The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Evidence that β-Amyloid Protein in Alzheimer's Disease Is Not Derived by Normal Processing
Abstract
The β-amyloid protein (β/A4), derived from a larger amyloid precursor protein (APP), is the principal component of senile plaques in Alzheimer's disease. APP is an integral membrane glycoprotein and is secreted as a carboxyl-terminal truncated molecule. APP cleavage, which is a membrane-associated event, occurred at a site located within the β/A4 region. This suggests that an intact amyloidogenic β/A4 fragment is not generated during normal APP catabolism. Therefore, an early event in amyloid formation may involve altered APP processing that results in the release and subsequent deposition of intact β/A4.
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
Self-citationBlessed, G., Tomlinson, B. E., & Roth, M. (1968) · British Journal of Psychiatry · doi:10.1192/bjp.114.512.797 · Cited by 4,117
Cited by
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
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-citationCitron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757
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
Trafficking and Proteolytic Processing of APP
Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075
Self-citationReview Article: Genetics of Alzheimer Disease
Bekris, L. M., Yu, C.-E., Bird, T. D., & Tsuang, D. W. (2010) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988710383571 · Cited by 1,029
Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor
Cai, X.-D., Golde, T. E., & Younkin, S. G. (1993) · Science · doi:10.1126/science.8424174 · Cited by 913
Nitsch, R. M., Slack, B. E., Wurtman, R. J., & Growdon, J. H. (1992) · Science · doi:10.1126/science.1411529 · Cited by 898
Evidence that production and release of amyloid beta-protein involves the endocytic pathway
Koo, E. H., & Squazzo, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32449-3 · Cited by 829
Self-citationRoher, A. E., Lowenson, J. D., Clarke, S., Wolkow, C., Wang, R., Cotter, R. J., Reardon, I. M., Zürcher-Neely, H. A., Heinrikson, R. L., & Ball, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53661-9 · Cited by 799
The secretases: enzymes with therapeutic potential in Alzheimer disease
De Strooper, B., Vassar, R., & Golde, T. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2009.218 · Cited by 799
History and progress of hypotheses and clinical trials for Alzheimer’s disease
Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723
Mattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I., & Rydel, R. E. (1993) · Neuron · doi:10.1016/0896-6273(93)90315-i · Cited by 656
Haass, C., Lemere, C. A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L., & Selkoe, D. J. (1995) · Nature Medicine · doi:10.1038/nm1295-1291 · Cited by 592
Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells.
Busciglio, J., Gabuzda, D. H., Matsudaira, P., & Yankner, B. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.2092 · Cited by 569
γ-Secretase, notch, Aβ and alzheimer's disease: Where do the presenilins fit in?
Sisodia, S. S., & St George-Hyslop, P. H. (2002) · Nature Reviews Neuroscience · doi:10.1038/nrn785 · Cited by 512
Self-citationA Portrait of Alzheimer Secretases--New Features and Familiar Faces
Esler, W. P., & Wolfe, M. S. (2001) · Science · doi:10.1126/science.1064638 · Cited by 493
Interleukin‐6 and α‐2‐macroglobulin indicate an acute‐phase state in Alzheimer's disease cortices
Bauer, J., Strauss, S., Schreiter-Gasser, U., Ganter, U., Schlegel, P., Witt, I., Yolk, B., & Berger, M. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80737-n · Cited by 483
Proteases and Proteolysis in Alzheimer Disease: A Multifactorial View on the Disease Process
De Strooper, B. (2010) · Physiological Reviews · doi:10.1152/physrev.00023.2009 · Cited by 455
ALZHEIMER'S DISEASE: Genetic Studies and Transgenic Models
Price, D. L., Tanzi, R. E., Borchelt, D. R., & Sisodia, S. S. (1998) · Annual Review of Genetics · doi:10.1146/annurev.genet.32.1.461 · Cited by 406
Self-citationKounnas, M. Z., Moir, R. D., Rebeck, G. W., Bush, A. I., Argraves, W. S., Tanzi, R. E., Hyman, B. T., & Strickland, D. K. (1995) · Cell · doi:10.1016/0092-8674(95)90320-8 · Cited by 401
Sheng, J. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00069-x · Cited by 388
Gabuzda, D., Busciglio, J., Chen, L. B., Matsudaira, P., & Yankner, B. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36875-8 · Cited by 373
Effects of PS1 Deficiency on Membrane Protein Trafficking in Neurons
Naruse, S., Thinakaran, G., Luo, J.-J., Kusiak, J. W., Tomita, T., Iwatsubo, T., Qian, X., Ginty, D. D., Price, D. L., Borchelt, D. R., et al. (1998) · Neuron · doi:10.1016/s0896-6273(00)80637-6 · Cited by 355
Self-citationBackstrom, J. R., Lim, G. P., Cullen, M. J., & Tökés, Z. A. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-24-07910.1996 · Cited by 331
Metabolism of the “Swedish” Amyloid Precursor Protein Variant in Neuro2a (N2a) Cells
Thinakaran, G., Teplow, D. B., Siman, R., Greenberg, B., & Sisodia, S. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9390 · Cited by 317
Self-citationIntroduction and expression of the 400 kilobase precursor amyloid protein gene in transgenic mice
Lamb, B. T., Sisodia, S. S., Lawler, A. M., Slunt, H. H., Kitt, C. A., Kearns, W. G., Pearson, P. L., Price, D. L., & Gearhart, J. D. (1993) · Nature Genetics · doi:10.1038/ng0993-22 · Cited by 311
Self-citationGhiso, J., Matsubara, E., Koudinov, A., Choi-Miura, N. H., Tomita, M., Wisniewski, T., & Frangione, B. (1993) · Biochemical Journal · doi:10.1042/bj2930027 · Cited by 304
Benjannet, S., Elagoz, A., Wickham, L., Mamarbachi, M., Munzer, J. S., Basak, A., Lazure, C., Cromlish, J. A., Sisodia, S., Checler, F., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009899200 · Cited by 301
Self-citationISHIZUKA, K., KIMURA, T., IGATA‐YI, R., KATSURAGI, S., TAKAMATSU, J., & MIYAKAWA, T. (1997) · Psychiatry and Clinical Neurosciences · doi:10.1111/j.1440-1819.1997.tb02375.x · Cited by 245
Nitsch, R. M., Farber, S. A., Growdon, J. H., & Wurtman, R. J. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.11.5191 · Cited by 244
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
Gowing, E., Roher, A. E., Woods, A. S., Cotter, R. J., Chaney, M., Little, S. P., & Ball, M. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78080-6 · Cited by 223
Beyreuther, K., & Masters, C. L. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00667.x · Cited by 221
Self-citationSerotonin 5-HT2a and 5-HT2c Receptors Stimulate Amyloid Precursor Protein Ectodomain Secretion
Nitsch, R. M., Deng, M., Growdon, J. H., & Wurtman, R. J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.8.4188 · Cited by 219
The Role of APP Processing and Trafficking Pathways in the Formation of Amyloid β‐Proteina
SELKOE, D. J., YAMAZAKI, T., CITRON, M., PODLISNY, M. B., KOO, E. H., TEPLOW, D. B., & HAASS, C. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34401.x · Cited by 205
Self-citationRole of microglia in senile plaque formation
Mackenzie, I. R. A., Hao, C., & Munoz, D. G. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00092-s · Cited by 183
(1994) · PubMed Central · Cited by 169
Senile plaques in temporal lobe epilepsy
Mackenzie, I. R. A., & Miller, L. A. (1994) · Acta Neuropathologica · doi:10.1007/bf00294177 · Cited by 168
MATTSON, M. P. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb44401.x · Cited by 166
Kumar-Singh, S. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.18.2589 · Cited by 158
Modulation of Statin-Activated Shedding of Alzheimer APP Ectodomain by ROCK
Pedrini, S., Carter, T. L., Prendergast, G., Petanceska, S., Ehrlich, M. E., & Gandy, S. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020018 · Cited by 154
Furin mediates enhanced production of fibrillogenic ABri peptides in familial British dementia
Kim, S.-H., Wang, R., Gordon, D. J., Bass, J., Steiner, D. F., Lynn, D. G., Thinakaran, G., Meredith, S. C., & Sisodia, S. S. (1999) · Nature Neuroscience · doi:10.1038/14783 · Cited by 154
Self-citationβ‐Amyloid Precursor Protein Isoforms in Various Rat Brain Regions and During Brain Development
Löffler, J., & Huber, G. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb08443.x · Cited by 150
Endo‐lysosomal and autophagic dysfunction: a driving factor in Alzheimer's disease?
Whyte, L. S., Lau, A. A., Hemsley, K. M., Hopwood, J. J., & Sargeant, T. J. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13935 · Cited by 150
Mills, J., Laurent Charest, D., Lam, F., Beyreuther, K., Ida, N., Pelech, S. L., & Reiner, P. B. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-24-09415.1997 · Cited by 134
Self-citationBiology of Aβ Amyloid in Alzheimer's Disease
Wisniewski, T., Ghiso, J., & Frangione, B. (1997) · Neurobiology of Disease · doi:10.1006/nbdi.1997.0147 · Cited by 134
Blood-brain barrier leakage in Alzheimer’s disease: From discovery to clinical relevance
Nehra, G., Bauer, B., & Hartz, A. M. S. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108119 · Cited by 127
Disease modifying therapy for AD?1
Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117
Nitsch, R. M., Rebeck, G. W., Deng, M., Richardson, U. I., Tennis, M., Schenk, D. B., Vigo‐Pelfrey, C., Lieberburg, I., Wurtman, R. J., Hyman, B. T., et al. (1995) · Annals of Neurology · doi:10.1002/ana.410370414 · Cited by 113
Tamboli, I. Y., Prager, K., Barth, E., Heneka, M., Sandhoff, K., & Walter, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414525200 · Cited by 110
Kinoshita, A., Whelan, C. M., Berezovska, O., & Hyman, B. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203372200 · Cited by 109
(1994) · PubMed Central · Cited by 105
Anti-Amyloid Therapies for Alzheimer’s Disease and the Amyloid Cascade Hypothesis
Fedele, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914499 · Cited by 102
Aged Non‐Human Primates: An Animal Model of Age‐Associated Neurodegenerative Disease
Price, D. L., Martin, L. J., Sisodia, S. S., Wagster, M. V., Koo, E. H., Walker, L. C., Koliatsos, V. E., & Cork, L. C. (1991) · Brain Pathology · doi:10.1111/j.1750-3639.1991.tb00672.x · Cited by 100
Self-citationMURAKAMI, N., YAMAKI, T., IWAMOTO, Y., SAKAKIBARA, T., KOBORI, N., FUSHIKI, S., & UEDA, S. (1998) · Journal of Neurotrauma · doi:10.1089/neu.1998.15.993 · Cited by 100
A non‐amyloidogenic function of BACE‐2 in the secretory pathway
Fluhrer, R., Capell, A., Westmeyer, G., Willem, M., Hartung, B., Condron, M. M., Teplow, D. B., Haass, C., & Walter, J. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00908.x · Cited by 95
Ciallella, J. R., Ikonomovic, M. D., Paljug, W. R., Wilbur, Y. I., Dixon, C. E., Kochanek, P. M., Marion, D. W., & DeKosky, S. T. (2002) · Journal of Neurotrauma · doi:10.1089/089771502762300229 · Cited by 94
Axonal transport of APP and the spatial regulation of APP cleavage and function in neuronal cells
Brunholz, S., Sisodia, S., Lorenzo, A., Deyts, C., Kins, S., & Morfini, G. (2012) · Experimental Brain Research · doi:10.1007/s00221-011-2870-1 · Cited by 92
Self-citationCathepsin D is involved in the clearance of Alzheimer's β‐amyloid protein
Hamazaki, H. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)01087-3 · Cited by 92
Felsenstein, K. M., Hunihan, L. W., & Roberts, S. B. (1994) · Nature Genetics · doi:10.1038/ng0394-251 · Cited by 90
Schönherr, C., Bien, J., Isbert, S., Wichert, R., Prox, J., Altmeppen, H., Kumar, S., Walter, J., Lichtenthaler, S. F., Weggen, S., et al. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0084-5 · Cited by 76
Kajkowski, E. M., Lo, C. F., Ning, X., Walker, S., Sofia, H. J., Wang, W., Edris, W., Chanda, P., Wagner, E., Vile, S., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m011161200 · Cited by 63
Campos-Peña, V., Toral-Rios, D., Becerril-Pérez, F., Sánchez-Torres, C., Delgado-Namorado, Y., Torres-Ossorio, E., Franco-Bocanegra, D., & Carvajal, K. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6768 · Cited by 58
Eckols, K., Bymaster, F. P., Mitch, C. H., Shannon, H. E., Ward, J. S., & DeLapp, N. W. (1995) · Life Sciences · doi:10.1016/0024-3205(95)02064-p · Cited by 53
Neuroimmunology of Alzheimer's disease: A conference report
Dickson, D. W., & Rogers, J. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90104-6 · Cited by 44
Imipramine and citalopram facilitate amyloid precursor protein secretion in vitro
PAKASKI, M., BJELIK, A., HUGYECZ, M., KASA, P., JANKA, Z., & KALMAN, J. (2005) · Neurochemistry International · doi:10.1016/j.neuint.2005.03.004 · Cited by 43
Savage, M. J., Iqbal, M., Loh, T., Trusko, S. P., Scott, R., & Siman, R. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90490-1 · Cited by 42
Chambers, J. K., Kuribayashi, H., Ikeda, S.-I., & Une, Y. (2010) · Amyloid · doi:10.3109/13506129.2010.483119 · Cited by 32
Papadopoulos, N., Suelves, N., Perrin, F., Vadukul, D. M., Vrancx, C., Constantinescu, S. N., & Kienlen-Campard, P. (2022) · Biomedicines · doi:10.3390/biomedicines10112753 · Cited by 20
KAPLITT, M., GOURAS, G. K., MAKIMURA, H., JOVANOVIC, J., SWEENEY, D., GREENGARD, P., RELKIN, N. R., & GANDY, S. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb32597.x · Cited by 12
Amyloidogenesis in familial British dementia is associated with a genetic defect on chromosome 13
GHISO, J., VIDAL, R., ROSTAGNO, A., MIRAVALLE, L., HOLTON, J. L., MEAD, S., RÉVÉSZ, T., PLANT, G., & FRANGIONE, B. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb06908.x · Cited by 12
Metadata
- Authors
- Sisodia, S. S., Koo, E. H., Beyreuther, K., Unterbeck, A., & Price, D. L.
- Venue
- Science
- Published
- 1990-04-27
- Volume
- 248
- Issue
- 4954
- Pages
- 492-495
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2071691905
- Cited by
- 893
- References
- 2
- FWCI
- 62.36
- 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.