Cited by 290Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 35 of the 36 references it cites were found in a registry or an index.

Detection of a Novel Intraneuronal Pool of Insoluble Amyloid β Protein that Accumulates with Time in Culture

Open access

Skovronsky, Daniel M., Doms, Robert W., Lee, Virginia M.-Y.·1998·The Journal of Cell Biology

DOI 10.1083/jcb.141.4.1031PMC PMC2132781

Open this paper in CoChat — free account

Abstract

The amyloid-β peptide (Aβ) is produced at several sites within cultured human NT2N neurons with Aβ1-42 specifically generated in the endoplasmic reticulum/intermediate compartment. Since Aβ is found as insoluble deposits in senile plaques of the AD brain, and the Aβ peptide can polymerize into insoluble fibrils in vitro, we examined the possibility that Aβ1-40, and particularly the more highly amyloidogenic Aβ1-42, accumulate in an insoluble pool within NT2N neurons. Remarkably, we found that formic acid extraction of the NT2N cells solubilized a pool of previously undetectable Aβ that accounted for over half of the total intracellular Aβ. Aβ1-42 was more abundant than Aβ1-40 in this pool, and most of the insoluble Aβ1-42 was generated in the endoplasmic reticulum/intermediate compartment pathway. High levels of insoluble Aβ were also detected in several nonneuronal cell lines engineered to overexpress the amyloid-β precursor protein. This insoluble intracellular pool of Aβ was exceptionally stable, and accumulated in NT2N neurons in a time-dependent manner, increasing 12-fold over a 7-wk period in culture. These novel findings suggest that Aβ amyloidogenesis may be initiated within living neurons rather than in the extracellular space. Thus, the data presented here require a reexamination of the prevailing view about the pathogenesis of Aβ deposition in the AD brain.

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

Crossref · 10.1083/jcb.141.4.1031

Cites

35 of 35 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Candidate gene for the chromosome 1 familial Alzheimer’s disease locus
Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178
The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
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
Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)
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
Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production
Citron, 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

Flagged first, then by citations

Show all 36 references

1 of the 36 references couldn’t be matched to a known paper.

Research works printed but not linked: 1

Kim, 1988, Production and characterization of monoclonal antibodies reactive to synthetic cerebrovascular amyloid peptide, Neurosci Res Commun, 2, 121

Sorted by citations

Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345
Intracellular amyloid-β in Alzheimer's disease
LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942
Untitled work
(1999) · doi:10.1002/1531-8249(199912)46:6
Translating cell biology into therapeutic advances in Alzheimer's disease
Selkoe, D. J. (1999) · Nature · doi:10.1038/399a023 · Cited by 1,166
Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease
Walsh, D. M., & Selkoe, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.010 · Cited by 1,207
Identification of a Novel Aspartic Protease (Asp 2) as β-Secretase
Hussain, I., Powell, D., Howlett, D. R., Tew, D. G., Meek, T. D., Chapman, C., Gloger, I. S., Murphy, K. E., Southan, C. D., Ryan, D. M., et al. (1999) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0811 · Cited by 1,080
Intraneuronal Aβ42 Accumulation in Human Brain
Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991
Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
Kayed, R., Head, E., Sarsoza, F., Saing, T., Cotman, C. W., Necula, M., Margol, L., Wu, J., Breydo, L., Thompson, J. L., et al. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-18 · Cited by 773
Intraneuronal Alzheimer Aβ42 Accumulates in Multivesicular Bodies and Is Associated with Synaptic Pathology
Takahashi, R. H., Milner, T. A., Li, F., Nam, E. E., Edgar, M. A., Yamaguchi, H., Beal, M. F., Xu, H., Greengard, P., & Gouras, G. K. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64463-x · Cited by 706
Toward a Comprehensive Theory for Alzheimer's Disease. Hypothesis: Alzheimer's Disease Is Caused by the Cerebral Accumulation and Cytotoxicity of Amyloid β‐Protein
Selkoe, D. J. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05554.x · Cited by 627
Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP
Kamal, A., Almenar-Queralt, A., LeBlanc, J. F., Roberts, E. A., & Goldstein, L. S. B. (2001) · Nature · doi:10.1038/414643a · Cited by 583
The Levels of Soluble versus Insoluble Brain Aβ Distinguish Alzheimer's Disease from Normal and Pathologic Aging
Wang, J., Dickson, D. W., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7085 · Cited by 567
Self-citation
The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain
Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000) · Biochemistry · doi:10.1021/bi001048s · Cited by 401
Stimulation of β-Amyloid Precursor Protein Trafficking by Insulin Reduces Intraneuronal β-Amyloid and Requires Mitogen-Activated Protein Kinase Signaling
Gasparini, L., Gouras, G. K., Wang, R., Gross, R. S., Beal, M. F., Greengard, P., & Xu, H. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-08-02561.2001 · Cited by 492
β‐Amyloid inhibits integrated mitochondrial respiration and key enzyme activities
Casley, C. S., Canevari, L., Land, J. M., Clark, J. B., & Sharpe, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2001.00681.x · Cited by 485
Intracellular accumulation of β-amyloid1–42 in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer’s disease
Nagele, R. G., D’Andrea, M. R., Anderson, W. J., & Wang, H.-Y. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00460-2 · Cited by 468
Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain
Takahashi, R. H., Almeida, C. G., Kearney, P. F., Yu, F., Lin, M. T., Milner, T. A., & Gouras, G. K. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5167-03.2004 · Cited by 445
Alzheimer’s disease pathogenesis and therapeutic interventions
Parihar, M. S., & Hemnani, T. (2004) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2003.12.007 · Cited by 441
Molecular Mechanisms of Amyloid Oligomers Toxicity
Kayed, R., & Lasagna‐Reeves, C. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129001 · Cited by 440
Maturation and Endosomal Targeting of β-Site Amyloid Precursor Protein-cleaving Enzyme
Huse, J. T., Pijak, D. S., Leslie, G. J., Lee, V. M.-Y., & Doms, R. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004175200 · Cited by 402
Self-citation
Beta-amyloid accumulation in APP mutant neurons reduces PSD-95 and GluR1 in synapses
Almeida, C. G., Tampellini, D., Takahashi, R. H., Greengard, P., Lin, M. T., Snyder, E. M., & Gouras, G. K. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.02.008 · Cited by 397
Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer’s disease
D'Andrea, M. R., Nagele, R. G., Wang, H., Peterson, P. A., & Lee, D. H. S. (2001) · Histopathology · doi:10.1046/j.1365-2559.2001.01082.x · Cited by 390
Altered Metabolism of the Amyloid β Precursor Protein Is Associated with Mitochondrial Dysfunction in Down's Syndrome
Busciglio, J., Pelsman, A., Wong, C., Pigino, G., Yuan, M., Mori, H., & Yankner, B. A. (2002) · Neuron · doi:10.1016/s0896-6273(02)00604-9 · Cited by 387
Alzheimer Disease: Mechanistic Understanding Predicts Novel Therapies
Selkoe, D. J. (2004) · Annals of Internal Medicine · doi:10.7326/0003-4819-140-8-200404200-00047 · Cited by 208
Temporal Profile of Amyloid-β (Aβ) Oligomerization in an in Vivo Model of Alzheimer Disease
Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L., & LaFerla, F. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507892200 · Cited by 379
Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease
Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372
Endoplasmic reticulum and trans-Golgi network generate distinct populations of Alzheimer β-amyloid peptides
Greenfield, J. P., Tsai, J., Gouras, G. K., Hai, B., Thinakaran, G., Checler, F., Sisodia, S. S., Greengard, P., & Xu, H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.2.742 · Cited by 366
Cytosolic β-amyloid deposition and supranuclear cataracts in lenses from people with Alzheimer's disease
Goldstein, L. E., Muffat, J., Cherny, R. A., Moir, R. D., Ericsson, M., Huang, X., Mavros, C., Coccia, J. A., Faget, K. Y., Fitch, K. A., et al. (2003) · The Lancet · doi:10.1016/s0140-6736(03)12981-9 · Cited by 366
A modified β‐amyloid hypothesis: intraneuronal accumulation of the β‐amyloid peptide – the first step of a fatal cascade
Wirths, O., Multhaup, G., & Bayer, T. A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02737.x · Cited by 357
Plaque formation and the intraneuronal accumulation of β‐amyloid in Alzheimer's disease
Takahashi, R. H., Nagao, T., & Gouras, G. K. (2017) · Pathology International · doi:10.1111/pin.12520 · Cited by 373
Amyloid-β Aggregation
Finder, V. H., & Glockshuber, R. (2007) · Neurodegenerative Diseases · doi:10.1159/000100355 · Cited by 367
Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease
Gouras, G. K., Almeida, C. G., & Takahashi, R. H. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.022 · Cited by 338
Amyloid-Beta Protein Clearance and Degradation (ABCD) Pathways and their Role in Alzheimer’s Disease
Baranello, R., Bharani, K., Padmaraju, V., Chopra, N., Lahiri, D., Greig, N., Pappolla, M., & Sambamurti, K. (2015) · Current Alzheimer Research · doi:10.2174/1567205012666141218140953 · Cited by 331
Protein Kinase C-dependent α-Secretase Competes with β-Secretase for Cleavage of Amyloid-β Precursor Protein in the Trans-Golgi Network
Skovronsky, D., Moore, D. B., Milla, M. E., Doms, R. W., & Lee, V. M. ‐. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2568 · Cited by 325
Self-citation
Dietary Docosahexaenoic Acid and Docosapentaenoic Acid Ameliorate Amyloid-β and Tau Pathology via a Mechanism Involving Presenilin 1 Levels
Green, K. N., Martínez‐Coria, H., Khashwji, H., Hall, E. B., Yurko‐Mauro, K., Ellis, L., & LaFerla, F. M. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0055-07.2007 · Cited by 336
Mean age-of-onset of familial alzheimer disease caused by presenilin mutations correlates with both increased Aβ42 and decreased Aβ40
Kumar‐Singh, S., Theuns, J., Broeck, B. V., Pirici, D. N., Vennekens, K., Corsmit, E., Cruts, M., Dermaut, B., Wang, R., & Broeckhoven, C. V. (2006) · Human Mutation · doi:10.1002/humu.20336 · Cited by 330
Apolipoprotein E: From lipid transport to neurobiology
Hauser, P. S., Narayanaswami, V., & Ryan, R. O. (2011) · Progress in Lipid Research · doi:10.1016/j.plipres.2010.09.001 · Cited by 320
ERGIC-53 and traffic in the secretory pathway
Hauri, H., Kappeler, F., Andersson, H. M., & Appenzeller‐Herzog, C. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.4.587 · Cited by 320
Oxidative Stress Induces Intracellular Accumulation of Amyloid β-Protein (Aβ) in Human Neuroblastoma Cells
Misonou, H., Morishima-Kawashima, M., & Ihara, Y. (2000) · Biochemistry · doi:10.1021/bi000169p · Cited by 304
Human and Murine ApoE Markedly Alters Aβ Metabolism before and after Plaque Formation in a Mouse Model of Alzheimer's Disease
Fagan, A. M., Watson, M., Parsadanian, M., Bales, K. R., Paul, S. M., & Holtzman, D. M. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0483 · Cited by 290
Wnt signaling function in Alzheimer’s disease
Ferrari, G. V. D., & Inestrosa, N. C. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00021-7 · Cited by 289
Amyloid-β peptide binds with heme to form a peroxidase: Relationship to the cytopathologies of Alzheimer’s disease
Atamna, H., & Boyle, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600134103 · Cited by 291
Mechanisms of Hybrid Oligomer Formation in the Pathogenesis of Combined Alzheimer's and Parkinson's Diseases
Tsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003135 · Cited by 281
Retracted
Manipulating the Amyloid-β Aggregation Pathway with Chemical Chaperones
Yang, D., Yip, C. M., Huang, T. H. J., Chakrabartty, A., & Fraser, P. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.46.32970 · Cited by 268
Aβ and tau form soluble complexes that may promote self aggregation of both into the insoluble forms observed in Alzheimer’s disease
Guo, J., Arai, T., Miklossy, J., & McGeer, P. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509386103 · Cited by 260
A Dynamic Relationship between Intracellular and Extracellular Pools of Aβ
Oddo, S., Caccamo, A., Smith, I. F., Green, K. N., & LaFerla, F. M. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.050593 · Cited by 261
The Arctic Alzheimer mutation facilitates early intraneuronal Aβ aggregation and senile plaque formation in transgenic mice
Lord, A., Kalimo, H., Eckman, C., Zhang, X.-Q., Lannfelt, L., & Nilsson, L. N. G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.12.007 · Cited by 260
Intraneuronal Aβ42 accumulation in Down syndrome brain: Original Articles
Mori, C., Spooner, E. T., Wisniewski, K. E., Wisniewski, T. M., Yamaguchi, H., Saido, T. C., Tolan, D. R., Selkoe, D. J., & Lemere, C. A. (2002) · Amyloid · doi:10.3109/13506120208995241 · Cited by 255
Alpha‐synuclein in Lewy Body Disease and Alzheimer's Disease
Hashimoto, M., & Masliah, E. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00552.x · Cited by 254
Intraneuronal Aβ-Amyloid Precedes Development of Amyloid Plaques in Down Syndrome
Gyure, K. A., Durham, R., Stewart, W. F., Smialek, J. E., & Troncoso, J. C. (2001) · Archives of Pathology & Laboratory Medicine · doi:10.5858/2001-125-0489-iaapdo · Cited by 248
Inhibition of Intracellular Cholesterol Transport Alters Presenilin Localization and Amyloid Precursor Protein Processing in Neuronal Cells
Runz, H., Rietdorf, J., Tomic, I., de Bernard, M., Beyreuther, K. T., Pepperkok, R., & Hartmann, T. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01679.2002 · Cited by 242
Heat Shock Protein 70 Participates in the Neuroprotective Response to Intracellularly Expressed β-Amyloid in Neurons
Magrané, J., Smith, R. C., Walsh, K. X., & Querfurth, H. W. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.4330-03.2004 · Cited by 246
The role of exosomes in the processing of proteins associated with neurodegenerative diseases
Vella, L. J., Sharples, R. A., Nisbet, R. M., Cappai, R., & Hill, A. F. (2007) · European Biophysics Journal · doi:10.1007/s00249-007-0246-z · Cited by 242
Mechanism of the cleavage specificity of Alzheimer’s disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein
Lichtenthaler, S. F., Wang, R., Grimm, H. S., Uljon, S., Masters, C. L., & Beyreuther, K. T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3053 · Cited by 231
Gradual Alteration of Mitochondrial Structure and Function by β-Amyloids: Importance of Membrane Viscosity Changes, Energy Deprivation, Reactive Oxygen Species Production, and Cytochrome c Release
Aleardi, A. M., Benard, G., Augereau, O., Malgat, M., Talbot, J.-C., Mazat, J., Letellier, T., Dachary-Prigent, J., Solaini, G., & Rossignol, R. (2005) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-005-6631-3 · Cited by 227
In vivo detection of amyloid plaques in a mouse model of Alzheimer's disease
Skovronsky, D., Zhang, B., Kung, M., Kung, H. F., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.13.7609 · Cited by 212
Self-citation
Intracellular Accumulation of Amyloidogenic Fragments of Amyloid-β Precursor Protein in Neurons with Niemann-Pick Type C Defects Is Associated with Endosomal Abnormalities
Jin, L., Maezawa, I., Vincent, I. J., & Bird, T. D. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63185-9 · Cited by 212
Intracellular Transport, Assembly, and Degradation of Wild-Type and Disease-linked Mutant Gap Junction Proteins
VanSlyke, J. K., Deschênes, S. M., & Musil, L. S. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.6.1933 · Cited by 210
The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing
Pietrzik, C. U., Busse, T., Merriam, D. E., Weggen, S., & Koo, E. H. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf568 · Cited by 198
Ibuprofen reduces Aβ, hyperphosphorylated tau and memory deficits in Alzheimer mice
McKee, A. C., Carreras, I., Hossain, L., Ryu, H., Klein, W. L., Oddo, S., LaFerla, F. M., Jenkins, B. G., Kowall, N. W., & Dedeoglu, A. (2008) · Brain Research · doi:10.1016/j.brainres.2008.01.095 · Cited by 201
β-Secretase Processing in the Trans-Golgi Network Preferentially Generates Truncated Amyloid Species That Accumulate in Alzheimer’s Disease Brain
Huse, J. T., Liu, K., Pijak, D. S., Carlin, D., Lee, V. M.-Y., & Doms, R. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111141200 · Cited by 176
Self-citation
Intracellular Amyloid-β1–42, but Not Extracellular Soluble Amyloid-β Peptides, Induces Neuronal Apoptosis
Kienlen-Campard, P., Miolet, S., Tasiaux, B., & Octave, J.-N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200887200 · Cited by 187
The Chaperone BiP/GRP78 Binds to Amyloid Precursor Protein and Decreases Aβ40 and Aβ42 Secretion
Yang, Y., Turner, R. S., & Gaut, J. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.25552 · Cited by 179
Key Factors in Alzheimer's Disease: β‐amyloid Precursor Protein Processing, Metabolism and Intraneuronal Transport
Bayer, T. A., Wirths, O., Majtényi, K., Hartmann, T., Multhaup, G., Beyreuther, K. T., & Czech, C. (2001) · Brain Pathology · doi:10.1111/j.1750-3639.2001.tb00376.x · Cited by 174
Aβ42 Mutants with Different Aggregation Profiles Induce Distinct Pathologies in Drosophila
Iijima, K., Chiang, H., Hearn, S., Hakker, I., Gatt, A., Shenton, C., Granger, L., Leung, A., Iijima‐Ando, K., & Zhong, Y. (2008) · PLoS ONE · doi:10.1371/journal.pone.0001703 · Cited by 169
JNK activation is associated with intracellular β-amyloid accumulation
Shoji, M., Iwakami, N., Takeuchi, S., Waragai, M., Suzuki, M., Kanazawa, I., Lippa, C. F., Ono, S., & Okazawa, H. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00245-x · Cited by 167
Apolipoprotein E and cholesterol in aging and disease in the brain
de Chaves, E. P., Narayanaswami, V., Christoffersen, C., & Nielsen, L. B. (2008) · Future Lipidology · doi:10.2217/17460875.3.5.505 · Cited by 164
Visualization of fibrillar amyloid deposits in living, transgenic Caenorhabditis elegans animals using the sensitive amyloid dye, X-34
Link, C. D., Johnson, C. J., Fonte, V. G., Paupard, M., Hall, D. H., Styren, S. D., Mathis, C. A., & Klunk, W. E. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00237-2 · Cited by 157
Accumulation and Aggregation of Amyloid β-Protein in Late Endosomes of Niemann-Pick Type C Cells
Yamazaki, T., Chang, T., Haass, C., & Ihara, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009598200 · Cited by 156
Nilotinib-induced autophagic changes increase endogenous parkin level and ubiquitination, leading to amyloid clearance
Lonskaya, I., Hebron, M. L., Desforges, N. M., Schachter, J. B., & Moussa, C. E.-H. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1112-3 · Cited by 152
APP Processing Induced by Herpes Simplex Virus Type 1 (HSV-1) Yields Several APP Fragments in Human and Rat Neuronal Cells
Chiara, G. D., Marcocci, M. E., Civitelli, L., Argnani, R., Piacentini, R., Ripoli, C., Manservigi, R., Grassi, C., Garaci, E., & Palamara, A. T. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013989 · Cited by 152
NF‐κB pathway: a target for preventing β‐amyloid (Aβ)‐induced neuronal damage and Aβ42 production
Valerio, A., Boroni, F., Benarese, M., Sarnico, I., Ghisi, V., Bresciani, L. G., Ferrario, M., Borsani, G., Spano, P., & Pizzi, M. (2006) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.04722.x · Cited by 148
THE GENETICS AND MOLECULAR PATHOLOGY OF ALZHEIMER'S DISEASE
Selkoe, D. J. (2000) · Neurologic Clinics · doi:10.1016/s0733-8619(05)70232-2 · Cited by 146
The Presence of Amyloid β-Protein in the Detergent-Insoluble Membrane Compartment of Human Neuroblastoma Cells
Morishima‐Kawashima, M., & Ihara, Y. (1998) · Biochemistry · doi:10.1021/bi981843u · Cited by 146
Alzheimer's Disease and the Amyloid β Protein
Small, D. H., & McLean, C. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730443.x · Cited by 146
β-Amyloid Mediated Nitration of Manganese Superoxide Dismutase
Muthuswamy, A., Tangpong, J., Keller, J. N., Murphy, M. P., Markesbery, W. R., Kiningham, K. K., & Clair, D. K. S. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051223 · Cited by 144
Intraneuronal amyloid‐β1‐42 production triggered by sustained increase of cytosolic calcium concentration induces neuronal death
Pierrot, N., Ghisdal, P., Caumont, A., & Octave, J. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02227.x · Cited by 146
Tyrosine kinase inhibition increases functional parkin‐Beclin‐1 interaction and enhances amyloid clearance and cognitive performance
Lonskaya, I., Hebron, M. L., Desforges, N. M., Franjie, A., & Moussa, C. (2013) · EMBO Molecular Medicine · doi:10.1002/emmm.201302771 · Cited by 143
Biochemistry and Molecular Biology of Amyloid β‐Protein and the Mechanism of Alzheimer's Disease
(2008) · Handbook of Clinical Neurology · doi:10.1016/s0072-9752(07)01223-7 · Cited by 137
Statins Cause Intracellular Accumulation of Amyloid Precursor Protein, β-Secretase-cleaved Fragments, and Amyloid β-Peptide via an Isoprenoid-dependent Mechanism
Cole, S. L., Grudzien, A., Manhart, I. O., Kelly, B. L., Oakley, H. D., & Vassar, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413895200 · Cited by 133
Presenilin-1 P264L Knock-In Mutation: Differential Effects on Aβ Production, Amyloid Deposition, and Neuronal Vulnerability
Siman, R., Reaume, A. G., Savage, M. J., Trusko, S., Lin, Y.-G., Scott, R. W., & Flood, D. G. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-23-08717.2000 · Cited by 133
Signal transduction during amyloid-β-peptide neurotoxicity: role in Alzheimer disease
Fuentealba, R. A., Farı́as, G. G., Scheu, J., Bronfman, M., Marzolo, M., & Inestrosa, N. C. (2004) · Brain Research Reviews · doi:10.1016/j.brainresrev.2004.07.018 · Cited by 126
Thymoquinone protects cultured rat primary neurons against amyloid β-induced neurotoxicity
Alhebshi, A., Gotoh, M., & Suzuki, I. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.11.139 · Cited by 127
Elevation of β-Amyloid Peptide 2–42 in Sporadic and Familial Alzheimer's Disease and Its Generation in PS1 Knockout Cells
Wiltfang, J., Esselmann, H., Cupers, P., Neumann, M., Kretzschmar, H. A., Beyermann, M., Schleuder, D., Jahn, H., Rüther, E., Kornhuber, J., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102790200 · Cited by 126
Three-dimensional tracking of axonal projections in the brain by magnetic resonance imaging
Mori, S., Crain, B. J., Chacko, V. P., & van Zijl, P. C. M. (1999) · Annals of Neurology · doi:10.1002/1531-8249(199902)45:2 · Cited by 3,513
Self-citation
Intraneuronal APP/Aβ Trafficking and Plaque Formation in β‐Amyloid Precursor Protein and Presenilin‐1 Transgenic Mice
Wirths, O., Multhaup, G., Czech, C., Feldmann, N., Blanchard, V., Tremp, G., Beyreuther, K., Pradier, L., & Bayer, T. A. (2002) · Brain Pathology · doi:10.1111/j.1750-3639.2002.tb00442.x · Cited by 125
Amyloid ?? peptide induces cytochrome c release from isolated mitochondria
Kim, H.-S., Lee, J.-H., Lee, J.-P., Kim, E.-M., Chang, K.-A., Park, C. H., Jeong, S.-J., Wittendorp, M. C., Seo, J.-H., Choi, S.-H., et al. (2002) · NeuroReport · doi:10.1097/00001756-200210280-00032 · Cited by 124
Differential Effects of Mitochondrial Heat Shock Protein 60 and Related Molecular Chaperones to Prevent Intracellular β-Amyloid-induced Inhibition of Complex IV and Limit Apoptosis
Veereshwarayya, V., Kumar, P., Rosen, K. M., Mestril, R., & Querfurth, H. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602533200 · Cited by 125
Anandamide and noladin ether prevent neurotoxicity of the human amyloid-β peptide
Milton, N. G. N. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00936-9 · Cited by 125
The role of the endosomal/ lysosomal system in amyloid-beta production and the pathophysiology of Alzheimer's disease: Reexamining the spatial paradox from a lysosomal perspective
Pasternak, S., Callahan, J. W., & Mahuran, D. J. (2003) · Journal of Alzheimer s Disease · doi:10.3233/jad-2004-6107 · Cited by 127
Silibinin inhibits acetylcholinesterase activity and amyloid β peptide aggregation: a dual-target drug for the treatment of Alzheimer’s disease
Duan, S., Guan, X., Lin, R., Liu, X., Yan, Y., Lin, R., Zhang, T., Chen, X., Huang, J., Sun, X., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.02.002 · Cited by 121
Calcium-mediated Transient Phosphorylation of Tau and Amyloid Precursor Protein Followed by Intraneuronal Amyloid-β Accumulation
Pierrot, 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 121
The Nonfibrillar Amyloid β‐Peptide Induces Apoptotic Neuronal Cell Death
Pillot, T., Drouet, B., Queillé, S., Labeur, C., Vandekerckhove, J. S., Rosseneu, M., Pinçon‐Raymond, M., & Chambaz, J. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0731626.x · Cited by 134
Internalization of β-Amyloid Peptide by Primary Neurons in the Absence of Apolipoprotein E
Saavedra, L., Mohamed, A., Ma, V., Kar, S., & de Chaves, E. P. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701823200 · Cited by 118
Amyloid Precursor Protein and Amyloid β Peptide in Human Platelets
Skovronsky, D., Lee, V. M. ‐., & Praticò, D. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006285200 · Cited by 110
Self-citation
Intracellular Accumulation of Insoluble, Newly Synthesized Aβn-42 in Amyloid Precursor Protein-transfected Cells That Have Been Treated with Aβ1–42
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
Transmembrane-4-superfamily proteins CD151 and CD81 associate with α3β1 integrin, and selectively contribute to α3β1-dependent neurite outgrowth
Stipp, C. S., & Hemler, M. E. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.11.1871 · Cited by 107
A Sensitive and Quantitative Assay for Measuring Cleavage of Presenilin Substrates
Karlström, H., Bergman, A., Lendahl, U., Näslund, J., & Lundkvist, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c100649200 · Cited by 103
Inclusion body myositis-like phenotype induced by transgenic overexpression of βAPP in skeletal muscle
Sugarman, M. C., Yamasaki, T. R., Oddo, S., Echegoyen, J. C., Murphy, M. P., Golde, T. E., Jannatipour, M., Leissring, M. A., & LaFerla, F. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082545599 · Cited by 104
Distinct Pools of β-Amyloid in Alzheimer Disease–Affected Brain: A Clinicopathologic Study
Steinerman, J. R., Irizarry, M., Scarmeas, N., Raju, S., Brandt, J., Albert, M., Blacker, D., Hyman, B., & Stern, Y. (2008) · Archives of Neurology · doi:10.1001/archneur.65.7.906 · Cited by 104

Authors: Skovronsky, D. M., Doms, R. W., & Lee, V. M.-Y.
Affiliations: University of Pennsylvania (US)
ORCID: Lee, Virginia M.-Y.
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 1998-05-18
Volume: 141
Issue: 4
Pages: 1031-1039
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.141.4.1031
PMC: PMC2132781
OpenAlex: W2130792655
Cited by: 290
References: 36
Citations by year: 2026: 2 · 2025: 4 · 2024: 4 · 2023: 4 · 2022: 6 · 2021: 3 · 2019: 8 · 2018: 2 · 2017: 4 · 2016: 1 · 2015: 6 · 2014: 3 · 2013: 8 · 2012: 8
FWCI: 15.16
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Cell Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta, amyloid-beta 42, Aβ40, endoplasmic reticulum, amyloidogenesis, Alzheimer's disease, amyloid plaques, amyloid precursor protein overexpression, formic acid extraction
MeSH terms: Alzheimer Disease, Animals, Brain, Cell Line, Endoplasmic Reticulum, Genetic Vectors, Cricetinae, Humans, Neurons, Peptide Fragments, Recombinant Proteins, Semliki forest virus, Solubility, Subcellular Fractions, Transfection, Tumor Cells, Cultured, Amyloid beta-Peptides, CHO Cells, Carcinoma, Embryonal

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

Detection of a Novel Intraneuronal Pool of Insoluble Amyloid β Protein that Accumulates with Time in Culture

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks