The DOI matches its Crossref record; 71 of the 72 references it cites were found in a registry or an index.
Soluble Aβ Oligomers Are Rapidly Sequestered from Brain ISF In Vivo and Bind GM1 Ganglioside on Cellular Membranes
Open accessAbstract
Soluble Aβ oligomers contribute importantly to synaptotoxicity in Alzheimer's disease, but their dynamics in vivo remain unclear. Here, we found that soluble Aβ oligomers were sequestered from brain interstitial fluid onto brain membranes much more rapidly than nontoxic monomers and were recovered in part as bound to GM1 ganglioside on membranes. Aβ oligomers bound strongly to GM1 ganglioside, and blocking the sialic acid residue on GM1 decreased oligomer-mediated LTP impairment in mouse hippocampal slices. In a hAPP transgenic mouse model, substantial levels of GM1-bound Aβ₄₂ were recovered from brain membrane fractions. We also detected GM1-bound Aβ in human CSF, and its levels correlated with Aβ₄₂, suggesting its potential as a biomarker of Aβ-related membrane dysfunction. Together, these findings highlight a mechanism whereby hydrophobic Aβ oligomers become sequestered onto GM1 ganglioside and presumably other lipids on neuronal membranes, where they may induce progressive functional and structural changes.
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
1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“If so, this could help clarify potential mechanisms behind observations that Ab oligomers, but not monomers, can exert synaptotoxicity (Gong et al., 2003; Klyubin et al., 2005; Lacor et al., 2004; Lambert et al., 1998; Lesné et al., 2006; Shankar et al., 2007, 2008; Walsh et al., 2002), alter tau and other cytoskeleta…”
RetractedTerry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291
Self-citationMembrane vesicles as conveyors of immune responses
Théry, C., Ostrowski, M., & Segura, É. (2009) · Nature reviews. Immunology · doi:10.1038/nri2567 · Cited by 3,996
Clinical and biomarker changes in dominantly inherited Alzheimer's disease
Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Self-citationDiffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Cerebrospinal fluid biomarker signature in Alzheimer's disease neuroimaging initiative subjects
Shaw, L. M., Vanderstichele, H., Knapik‐Czajka, M., Clark, C. M., Aisen, P. S., Petersen, R. C., Blennow, K., Soares, H., Simon, A., Lewczuk, P., et al. (2009) · Annals of Neurology · doi:10.1002/ana.21610 · Cited by 2,065
The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes
Benilova, I., Karran, E., & De Strooper, B. (2012) · Nature Neuroscience · doi:10.1038/nn.3028 · Cited by 1,962
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
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592
Self-citationCellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526
Alzheimer’s Disease Neuroimaging Initiative
Mueller, S. G., Weiner, M. W., Thal, L. J., Petersen, R. C., Jack, C. R., Jagust, W. J., Trojanowski, J. Q., Toga, A. W., & Beckett, L. A. (2007) · Springer eBooks · doi:10.1007/978-0-387-72076-0_18 · Cited by 1,493
Differences in the pattern of hippocampal neuronal loss in normal ageing and Alzheimer's disease
West, M. J., Coleman, P. D., Flood, D. G., & Troncoso, J. C. (1994) · The Lancet · doi:10.1016/s0140-6736(94)92338-8 · Cited by 1,267 · cited 1×
“Enhanced synapse loss, particularly in the temporal and frontal cortices, helps distinguish AD from normal brain aging (West et al., 1994) and serves as a strong correlate of cognitive decline (Terry et al.”
Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000
Self-citationSynaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882
Jin, M., Shepardson, N., Yang, T., Chen, G., Walsh, D., & Selkoe, D. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017033108 · Cited by 876
Self-citationβ-Amyloid1–42 Binds to α7 Nicotinic Acetylcholine Receptor with High Affinity
Wang, H.-Y., Lee, D. H. S., D’Andrea, M. R., Peterson, P. A., Shank, R. P., & Reitz, A. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5626 · Cited by 818
Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H., & LaFerla, F. M. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.003 · Cited by 780
Li, S., Jin, M., Koeglsperger, T., Shepardson, N. E., Shankar, G. M., & Selkoe, D. J. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0203-11.2011 · Cited by 703
Self-citationReduction of β‐amyloid peptide42 in the cerebrospinal fluid of patients with Alzheimer's disease
Motter, R., Vigo‐Pelfrey, C., Kholodenko, D., Barbour, R., Johnson‐Wood, K., Galasko, D., Chang, L., Miller, B., Clark, C., Green, R., et al. (1995) · Annals of Neurology · doi:10.1002/ana.410380413 · Cited by 701
Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686
De Felice, F. G., Vieira, M. N. N., Bomfim, T. R., Decker, H., Velasco, P. T., Lambert, M. P., Viola, K. L., Zhao, W.-Q., Ferreira, S. T., & Klein, W. L. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809158106 · Cited by 657
Crystal structure of cholera toxin B‐pentamer bound to receptor G M1 pentasaccharide
Merritt, E. A., Sarfaty, S., van den Akker, F., L'Hoir, C., MARTIAL, J. A., & Hol, W. G. J. (1994) · Protein Science · doi:10.1002/pro.5560030202 · Cited by 573
GM1 ganglioside–bound amyloid β–protein (Aβ): A possible form of preamyloid in Alzheimer's disease
Yanagisawa, K., Odaka, A., Suzuki, N., & Ihara, Y. (1995) · Nature Medicine · doi:10.1038/nm1095-1062 · Cited by 544
Self-citationAmyloid β protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo
Klyubin, I., Walsh, D. M., Lemere, C. A., Cullen, W. K., Shankar, G. M., Betts, V., Spooner, E. T., Jiang, L., Anwyl, R., Selkoe, D. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1234 · Cited by 489
Self-citationKim, T., Vidal, G. S., Djurisic, M., William, C. M., Birnbaum, M. E., Garcia, K. C., Hyman, B. T., & Shatz, C. J. (2013) · Science · doi:10.1126/science.1242077 · Cited by 410
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
Self-citationMice lacking complex gangliosides develop Wallerian degeneration and myelination defects
Sheikh, K. A., Sun, J., Liu, Y., Kawai, H., Crawford, T. O., Proia, R. L., Griffin, J. W., & Schnaar, R. L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.13.7532 · Cited by 396
Tomiyama, T., Matsuyama, S., Iso, H., Umeda, T., Takuma, H., Ohnishi, K., Ishibashi, K., Teraoka, R., Sakama, N., Yamashita, T., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5825-09.2010 · Cited by 396
Cirrito, J. R., May, P. C., O'Dell, M. A., Taylor, J. W., Parsadanian, M., Cramer, J. W., Audia, J. E., Nissen, J. S., Bales, K. R., Paul, S. M., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08844.2003 · Cited by 394
Anti-Aβ Therapeutics in Alzheimer's Disease: The Need for a Paradigm Shift
Golde, T. E., Schneider, L. S., & Koo, E. H. (2011) · Neuron · doi:10.1016/j.neuron.2011.01.002 · Cited by 382
Thermodynamics of lipid–peptide interactions
Seelig, J. (2004) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2004.08.004 · Cited by 348
Gangliosides as components of lipid membrane domains
Sonnino, S., Mauri, L., Chigorno, V., & Prinetti, A. (2006) · Glycobiology · doi:10.1093/glycob/cwl052 · Cited by 342
McLaurin, J., & Chakrabartty, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.43.26482 · Cited by 337
Svennerholm, L. T., & Gottfries, C. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62031039.x · Cited by 327
Decreased cerebrospinal fluid Aβ 42 correlates with brain atrophy in cognitively normal elderly
Fagan, A. M., Head, D., Shah, A. R., Marcus, D., Mintun, M., Morris, J. C., & Holtzman, D. M. (2009) · Annals of Neurology · doi:10.1002/ana.21559 · Cited by 327 · cited 2×
“In light of numerous such studies implicating a pathogenic role of soluble Ab oligomers and the evidence that lowered Ab42 monomer levels in cerebrospinal fluid (CSF) represents the earliest biomarker for AD (Bateman et al., 2012; Craig-Schapiro et al., 2009; Fagan et al., 2009; Golde et al., 2011; Morris and Selkoe,…”
Cholera Toxin: Interaction of Subunits with Ganglioside G M1
HEYNINGEN, S. V. (1974) · Science · doi:10.1126/science.183.4125.656 · Cited by 326
Klyubin, I., Betts, V., Welzel, A. T., Blennow, K., Zetterberg, H., Wallin, A., Lemere, C. A., Cullen, W. K., Peng, Y., Wisniewski, T., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.5161-07.2008 · Cited by 321
Self-citationAmyloid‐beta oligomerization in Alzheimer dementia versus high‐pathology controls
Esparza, T. J., Zhao, H., Cirrito, J. R., Cairns, N. J., Bateman, R. J., Holtzman, D. M., & Brody, D. L. (2012) · Annals of Neurology · doi:10.1002/ana.23748 · Cited by 319
Choo, L.-P., Garzon-Rodriguez, W., Glabe, C. G., & Surewicz, W. K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.37.22987 · Cited by 317
Interaction between Human Prion Protein and Amyloid-β (Aβ) Oligomers
Chen, S., Yadav, S. P., & Surewicz, W. K. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145516 · Cited by 301
Ultrastructural localization of cell membrane G M1 ganglioside by cholera toxin
Hansson, H., Holmgren, J. R., & Svennerholm, L. T. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.9.3782 · Cited by 288
High‐molecular‐weight β‐amyloid oligomers are elevated in cerebrospinal fluid of Alzheimer patients
Fukumoto, H., Tokuda, T., Kasai, T., Ishigami, N., Hidaka, H., Kondo, M., Allsop, D., & Nakagawa, M. (2010) · The FASEB Journal · doi:10.1096/fj.09-150359 · Cited by 264
Demattos, R. B., Bales, K. R., Parsadanian, M., O'Dell, M. A., Foss, E. M., Paul, S. M., & Holtzman, D. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00889.x · Cited by 254
A Seed for Alzheimer Amyloid in the Brain
Hayashi, H., Kimura, N., Yamaguchi, H., Hasegawa, K., Yokoseki, T., Shibata, M. S., Yamamoto, N., Michikawa, M., Yoshikawa, Y., Terao, K., et al. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.0861-04.2004 · Cited by 239
Self-citationBiomarkers of Alzheimer's disease
Craig‐Schapiro, R., Fagan, A. M., & Holtzman, D. M. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.10.003 · Cited by 228
Molander‐Melin, M., Blennow, K., Bogdanović, N., Dellheden, B., Månsson, J., & Fredman, P. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02849.x · Cited by 224
Titration calorimetry of lipid–peptide interactions
Seelig, J. (1997) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/s0304-4157(97)00002-6 · Cited by 206
Li, S., Jin, M., Zhang, D., Yang, T., Koeglsperger, T., Fu, H., & Selkoe, D. J. (2013) · Neuron · doi:10.1016/j.neuron.2012.12.040 · Cited by 189
Self-citationZhao, W.-Q., Santini, F., Breese, R., Ross, D., Zhang, X. D., Stone, D. J., Ferrer, M., Townsend, M., Wolfe, A. L., Seager, M. A., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057182 · Cited by 188
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 185
Self-citationCharacterization of High-Affinity Binding between Gangliosides and Amyloid β-Protein
Ariga, T., Kobayashi, K., Hasegawa, A., Kiso, M., Ishida, H., & Miyatake, T. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2304 · Cited by 158
Yamamoto, N., Matsubara, T., Sato, T., & Yanagisawa, K. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.07.028 · Cited by 135
Self-citationYang, T., Hong, S. Y., O’Malley, T. T., Sperling, R. A., Walsh, D. M., & Selkoe, D. J. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.11.005 · Cited by 122
Self-citationYahi, N., Aulas, A., & Fantini, J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009079 · Cited by 112
Hong, S., Quintero-Monzon, O., Ostaszewski, B. L., Podlisny, D. R., Cavanaugh, W. T., Yang, T., Holtzman, D. M., Cirrito, J. R., & Selkoe, D. J. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3272-11.2011 · Cited by 111
Self-citationAβ40 Oligomers Identified as a Potential Biomarker for the Diagnosis of Alzheimer's Disease
Gao, C. M., Yam, A. Y., Wang, X., Magdangal, E., Salisbury, C., Peretz, D., Zuckermann, R. N., Connolly, M. D., Hansson, O., Minthon, L., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015725 · Cited by 105 · cited 1×
“A few reports of the detection of apparent Ab oligomers in CSF and plasma have appeared (Fukumoto et al., 2010; Gao et al., 2010; Klyubin et al., 2008; Villemagne et al., 2010); however, the interpretation of these reports has been clouded by failure to define the precise oligomeric unit the assays are detecting, an i…”
Gangliosides in Cerebrospinal Fluid in 'Probable Alzheimer's Disease'
Blennow, K., Davidsson, P., Wallin, A., Fredman, P., Gottfries, C. G., Karlsson, I., Månsson, J., & Svennerholm, L. T. (1991) · Archives of Neurology · doi:10.1001/archneur.1991.00530220048018 · Cited by 81
Wu, G., Xie, X., Lu, Z., & Ledeen, R. W. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.1.307 · Cited by 77
Blood-Borne Amyloid-β Dimer Correlates with Clinical Markers of Alzheimer's Disease
Villemagne, V. L., Perez, K. A., Pike, K. E., Kok, W. M., Rowe, C. C., White, A. R., Bourgeat, P., Salvado, O., Bedő, J., Hutton, C. A., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.5180-09.2010 · Cited by 72
Assembly of hereditary amyloid β‐protein variants in the presence of favorable gangliosides
Yamamoto, N., Hirabayashi, Y., Amari, M., Yamaguchi, H., Romanov, G. A., Nostrand, W. E. V., & Yanagisawa, K. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.03.013 · Cited by 70
Self-citationAltered Distribution of the Gangliosides GM1 and GM2 in Alzheimer’s Disease
Pernber, Z., Blennow, K., Bogdanović, N., Månsson, J., & Blomqvist, M. (2012) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000338181 · Cited by 60
Grimm, M. O. W., Zinser, E. G., Grösgen, S., Hundsdörfer, B., Rothhaar, T. L., Burg, V. K., Kaestner, L., Bayer, T. A., Lipp, P., Müller, U., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0034095 · Cited by 59
Yanagisawa, K., McLaurin, J., Michikawa, M., Chakrabartty, A., & Ihara, Y. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01484-1 · Cited by 43
Self-citationRecommendations for the incorporation of biomarkers into Alzheimer clinical trials: an overview
Morris, J. C., & Selkoe, D. J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.09.005 · Cited by 37
Self-citationSanghera, N., Wall, M. J., Vénien‐Bryan, C., & Pinheiro, T. J. T. (2008) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2008.02.017 · Cited by 28
Flagged first, then by citations
1 of the 72 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The amyloid hypothesis of Alzheimer's disease at 25 years
Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164
Self-citationComplement and microglia mediate early synapse loss in Alzheimer mouse models
Hong, S., Beja-Glasser, V. F., Nfonoyim, B. M., Frouin, A., Li, S., Ramakrishnan, S., Merry, K. M., Shi, Q., Rosenthal, A., Barres, B. A., et al. (2016) · Science · doi:10.1126/science.aad8373 · Cited by 3,343
“This could occur in multiple ways: soluble oAβ associates with synaptic membranes and other synaptic markers (4, 26); thus, oAβ bound to synapses may anchor C1q directly.”
Self-citationImmune attack: the role of inflammation in Alzheimer disease
Heppner, F. L., Ransohoff, R. M., & Becher, B. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3880 · Cited by 2,134
Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future
Zhang, Y., Chen, H., Li, R., Sterling, K., & Song, W. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01484-7 · Cited by 988
“For example, AβOs bind to sialic acid-containing GM1 ganglioside on cell membrane to induce LTP impairment.(64) On the other hand, cholesterol-rich lipid rafts provide an optimal environment for Aβ synthesis and enhance the interaction of Aβ with the membrane.”
Lee, S. J. C., Nam, E., Lee, H. J., Savelieff, M. G., & Lim, M. H. (2017) · Chemical Society Reviews · doi:10.1039/c6cs00731g · Cited by 576
Metadata
- Authors
- Hong, S., Ostaszewski, B. L., Yang, T., O’Malley, T. T., Jin, M., Yanagisawa, K., Li, S., Bartels, T., & Selkoe, D. J.
- Affiliations
- Brigham and Women's Hospital (US)
- University College Dublin (IE)
- National Center for Geriatrics and Gerontology (JP)
- Corresponding author
- Selkoe, Dennis J.
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2014-04
- Volume
- 82
- Issue
- 2
- Pages
- 308-319
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC4129520
- OpenAlex
- W2052707772
- Cited by
- 213
- References
- 72
- Citations by year
- 2026: 18 · 2025: 11 · 2024: 8 · 2023: 14 · 2022: 21 · 2021: 24 · 2020: 21 · 2019: 14 · 2018: 14 · 2017: 17 · 2016: 21 · 2015: 22 · 2014: 8
- FWCI
- 15.07
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R01AG027443, R01 AG06173, R01AG006173, P01AG036694)
- Yale Center for Clinical Investigation, Yale School of Medicine
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- soluble amyloid-beta oligomers, GM1 ganglioside, brain interstitial fluid, membrane binding, sialic acid, long-term potentiation, hippocampus, Alzheimer's disease, amyloid-beta 42, synaptotoxicity, membrane dysfunction
- MeSH terms
- Age Factors, Alzheimer Disease, Animals, Brain, Cell Membrane, Dose-Response Relationship, Drug, Embryo, Mammalian, G(M1) Ganglioside, Gangliosides, Hippocampus, Humans, Mice, Inbred C57BL, Mice, Transgenic, Mutation, Peptide Fragments, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Extracellular Fluid, Mice, 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