Matsubara, E., Frangione, B., & Ghiso, J. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7563 · Cited by 195 · see citing works
Apolipoprotein J and Alzheimer's amyloid β solubility
Matsubara, E., Soto, C. A., Governale, S., Frangione, B., & Ghiso, J. A. (1996) · Biochemical Journal · doi:10.1042/bj3160671 · Cited by 187 · see citing works
Yu, S. P., Farhangrazi, Z. S., Ying, H. S.-C., Yeh, C.-H., & Choi, D. W. (1998) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0186 · Cited by 189 · see citing works
Amyloid Fibril Formation by Lens Crystallin Proteins and Its Implications for Cataract Formation*
Meehan, S., Berry, Y. J., Luisi, B., Dobson, C., Carver, J., & MacPhee, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308203200 · Cited by 195 · see citing works
Podlisny, M. B., Walsh, D. M., Amarante, P., Ostaszewski, B. L., Stimson, E. R., Maggio, J. E., Teplow, D. B., & Selkoe, D. J. (1998) · Biochemistry · doi:10.1021/bi972029u · Cited by 181 · see citing works
[13] Methodological and chemical factors affecting amyloid β peptide amyloidogenicity
Zagorski, M. G., Yang, J., Shao, H., Ma, K., Zeng, H., & Hong, A. (1999) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(99)09015-1 · Cited by 185 · see citing works
Lashuel, H. A., Wurth, C., Woo, L., & Kelly, J. W. (1999) · Biochemistry · doi:10.1021/bi991021c · Cited by 177 · see citing works
Kapurniotu, A., Schmauder, A., & Tenidis, K. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5244 · Cited by 173 · see citing works
Lashley, T., Holton, J. L., Gray, E., Kirkham, K., O’Sullivan, S. S., Hilbig, A., Wood, N. W., Lees, A. J., & Révész, T. (2008) · Acta Neuropathologica · doi:10.1007/s00401-007-0336-0 · Cited by 172 · see citing works
Tamaoka, A., Odaka, A., Ishibashi, Y., Usami, M., Sahara, N., Suzuki, N., Nukina, N., Mizusawa, H., Shoji, S., & Kanazawa, I. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)30050-8 · Cited by 165 · see citing works
Amyloid β-peptide polymerization studied using fluorescence correlation spectroscopy
Tjernberg, L. O., Pramanik, A., Björling, S. C., Thyberg, P., Thyberg, J., Nordstedt, C., Berndt, K. D., Terenius, L. Y., & Rigler, R. W. (1999) · Chemistry & Biology · doi:10.1016/s1074-5521(99)80020-9 · Cited by 159 · see citing works
A Molecular Switch in Amyloid Assembly: Met35and Amyloid β-Protein Oligomerization
Bitan, G., Tarus, B., Vollers, S. S., Lashuel, H. A., Condron, M. M., Straub, J. E., & Teplow, D. B. (2003) · Journal of the American Chemical Society · doi:10.1021/ja0349296 · Cited by 158 · see citing works
The nanometer-scale structure of amyloid-Β visualized by atomic force microscopy
Stine, W. B., Snyder, S. W., Ladror, U. S., Wade, W. S., MILLER, M. F., Perun, T. J., Holzman, T. F., & Krafft, G. A. (1996) · Journal of Protein Chemistry · doi:10.1007/bf01887400 · Cited by 159 · see citing works
Self-citationCukalevski, R., Yang, X., Meisl, G., Weininger, U., Bernfur, K., Frohm, B., Knowles, T. P. J., & Linse, S. S. (2015) · Chemical Science · doi:10.1039/c4sc02517b · Cited by 155 · see citing works
Lashuel, H., Hartley, D., Balakhaneh, D., Aggarwal, A., Teichberg, S., & Callaway, D. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206593200 · Cited by 141 · see citing works
Watson, A. A., Fairlie, D. P., & Craik, D. J. (1998) · Biochemistry · doi:10.1021/bi9810757 · Cited by 142 · see citing works
Economou, N. J., Giammona, M. J., Do, T. D., Zheng, X., Teplow, D. B., Buratto, S. K., & Bowers, M. T. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.5b11913 · Cited by 142 · see citing works
Gursky, O., & Aleshkov, S. B. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00228-9 · Cited by 140 · see citing works
Man, B. Y.-W., Chan, H., Leung, C., Chan, D. S., Bai, L., Jiang, Z., Li, H., & Ma, D. (2011) · Chemical Science · doi:10.1039/c0sc00636j · Cited by 136 · see citing works
Oxidation of Methionine 35 Attenuates Formation of Amyloid β-Peptide 1–40 Oligomers
Palmblad, M., Westlind‐Danielsson, A., & Bergquist, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112218200 · Cited by 129 · see citing works
Decreased pH in the aging brain and Alzheimer's disease
Decker, Y., Németh, E., Schomburg, R., Chemla, A., Fülöp, L., Menger, M. D., Liu, Y., & Fassbender, K. C. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.12.007 · Cited by 127 · see citing works
Reynolds, R., & Hardy, R. (1997) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19970301)47:5 · Cited by 258 · see citing works
The amyloid cascade and Alzheimer's disease therapeutics: theory versus observation
Castellani, R. J., Plascencia‐Villa, G., & Perry, G. L. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0231-z · Cited by 124 · see citing works
Srivareerat, M., Tran, T. T., Alzoubi, K. H., & Alkadhi, K. A. (2008) · Biological Psychiatry · doi:10.1016/j.biopsych.2008.08.021 · Cited by 122 · see citing works
The case for soluble Aβ oligomers as a drug target in Alzheimer's disease
Hefti, F. F., Goure, W. F., Jerecı̀ć, J., Iverson, K. S., Walicke, P. A., & Krafft, G. A. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.03.002 · Cited by 119 · see citing works
Self-citationPierrot, N., Santos, S. F., Feyt, C., Morel, M., Brion, J., & Octave, J. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606015200 · Cited by 118 · see citing works
Sayre, L. M., Zagorski, M. G., Surewicz, W. K., Krafft, G. A., & Perry, G. L. (1997) · Chemical Research in Toxicology · doi:10.1021/tx970009n · Cited by 119 · see citing works
Self-citationInfluence of Hydrophobic Teflon Particles on the Structure of Amyloid β-Peptide
Giacomelli, C. E., & Norde, W. (2003) · Biomacromolecules · doi:10.1021/bm034151g · Cited by 113 · see citing works
Yun, S., Urbanc, B., Cruz, L., Bitan, G., Teplow, D. B., & Stanley, E. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.097766 · Cited by 111 · see citing works
Felice, F. G. D., Houzel, J., Garcia-Abreu, J., Louzada, P. R., Afonso, R. C. D. H., Meirelles, M. N. L., Lent, R., Neto, V. M., & Ferreira, S. T. (2001) · The FASEB Journal · doi:10.1096/fj.00-0676fje · Cited by 113 · see citing works
Johansson, A., Berglind‐Dehlin, F., Karlsson, G., Edwards, K., Gellerfors, P., & Lannfelt, L. (2006) · FEBS Journal · doi:10.1111/j.1742-4658.2006.05263.x · Cited by 111 · see citing works
Cenini, G., Rüb, C., Bruderek, M., & Voos, W. (2016) · Molecular Biology of the Cell · doi:10.1091/mbc.e16-05-0313 · Cited by 110 · see citing works
Probing the Kinetics of β-Amyloid Self-Association
Murphy, R. M., & Pallitto, M. M. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4253 · Cited by 109 · see citing works
Jarvet, J., Damberg, P., Bodell, K., Eriksson, L. E. G., & Gräslund, A. (2000) · Journal of the American Chemical Society · doi:10.1021/ja991167z · Cited by 109 · see citing works
Trifluoroacetic acid pretreatment reproducibly disaggregates the amyloid β-peptide
Jao, S., Ma, K., Talafous, J., Orlando, R., & Zagorski, M. G. (1997) · Amyloid · doi:10.3109/13506129709003835 · Cited by 107 · see citing works
- 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
- Health Sciences › Medicine › Physiology › 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