Cited by 67Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 351 of the 355 references it cites were found in a registry or an index.

Amyloid β-interacting partners in Alzheimer's disease: From accomplices to possible therapeutic targets

Han, Sun-Ho, Park, Jong-Chan, Mook-Jung, Inhee·2016·Progress in Neurobiology

DOI 10.1016/j.pneurobio.2015.12.004

Open this paper in CoChat — free account

Abstract

Alzheimer's disease (AD) is one of the most devastating neurodegenerative diseases in modern society because of insurmountable difficulties in early diagnosis and lack of therapeutic treatments. AD pathogenesis is tightly linked to the abnormal accumulation and aggregation of amyloid β (Aβ), seemingly the main causative factor of AD; however, intensive research on Aβ has not yet explained the complexity of AD pathogenesis. Consequently, the role of other supportive partners of Aβ have been elucidated and evaluated in the etiology of AD, and their potential molecular mechanisms have emerged as possible therapeutic targets. In this review, we compile information regarding Aβ-interacting partners in normal conditions and AD pathology, and analyze their etiological roles in diverse areas. Furthermore, we integrate this information into suggestions for probable clinical applications for AD diagnosis and therapeutics. We include Aβ-interacting partners localized to the cell surface and intracellular and extracellular compartments of different cell types ranging from the central nervous system to peripheral regions. Additionally, we expand the range of Aβ-interacting partners by including not only proteins, but also inorganic substances like metals, expecting that one of these partners may yield a critical breakthrough in the field of AD diagnostics and therapeutic drug development.

Integrity signals

Registry

Crossref · 10.1016/j.pneurobio.2015.12.004

Cites

351 of 351 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

2 retracted

Items 201–351 of 351

Expression of αB-crystallin in Alzheimer's disease
Renkawek, K., Voorter, C., Bosman, G. C. G. M., van Workum, F. V., & de Jong, W. D. (1994) · Acta Neuropathologica · doi:10.1007/bf00296185 · Cited by 157
Prion Protein-mediated Toxicity of Amyloid-β Oligomers Requires Lipid Rafts and the Transmembrane LRP1
Rushworth, J. V., Jarosz-Griffiths, H., Watt, N. T., & Hooper, N. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400358 · Cited by 157
Scavenger receptor CD36 is essential for the cerebrovascular oxidative stress and neurovascular dysfunction induced by amyloid-β
Park, L., Wang, G., Zhou, P., Zhou, J., Pitstick, R., Previti, M. L., Younkin, L., Younkin, S. G., Van Nostrand, W. E., Cho, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1015413108 · Cited by 156
Characterization of Apolipoprotein J-Alzheimer's Aβ Interaction
Matsubara, E., Frangione, B., & Ghiso, J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7563 · Cited by 153
Anti-PrPC monoclonal antibody infusion as a novel treatment for cognitive deficits in an alzheimer's disease model mouse
Chung, E., Ji, Y., Sun, Y., Kascsak, R. J., Kascsak, R. B., Mehta, P. D., Strittmatter, S. M., & Wisniewski, T. (2010) · BMC Neuroscience · doi:10.1186/1471-2202-11-130 · Cited by 152
Mitochondrial import and degradation of amyloid-β peptide
Pinho, C. M., Teixeira, P. F., & Glaser, E. G. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2014.02.007 · Cited by 149
Plasma apolipoprotein E and Alzheimer disease risk: The AIBL study of aging
Gupta, V. B., Laws, S. M., Villemagne, V. L., Ames, D., Bush, A. I., Ellis, K. A., Lui, J. K., Masters, C., Rowe, C. C., Szoeke, C., et al. (2011) · Neurology · doi:10.1212/wnl.0b013e318211c352 · Cited by 149
Alzheimer's disease: Effects of β-amyloid on mitochondria
Tillement, L., Lecanu, L., & Papadopoulos, V. (2010) · Mitochondrion · doi:10.1016/j.mito.2010.08.009 · Cited by 148
A molecular pathway of neurodegeneration linking α-synuclein to ApoE and Aβ peptides
Gallardo, G., Schlüter, O. M., & Südhof, T. C. (2008) · Nature Neuroscience · doi:10.1038/nn2058 · Cited by 145
Accelerated A Deposition in APPswe/PS1 E9 Mice with Hemizygous Deletions of TTR (Transthyretin)
Choi, S. H., Leight, S. N., Lee, V. M. ‐., Li, T., Wong, P. C., Johnson, J. A., Saraiva, M. J., & Sisodia, S. S. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1919-07.2007 · Cited by 145
Cyclophilins and their possible role in the stress response
Andreeva, L. V., Heads, R. J., & Green, C. J. (1999) · International Journal of Experimental Pathology · doi:10.1046/j.1365-2613.1999.00128.x · Cited by 144
S100B binding to RAGE in microglia stimulates COX-2 expression
Bianchi, R., Adami, C., Giambanco, I., & Donato, R. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0306198 · Cited by 144
The voltage-dependent anion channel 1 mediates amyloid β toxicity and represents a potential target for Alzheimer disease therapy
Smilansky, A., Dangoor, L., Nakdimon, I., Ben-Hail, D., Mizrachi, D., & Shoshan-Barmatz, V. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.691493 · Cited by 143
Microglial Activation is Required for Aβ Clearance After Intracranial Injection of Lipopolysaccharide in APP Transgenic Mice
Herber, D. L., Mercer, M., Roth, L. M., Symmonds, K., Maloney, J. L., Wilson, N., Freeman, M. J., Morgan, D., & Gordon, M. N. (2007) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-007-9069-z · Cited by 143
Amyloid precursor protein and amyloid β-peptide bind to ATP synthase and regulate its activity at the surface of neural cells
Schmidt, C., Lepsverdize, E., L, S., Das, A. M., Pizzo, S. V., Dityatev, A. E., & Schachner, M. (2007) · Molecular Psychiatry · doi:10.1038/sj.mp.4002077 · Cited by 139
Serum Albumin Concentration and Cognitive Impairment
Llewellyn, D. J., Langa, K. M., Friedland, R. P., & Lang, I. (2010) · Current Alzheimer Research · doi:10.2174/156720510790274392 · Cited by 138
Receptor for advanced glycation end products (RAGE) in a dash to the rescue: inflammatory signals gone awry in the primal response to stress
Herold, K. C., Moser, B., Chen, Y., Zeng, S., Yan, S. F., Ramasamy, R., Emond, J. C., Clynes, R., & Schmidt, A. M. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.1206751 · Cited by 138
Interaction of Nascent ApoE2, ApoE3, and ApoE4 Isoforms Expressed in Mammalian Cells with Amyloid Peptide β (1−40). Relevance to Alzheimer's Disease
Aleshkov, S., Abraham, C. R., & Zannis, V. I. (1997) · Biochemistry · doi:10.1021/bi9626362 · Cited by 138
Alpha 1-antichymotrypsin regulates Alzheimer beta-amyloid peptide fibril formation.
Eriksson, S., Janciauskiene, S. M., & Lannfelt, L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.6.2313 · Cited by 137
Synaptic Released Zinc Promotes Tau Hyperphosphorylation by Inhibition of Protein Phosphatase 2A (PP2A)
Sun, X., Wei, Y., Xiong, Y., Wang, X., Xie, A., Wang, X., Yang, Y., Wang, Q., Lu, Y., Liu, R., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.309070 · Cited by 137
Effect of TTP488 in patients with mild to moderate Alzheimer’s disease
Burstein, A. H., Grimes, I., Galasko, D. R., Aisen, P. S. S., Sabbagh, M. N., & Mjalli, A. M. M. (2014) · BMC Neurology · doi:10.1186/1471-2377-14-12 · Cited by 137
α-1-Antichymotrypsin Promotes β-Sheet Amyloid Plaque Deposition in a Transgenic Mouse Model of Alzheimer's Disease
Nilsson, L. N. G., Bales, K. R., DiCarlo, G., Gordon, M. N., Morgan, D., Paul, S. M., & Potter, H. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-05-01444.2001 · Cited by 137
Site-Specific Blockade of RAGE-VdPrevents Amyloid-β Oligomer Neurotoxicity
Sturchler, E., Galichet, A., Weibel, M., Leclerc, E., & Heizmann, C. W. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4878-07.2008 · Cited by 136
Aluminium, Alzheimer's disease, and drinking water
Neri, L., & Hewitt, D. (1991) · The Lancet · doi:10.1016/0140-6736(91)90531-s · Cited by 136
Increased soluble amyloid-β peptide and memory deficits in amyloid model mice overexpressing the low-density lipoprotein receptor-related protein
Zerbinatti, C. V., Wozniak, D. F., Cirrito, J., Cam, J. A., Osaka, H., Bales, K. R., Zhuo, M., Paul, S. M., Holtzman, D. M., & Bu, G. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0305803101 · Cited by 133
The low density lipoprotein receptor-related protein/alpha 2-macroglobulin receptor binds and mediates catabolism of bovine milk lipoprotein lipase
Chappell, D. A., Fry, G. L., Waknitz, M. A., Iverius, P. H., Williams, S. E., & Strickland, D. K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)35675-8 · Cited by 133
alpha2-Macroglobulin as a beta-amyloid peptide-binding plasma protein.
Du, Y., Ni, B., Glinn, M. A., Dodel, R. C., Bales, K. R., Zhang, Z., Hyslop, P. A., & Paul, S. M. (1997) · PubMed · Cited by 132
Innate immunity receptor CD36 promotes cerebral amyloid angiopathy
Park, L., Zhou, J., Zhou, P., Pistick, R., Jamal, S. E., Younkin, L. H., Pierce, J. P., Arreguin, A. J., Anrather, J., Younkin, S. G., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300021110 · Cited by 132
Zinc Binding to Alzheimer's Aβ(1–16) Peptide Results in Stable Soluble Complex
Kozin, S. A., Zirah, S., Rebuffat, S., Hoa, G. H. B., & Debey, P. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5284 · Cited by 131
A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, -RHDS-, that promotes cell adhesion
Ghiso, J. A., Rostagno, A. A., Gardella, J. E., Liem, L.-K., Gorevic, P. D., & Frangione, B. (1992) · Biochemical Journal · doi:10.1042/bj2881053 · Cited by 130
Apolipoprotein E and Low Density Lipoprotein Receptor-related Protein Facilitate Intraneuronal Aβ42 Accumulation in Amyloid Model Mice
Zerbinatti, C. V., Wahrle, S. E., Kim, H., Cam, J. A., Bales, K., Paul, S. M., Holtzman, D. M., & Bu, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604436200 · Cited by 129
Transthyretin Protects against A-Beta Peptide Toxicity by Proteolytic Cleavage of the Peptide: A Mechanism Sensitive to the Kunitz Protease Inhibitor
Costa, R., Ferreira-da-Silva, F., Saraiva, M., & Cardoso, I. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002899 · Cited by 128
Amyloid β Protein: Aβ40 Inhibits Aβ42 Oligomerization
Murray, M. M., Bernstein, S. L., Nyugen, V., Condron, M. M., Teplow, D. B., & Bowers, M. T. (2009) · Journal of the American Chemical Society · doi:10.1021/ja8092604 · Cited by 128
An interaction of β‐amyloid with aluminium in vitro
Exley, C., Price, N. C., Kelly, S. M., & Birchall, J. D. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80137-j · Cited by 128
Therapeutic Redistribution of Metal Ions To Treat Alzheimer’s Disease
Crouch, P. J., & Barnham, K. J. (2012) · Accounts of Chemical Research · doi:10.1021/ar300074t · Cited by 125
RAGE regulates BACE1 and Aβ generation via NFAT1 activation in Alzheimer's disease animal model
Cho, H. J., Son, S. M., Jin, S. M., Hong, H. S., Shin, D. H., Kim, S. J., Huh, K. H., & Mook‐Jung, I. (2009) · The FASEB Journal · doi:10.1096/fj.08-126383 · Cited by 124
Self-citation
Zinc induces protein phosphatase 2A inactivation and tau hyperphosphorylation through Src dependent PP2A (tyrosine 307) phosphorylation
Xiong, Y., Jing, X.-P., Zhou, X.-W., Wang, X.-L., Yang, Y., Sun, X.-Y., Qiu, M., Cao, F.-Y., Lu, Y.-M., Liu, R., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.07.003 · Cited by 122
Inhibition of amyloid-β plaque formation by α-synuclein
Bachhuber, T., Katzmarski, N., McCarter, J. F., Loreth, D., Tahirović, S., Kamp, F., Abou‐Ajram, C., Nuscher, B., Serrano‐Pozo, A., Müller, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3885 · Cited by 120
Effect of amyloid β‐peptide on permeability transition pore: A comparative study
Moreira, P. I., Santos, M. S., Moreno, A. J., Rego, A. C., & Oliveira, C. R. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10282 · Cited by 120
Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity
Nicoll, A. J., Panico, S., Freir, D. B., Wright, D., Terry, C., Risse, E., Herron, C. E., O’Malley, T., Wadsworth, J. D. F., Farrow, M. A., et al. (2013) · Nature Communications · doi:10.1038/ncomms3416 · Cited by 119
Decreased Proteolytic Activity of the Mitochondrial Amyloid-β Degrading Enzyme, PreP Peptidasome, in Alzheimer's Disease Brain Mitochondria
Alikhani, N., Guo, L., Yan, S., Du, H., Pinho, C. M., Chen, J. X., Glaser, E. G., & Yan, S. S. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101716 · Cited by 119
A theoretical molecular network for dyslexia: integrating available genetic findings.
Poelmans, G., Buitelaar, J. K., Pauls, D. L., & Franke, B. (2011) · Molecular Psychiatry · doi:10.1038/mp.2010.105 · Cited by 119
Purification and Characterization of Brain Clusterin
Oda, T., Pasinetti, G. M., Osterburg, H. H., Anderson, C., Johnson, S. A., & Finch, C. E. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2580 · Cited by 118
Seeding of Aβ Fibril Formation Is Inhibited by All Three Isotypes of Apolipoprotein E
Wood, S. J., Chan, W., & Wetzel, R. B. (1996) · Biochemistry · doi:10.1021/bi961074j · Cited by 118
β-Amyloid Modulation of Synaptic Transmission and Plasticity
Venkitaramani, D. V., Chin, J., Netzer, W. J., Gouras, G. K., Lesné, S., Malinow, R., & Lombroso, P. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.3478-07.2007 · Cited by 118
Cellular prion protein is essential for oligomeric amyloid- -induced neuronal cell death
Kudo, W., Hp, L., Zou, W.-Q., Wang, X., Perry, G., Zhu, X., Smith, M. A., Petersen, R. B., & Lee, H. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr542 · Cited by 116
Low-Density Lipoprotein Receptor-Related Protein 1 (LRP1) Mediates Neuronal Aβ42 Uptake and Lysosomal Trafficking
Fuentealba, R. A., Liu, Q., Zhang, J., Kanekiyo, T., Hu, X., Lee, J.-M., LaDu, M. J., & Bu, G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011884 · Cited by 116
Transthyretin and Alzheimer's disease: Where in the brain?
Sousa, J. C., Cardoso, I., Marques, F., Saraiva, M. J., & Palha, J. A. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.03.015 · Cited by 115
Early Changes in Hippocampal Eph Receptors Precede the Onset of Memory Decline in Mouse Models of Alzheimer's Disease
Simón, A. M., de Maturana, R. L., Ricobaraza, A., Escribano, L., Schiapparelli, L., Cuadrado‐Tejedor, M., Pérez‐Mediavilla, A., Ávila, J., Rı́o, J. D., & Frechilla, D. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1096 · Cited by 114
Alzheimer's Disease, β-Amyloid Protein and Zinc
Huang, X., Cuajungco, M. P., Atwood, C., Moir, R. D., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Nutrition · doi:10.1093/jn/130.5.1488s · Cited by 114
BRI2 (ITM2b) Inhibits A Deposition In Vivo
Kim, J., Miller, V. M., Levites, Y., West, K. J., Zwizinski, C. W., Moore, B. D., Troendle, F. J., Bann, M., Verbeeck, C., Price, R. W., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0891-08.2008 · Cited by 113
Reduced Levels of Amyloid-β-Binding Proteins in Cerebrospinal Fluid from Alzheimer's Disease Patients
Hansson, S., Andréasson, U., Wall, M., Skoog, I. G., Andreasen, N., Wallin, A., Zetterberg, H., & Blennow, K. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0966 · Cited by 113
α2‐Macroglobulin as a β‐Amyloid Peptide‐Binding Plasma Protein
Du, Y., Ni, B., Glinn, M., Dodel, R. C., Bales, K. R., Zhang, Z., Hyslop, P. A., & Paul, S. M. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69010299.x · Cited by 113
Effect of Zinc Binding on β-Amyloid Structure and Dynamics: Implications for Aβ Aggregation
Rezaei‐Ghaleh, N., Giller, K., Becker, S., & Zweckstetter, M. (2011) · Biophysical Journal · doi:10.1016/j.bpj.2011.06.062 · Cited by 112
Microglial Receptor for Advanced Glycation End Product-Dependent Signal Pathway Drives β-Amyloid-Induced Synaptic Depression and Long-Term Depression Impairment in Entorhinal Cortex
Origlia, N., Bonadonna, C., Rosellini, A., Leznik, E., Arancio, O., Yan, S. S., & Domenici, L. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2127-10.2010 · Cited by 111
Increased expression of the receptor for advanced glycation end products in neurons and astrocytes in a triple transgenic mouse model of Alzheimer’s disease
Choi, B.-R., Cho, W.-H., Kim, J., Lee, H. J., Chung, C., Jeon, W. K., & Han, J.-S. (2014) · Experimental & Molecular Medicine · doi:10.1038/emm.2013.147 · Cited by 111
Characterization of the Binding of Amyloid‐β Peptide to Cell Culture‐Derived Native Apolipoprotein E2, E3, and E4 Isoforms and to Isoforms from Human Plasma
Yang, D., Smith, J. D., Zhou, Z., Gandy, S. E., & Martins, R. N. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68020721.x · Cited by 111
Amyloid-targeted therapeutics in Alzheimer's disease: Use of human albumin in plasma exchange as a novel approach for abeta mobilization
Boada, M., Ortiz, P., Anaya, F., & Hernández, I. (2009) · Drug News & Perspectives · doi:10.1358/dnp.2009.22.6.1395256 · Cited by 110
RAGE: The Beneficial and Deleterious Effects by Diverse Mechanisms of Actions
Han, S.-H., Kim, Y. H., & Mook‐Jung, I. (2011) · Molecules and Cells · doi:10.1007/s10059-011-0030-x · Cited by 110
Self-citation
Inflammatory markers in younger vs elderly normal volunteers and in patients with Alzheimer’s disease
Maes, M. H. J., Devos, N., Wauters, A., Demedts, P., Maurits, V., Neels, H. M., Bosmans, E., Altamura, C. A., Lin, A., Song, C., et al. (1999) · Journal of Psychiatric Research · doi:10.1016/s0022-3956(99)00016-3 · Cited by 110
Aluminium and iron, but neither copper nor zinc, are key to the precipitation of β-sheets of Aβ42 in senile plaque cores in Alzheimer's disease
Exley, C. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-102-305 · Cited by 107
α2‐Macroglobulin Enhances the Clearance of Endogenous Soluble β‐Amyloid Peptide via Low‐Density Lipoprotein Receptor‐Related Protein in Cortical Neuron
Qiu, Z., Strickland, D. K., Hyman, B. T., & Rebeck, G. W. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0731393.x · Cited by 107
β Amyloid peptide (Aβ 42 ) is internalized via the G‐protein‐coupled receptor FPRL1 and forms fibrillar aggregates in macrophages 1
YAZAWA, H., YU, Z.-X., TAKEDA, K., LE, Y., GONG, W., FERRANS, V. J., OPPENHEIM, J. J., LI, C. C. H., & WANG, J. M. (2001) · The FASEB Journal · doi:10.1096/fj.01-0251com · Cited by 105
Peripheral reduction of β-amyloid is sufficient to reduce brain β-amyloid: Implications for Alzheimer's disease
Sutcliffe, J. G., Hedlund, P. B., Thomas, E. A., Bloom, F. E., & Hilbush, B. S. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22603 · Cited by 105
Untitled work
(2008) · doi:10.1074/jbc.m801487200 · Cited by 105
Postsynaptic Receptors for Amyloid-β Oligomers as Mediators of Neuronal Damage in Alzheimer’s Disease
Dinamarca, M. C., Ríos, J. A., & Inestrosa, N. C. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00464 · Cited by 105
Copper and Ceruloplasmin Abnormalities in Alzheimer’s Disease
Brewer, G. J., Kanzer, S. H., Zimmerman, E. A., Celmins, D. F., Heckman, S. M., & Dick, R. (2010) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/1533317510375083 · Cited by 104
Plasma Transthyretin as a Candidate Marker for Alzheimer's Disease
Velayudhan, L., Killick, R., Hye, A., Kinsey, A. M., Güntert, A., Lynham, S., Ward, M. A., Leung, R., Lourdusamy, A., To, A. W. M., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110611 · Cited by 103
Dissociating β-Amyloid from α7 Nicotinic Acetylcholine Receptor by a Novel Therapeutic Agent, S 24795, Normalizes α7 Nicotinic Acetylcholine and NMDA Receptor Function in Alzheimer's Disease Brain
Wang, H.-Y., Stucky, A., Liu, J., Shen, C., Trocmé, C., & Morain, P. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.6088-08.2009 · Cited by 102
Amyloid β binding proteins in vitro and in normal human cerebrospinal fluid
Golabek, A., Marques, M. A., Lalowski, M., & Wisniewski, T. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11565-7 · Cited by 99
Aβ40 Protects Non-toxic Aβ42 Monomer from Aggregation
Yan, Y., & Wang, C. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.04.014 · Cited by 99
Cellular Membrane Composition Defines Aβ-Lipid Interactions
Waschuk, S. A., Elton, E. A., Darabie, A. A., Fraser, P. E., & McLaurin, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103598200 · Cited by 98
α2-Macroglobulin in late-onset Alzheimer's disease
Kovacs, D. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00113-3 · Cited by 98
Intake of copper has no effect on cognition in patients with mild Alzheimer’s disease: a pilot phase 2 clinical trial
Kessler, H., Bayer, T. A., Bach, D., Schneider-Axmann, T., Supprian, T., Herrmann, W., Haber, M., Multhaup, G., Falkai, P., & Pajonk, F. (2008) · Journal of Neural Transmission · doi:10.1007/s00702-008-0080-1 · Cited by 98
The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
Matter, M. L., Zhang, Z., Nordstedt, C., & Ruoslahti, E. I. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.1019 · Cited by 97
Binding of copper (II) ion to an Alzheimer's tau peptide as revealed by MALDI‐TOF MS, CD, and NMR
Ma, Q., Li, Y., Du, J., Kanazawa, K., Nemoto, T., Nakanishi, H., & Zhao, Y. (2005) · Biopolymers · doi:10.1002/bip.20335 · Cited by 96
Mitochondrial ATP synthase activity is impaired by suppressed O-GlcNAcylation in Alzheimer's disease
Cha, M.-Y., Cho, H. J., Kim, C., Jung, Y. O., Kang, M. J., Murray, M. E., Hong, H. S., Choi, Y.-J., Choi, H., Kim, D. K., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv358 · Cited by 95
Self-citation
The Aluminium-Amyloid Cascade Hypothesis and Alzheimer’s Disease
Exley, C. (2005) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/0-387-23226-5_11 · Cited by 93
Amyloid-β-induced Synapse Damage Is Mediated via Cross-linkage of Cellular Prion Proteins
Bate, C., & Williams, A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.248724 · Cited by 93
Amyloid-β Peptide Binds to Cytochrome C Oxidase Subunit 1
Hernández-Zimbrón, L. F., Luna‐Muñoz, J., Mena, R., Vázquez‐Ramírez, R., Kubli‐Garfias, C., Cribbs, D. H., Manoutcharian, K., & Gevorkian, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0042344 · Cited by 93
Uptake and pathogenic effects of amyloid beta peptide 1–42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists
Bi, X., Gall, C. M., Zhou, J., & Lynch, G. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00132-x · Cited by 92
The Serpin-Enzyme Complex Receptor Recognizes Soluble, Nontoxic Amyloid-β Peptide but Not Aggregated, Cytotoxic Amyloid-β Peptide
Boland, K., Behrens, M. I., Choi, D. W., Manias, K., & Perlmutter, D. H. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.18032 · Cited by 91
Inhibitory Effect of Copper(II) on Zinc(II)-Induced Aggregation of Amyloid β-Peptide
Suzuki, K., Miura, T., & Takeuchi, H. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5263 · Cited by 90
VDAC1, Having a Shorter N-Terminus Than VDAC2 but Showing the Same Migration in an SDS−Polyacrylamide Gel, Is the Predominant Form Expressed in Mitochondria of Various Tissues
Yamamoto, T., Yamada, A., Watanabe, M., Yoshimura, Y., Yamazaki, N., Yoshimura, Y., Yamauchi, T., Kataoka, M., Nagata, T., Terada, H., et al. (2006) · Journal of Proteome Research · doi:10.1021/pr060291w · Cited by 90
Blocking the Interaction between Apolipoprotein E and Aβ Reduces Intraneuronal Accumulation of Aβ and Inhibits Synaptic Degeneration
Kuszczyk, M. A., Sanchez, S., Pankiewicz, J., Kim, J., Duszczyk, M., Guridi, M., Asuni, A. A., Sullivan, P. M., Holtzman, D. M., & Sadowski, M. J. (2013) · The American Journal of Pathology · doi:10.1016/j.ajpath.2013.01.034 · Cited by 89
Investigations with cultured human microglia on pathogenic mechanisms of Alzheimer's disease and other neurodegenerative diseases
Walker, D. G., & Lue, L.-F. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20484 · Cited by 89
Human Serum Transthyretin Levels Correlate Inversely with Alzheimer's Disease
Han, S.-H., Jung, E. S., Sohn, J.-H., Hong, H. J., Hong, H., Kim, J., Na, D. L., Kim, M., Kim, H. Y., Ha, H. J., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-102145 · Cited by 88
Self-citation
Measurement of Apolipoprotein E (apoE) in Cerebrospinal Fluid
Hesse, C., Larsson, H. E., Fredman, P., Minthon, L., Andreasen, N., Davidsson, P., & Blennow, K. (2000) · Neurochemical Research · doi:10.1023/a:1007516210548 · Cited by 87
RAGE-Abeta interactions in the pathophysiology of Alzheimer's disease.
Yan, S. S., Stern, D. M., Kane, M. D., Kuo, Y., Lampert, H. C., & Roher, A. E. (1998) · PubMed · Cited by 83
Inhibition of Alzheimer β-Peptide Fibril Formation by Serum Amyloid P Component
Janciauskiene, S. M., de Frutos, P. G., Carlemalm, E., Dahlbäck, B., & Eriksson, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.44.26041 · Cited by 82
Amyloidogenic determinant as a substrate recognition motif of insulin‐degrading enzyme
Kurochkin, I. V. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00422-0 · Cited by 79
Apolipoprotein E influences amyloid-beta clearance from the murine periphery
Hone, E., Martins, I., Fonte, J., & Martins, R. N. (2003) · Journal of Alzheimer's Disease · doi:10.3233/jad-2003-5101 · Cited by 78
Peripheral Amyloid-β Levels Regulate Amyloid-β Clearance from the Central Nervous System
Marques, M. A., Kulstad, J. J., Savard, C. E., Green, P. S., Lee, S. P., Craft, S., Watson, G. S., & Cook, D. G. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0964 · Cited by 77
Increased expressions of TLR2 and TLR4 on peripheral blood mononuclear cells from patients with Alzheimer's disease
Zhang, W., Wang, L., Yu, J., Zhao-fu, C., & Tan, L. (2011) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2011.11.032 · Cited by 77
Coaxing the LDL Receptor Family into the Fold
Herz, J., & Marschang, P. (2003) · Cell · doi:10.1016/s0092-8674(03)00073-4 · Cited by 74
The Biphasic Role of Microglia in Alzheimer's Disease
Mizuno, T. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/737846 · Cited by 73
Serum Zinc Levels and Alzheimer's Disease
Rulon, L. L., Robertson, J. D., Lovell, M. A., Deibel, M. A., Ehmann, W. D., & Markesbery, W. R. (2000) · Biological Trace Element Research · doi:10.1385/bter:75:1-3:79 · Cited by 71
The β‐amyloid protein of Alzheimer’s disease binds to membrane lipids but does not bind to the α7 nicotinic acetylcholine receptor
Small, D. H., Maksel, D., Kerr, M. L., Ng, J., Hou, X., Chu, C., Mehrani, H., Unabia, S., Azari, M. F., Loiacono, R., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04444.x · Cited by 69
Identification of beta-amyloid-binding sites on transthyretin
Du, J., Cho, P. Y., Yang, D. T., & Murphy, R. M. (2012) · Protein Engineering Design and Selection · doi:10.1093/protein/gzs026 · Cited by 69
The serpin-enzyme complex (SEC) receptor mediates the neutrophil chemotactic effect of alpha-1 antitrypsin-elastase complexes and amyloid-beta peptide.
Joslin, G., Griffin, G. L., August, A. M., Adams, S. P., Fallon, R. J., Senior, R. M., & Perlmutter, D. H. (1992) · Journal of Clinical Investigation · doi:10.1172/jci115934 · Cited by 68
Promiscuous Alzheimer's Amyloid: Yet Another Partner
Benilova, I., & De Strooper, B. (2013) · Science · doi:10.1126/science.1244166 · Cited by 67
Differential physiologic responses of α7 nicotinic acetylcholine receptors to β‐amyloid1–40 and β‐amyloid1–42
Lee, D. H. S., & Wang, H.-Y. (2003) · Journal of Neurobiology · doi:10.1002/neu.10203 · Cited by 67
Regulation of serine protease activity by aluminum: implications for Alzheimer disease.
Clauberg, M., & Joshi, J. G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.3.1009 · Cited by 67
Alzheimer's Peptide Aβ1–42 Binds to Two β-Sheets of α1-Antichymotrypsin and Transforms It from Inhibitor to Substrate
Janciauskiene, S. M., Rubin, H. N., Lukacs, C., & Wright, H. T. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28360 · Cited by 64
Promotion of formation of amyloid fibrils by aluminium adenosine triphosphate (AlATP)
Exley, C., & Korchazhkina, O. V. (2001) · Journal of Inorganic Biochemistry · doi:10.1016/s0162-0134(01)00171-4 · Cited by 63
Interaction of beta-amyloid peptides with integrins in a human nerve cell line
Sabo, S. L., Lambert, M. P., Kessey, K., Wade, W. S., Krafft, G. A., & Klein, W. L. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(94)11159-g · Cited by 62
LRP and Alzheimer's Disease
Zerbinatti, C., & Bu, G. (2005) · Reviews in the Neurosciences · doi:10.1515/revneuro.2005.16.2.123 · Cited by 62
Interaction of Transthyretin with Amyloid β‐Protein: Binding and Inhibition of Amyloid Formation
Schwarzman, A. L., & Goldgaber, D. (2007) · Novartis Foundation symposium · doi:10.1002/9780470514924.ch10 · Cited by 61
Amyloid beta antagonizes insulin promoted secretion of the amyloid beta protein precursor
Xie, L., Martins, R. N., Racchi, M., Craft, S., & Helmerhorst, E. (2002) · Journal of Alzheimer s Disease · doi:10.3233/jad-2002-4504 · Cited by 61
Probing copper/tau protein interactions electrochemically
Martic, S., Rains, M. K., & Kraatz, H.-B. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.07.015 · Cited by 60
β‐Amyloid activates presynaptic α7 nicotinic acetylcholine receptors reconstituted into a model nerve cell system: involvement of lipid rafts
Khan, G. M., Tong, M., Jhun, M., Arora, K., & Nichols, R. A. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07116.x · Cited by 59
Blocking the apoE/Aβ interaction ameliorates Aβ-related pathology in APOE ε2 and ε4 targeted replacement Alzheimer model mice
Pankiewicz, J. E., Guridi, M., Kim, J., Asuni, A. A., Sanchez, S., Sullivan, P. M., Holtzman, D. M., & Sadowski, M. J. (2014) · Acta Neuropathologica Communications · doi:10.1186/s40478-014-0075-0 · Cited by 57
α2-Macroglobulin-Mediated Degradation of Amyloid β1–42: A Mechanism to Enhance Amyloid β Catabolism
Lauer, D., Reichenbach, A., & Birkenmeier, G. (2001) · Experimental Neurology · doi:10.1006/exnr.2000.7569 · Cited by 57
Subcellular localization of the low density lipoprotein receptor-related protein (α2-macroglobulin receptor) in human brain
Tooyama, I., Kawamata, T., Akiyama, H., Kimura, H., Moestrup, S. K., Gliemann, J., Matsuo, A., & McGeer, P. L. (1995) · Brain Research · doi:10.1016/0006-8993(95)00735-9 · Cited by 56
C4b-binding protein in Alzheimer's disease: Binding to Aβ1–42 and to dead cells
Trouw, L. A., Nielsen, H. M., Minthon, L., Londos, E., Landberg, G., Veerhuis, R., Janciauskiene, S. M., & Blom, A. M. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.04.025 · Cited by 54
Aluminum Increases Levels of beta-Amyloid and Ubiquitin in Neuroblastoma But Not in Glioma Cells
Campbell, A., Kumar, A., Rosa, F. G. L., Prasad, K. N., & Bondy, S. C. (2000) · Proceedings of The Society for Experimental Biology and Medicine · doi:10.1046/j.1525-1373.2000.22356.x · Cited by 53
Therapeutic Albumin Binding to Remove Amyloid-β
Costa, M., Ortiz, A. M., & Jorquera, J. I. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-111139 · Cited by 52
Behavioral stress causes mitochondrial dysfunction via ABAD up-regulation and aggravates plaque pathology in the brain of a mouse model of Alzheimer disease
Seo, J., Lee, K.-W., Kim, T., Baek, I., Im, J., & Han, P. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.02.035 · Cited by 51
Effects of apolipoprotein E (apoE) isoforms, β-amyloid (Aβ) and apoE/Aβ complexes on Protein Kinase C-α (PKC-α) translocation and amyloid precursor protein (APP) processing in human SH-SY5Y neuroblastoma cells and fibroblasts
Cedazo-Mı́nguez, A., Wiehager, B., Winblad, B., Hüttinger, M., & Cowburn, R. F. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(00)00128-5 · Cited by 50
The role of cytochrome c oxidase deficiency in ROS and amyloid plaque formation
Pickrell, A. M., Fukui, H., & Moraes, C. T. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9245-3 · Cited by 47
Specificity in Recognition of Amyloid-β Peptide by the Serpin-Enzyme Complex Receptor in Hepatoma Cells and Neuronal Cells
Boland, K. A., Manias, K., & Perlmutter, D. H. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.28022 · Cited by 47
Serum levels of albumin‐amyloid beta complexes are decreased in Alzheimer's disease
Yamamoto, K., Shimada, H., Koh, H., Ataka, S., & Miki, T. (2013) · Geriatrics and gerontology international/Geriatrics & gerontology international · doi:10.1111/ggi.12147 · Cited by 46
Interaction of Amyloid Inhibitor Proteins with Amyloid Beta Peptides: Insight from Molecular Dynamics Simulations
Das, P., Kang, S.-G., Temple, S., & Belfort, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113041 · Cited by 46
Amyloid P component and other acute-phase proteins associated with cerebellar Aβ-deposits in Alzheimer's disease
Kalaria, R. N., & Perry, G. L. (1993) · Brain Research · doi:10.1016/0006-8993(93)91202-4 · Cited by 46
Genetic Alterations of the BRI2 gene: Familial British and Danish Dementias
J, G., A, R., Y, T., T, L., M, B.-M., H, B., G, P., J, H., R, L., T, R., et al. (2006) · Brain Pathology · doi:10.1111/j.1750-3639.2006.tb00563.x · Cited by 44
Amyloid β‐peptide activates nuclear factor‐κB through an N‐methyl‐D‐aspartate signaling pathway in cultured cerebellar cells
Kawamoto, E. M., Lepsch, L. B., Cury‐Boaventura, M. F., Munhoz, C. D., Lima, L. S., Yshii, L., Avellar, M. C. W., Curi, R., Mattson, M. P., & Scavone, C. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21548 · Cited by 43
Assessing Candidate Serum Biomarkers for Alzheimer's Disease: A Longitudinal Study
Zabel, M. K., Schrag, M., Mueller, C., Zhou, W., Crofton, A. R., Petersen, F. F., Dickson, A., & Kirsch, W. M. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-112012 · Cited by 41
A phase 2 randomized, controlled trial of the α7 agonist ABT‐126 in mild‐to‐moderate Alzheimer's dementia
Gault, L. M., Ritchie, C. W., Robieson, W., Pritchett, Y., Othman, A. A., & Lenz, R. A. (2015) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2015.06.001 · Cited by 41
Signaling of the neurotrophin receptor p75 in relation to Alzheimer’s disease
Diarra, A., Geetha, T., Potter, P., & Babu, J. R. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.09.116 · Cited by 39
Transthyretin Accelerates Vascular Aβ Deposition in a Mouse Model of Alzheimer's Disease
Wati, H., Kawarabayashi, T., Matsubara, E., Kasai, A., Hirasawa, T., Kubota, T., Harigaya, Y., Shoji, M., & Maeda, S. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00166.x · Cited by 36
The Functions of the Amyloid Precursor Protein Gene
Panegyres, P. K. (2001) · Reviews in the Neurosciences · doi:10.1515/revneuro.2001.12.1.1 · Cited by 36
Lack of α-synuclein increases amyloid plaque accumulation in a transgenic mouse model of Alzheimer's disease
Kallhoff, V., Peethumnongsin, E., & Zheng, H. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-6 · Cited by 33
The Inhibition of Trypsin and α-Chymotrypsin Proteolytic Activity by Aluminum(III)
Zatta, P. F., Bordin, C., & Favarato, M. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1302 · Cited by 32
Defining pre‐synaptic nicotinic receptors regulated by beta amyloid in mouse cortex and hippocampus with receptor null mutants
Mehta, T. K., Dougherty, J. J., Wu, J., Choi, C. H., Khan, G. M., & Nichols, R. A. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06070.x · Cited by 30
Aβ Inhibition of Ionic Conductance in Mouse Basal Forebrain Neurons Is Dependent upon the Cellular Prion Protein PrPC
Alier, K. A., Ma, L., Yang, J., Westaway, D. A., & Jhamandas, J. H. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4367-11.2011 · Cited by 30
Both Targeted Mass Spectrometry and Flow Sorting Analysis Methods Detected the Decreased Serum Apolipoprotein E Level in Alzheimer's Disease Patients
Han, S.-H., Kim, J. S., Lee, Y., Choi, H., Kim, J.-W., Na, D. L., Yang, E. G., Yu, M.-H., Hwang, D., Lee, C., et al. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.028639 · Cited by 29
Self-citation
Intracellular Trafficking of the Amyloid β-Protein Precursor (APP) Regulated by Novel Function of X11-Like
Saito, Y., Akiyama, M., Araki, Y., Sumioka, A., Shiono, M., Taru, H., Nakaya, T., Yamamoto, T., & Suzuki, T. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022108 · Cited by 29
Advanced Glycation Endproducts Induce Changes in Glucose Consumption, Lactate Production, and ATP Levels in SH-SY5Y Neuroblastoma Cells by a Redox-Sensitive Mechanism
de Arriba, S. G., Loske, C., Meiners, I., Fleischer, G., Lobisch, M., Wessel, K., Tritschler, H., Schinzel, R., & Münch, G. W. (2003) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000090622.86921.0e · Cited by 28
Serum Amyloid P Component Accelerates the Formation and Enhances the Stability of Amyloid Fibrils in a Physiologically Significant Under-Saturated Solution of Amyloid-β42
Mold, M., Shrive, A. K., & Exley, C. (2012) · Journal of Alzheimer's Disease · doi:10.3233/jad-2012-120076 · Cited by 26
New Hope from an Old Drug: Fighting Alzheimer's Disease with the Cancer Drug Bexarotene (Targretin)?
Aicardi, G. (2013) · Rejuvenation Research · doi:10.1089/rej.2013.1497 · Cited by 24
Amyloid-β1–40 Inhibits Amyloid-β1–42 Induced Activation of Cytoplasmic Phospholipase A2 and Synapse Degeneration
Bate, C., & Williams, A. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100528 · Cited by 23
Aluminum-sensitive degradation of amyloid β-protein1–40 by murine and human intracellular enzymes
Banks, W. A. (1996) · Neurotoxicology and Teratology · doi:10.1016/s0892-0362(96)00084-0 · Cited by 23
High density lipoproteins bind Aβ and apolipoprotein C-II amyloid fibrils
Wilson, L. M., Pham, C. L. L., Jenkins, A. J., Wade, J. D., Hill, A. F., Perugini, M. A., & Howlett, G. J. (2006) · Journal of Lipid Research · doi:10.1194/jlr.c500022-jlr200 · Cited by 17
The Plasma Membrane: A Target and Hurdle for the Development of Anti- A? Drugs?
Talaga, B. S. P. P., & Quere, B. S. P. L. (2002) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1568007023338897 · Cited by 16
Application of fluoroimmunoassay to cerebrospinal fluid immunoglobulin G and albumin
Stevens, R. W., Elmendorf, D., Gourlay, M., Stroebel, E., & Gaafar, H. A. (1979) · Journal of Clinical Microbiology · doi:10.1128/jcm.10.3.346-350.1979 · Cited by 14
The degradation of Aβ25–35 by the serine protease plasmin is inhibited by aluminium
Korchazhkina, O. V., Ashcroft, A. E., Kiss, T., & Exley, C. (2002) · Journal of Alzheimer s Disease · doi:10.3233/jad-2002-4503 · Cited by 13
Protective Effects of Bexarotene against Amyloid-β25-35-Induced Dysfunction in Hippocampal Neurons through the Insulin Signaling Pathway
Dai, W., Yang, J., Chen, T., & Yang, Z. R. (2014) · Neurodegenerative Diseases · doi:10.1159/000358397 · Cited by 11
Untitled work
(1992) · PubMed Central
Untitled work
Webster (1996) · doi:10.1002/(sici)1097-4547(19961001)46:1
Untitled work
Yamauchi (2000) · doi:10.1002/1097-4547(20001115)62:4
Untitled work
Cole (2000) · doi:10.1002/1097-0029(20000815)50:4

Sorted by citations

Extracellular protein components of amyloid plaques and their roles in Alzheimer’s disease pathology
Rahman, M. M., & Lendel, C. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00465-0 · Cited by 260
Peripheral inflammatory biomarkers in Alzheimer’s disease: a brief review
Park, J., Han, S.-H., & Mook‐Jung, I. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.1.309 · Cited by 206
Self-citation
Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease
Liao, F., Yoon, H., & Kim, J. (2017) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000383 · Cited by 191
Plasma tau/amyloid-β1–42 ratio predicts brain tau deposition and neurodegeneration in Alzheimer’s disease
Park, J., Han, S.-H., Yi, D., Byun, M. S., Lee, J. H., Jang, S. S., Ko, K., Jeon, S. Y., Lee, Y., Kim, Y. K., et al. (2018) · Brain · doi:10.1093/brain/awy347 · Cited by 181
Self-citation
Neuroprotective effect of berberine against environmental heavy metals-induced neurotoxicity and Alzheimer's-like disease in rats
Hussien, H. M., Abd-Elmegied, A., Ghareeb, D. A., Hafez, H. S., Ahmed, H. E. A., & Moneam, N. M. A. E. (2017) · Food and Chemical Toxicology · doi:10.1016/j.fct.2017.11.025 · Cited by 176

See all 67

Authors: Han, S.-H., Park, J.-C., & Mook-Jung, I.
Affiliations: Seoul National University (KR)
ORCID: Park, Jong-Chan
Venue: Progress in Neurobiology
Publisher: Elsevier BV
Published: 2016-02
Volume: 137
Pages: 17-38
ISSN: 0301-0082 (ISSN-L)
DOI: 10.1016/j.pneurobio.2015.12.004
OpenAlex: W2207689373
Cited by: 67
References: 355
Citations by year: 2026: 1 · 2025: 3 · 2024: 4 · 2023: 4 · 2022: 4 · 2021: 11 · 2020: 5 · 2019: 10 · 2018: 9 · 2017: 12 · 2016: 4
FWCI: 1.02
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Progress in Neurobiology (publishedVersion)
PubMed (publishedVersion)
Funders: NRF (2015R1A2A1A05001794, 2014M3C7A1046047, 2015M3C7A1028790, 2015R1C1A2A01053545)
MRC (2012R1A5A2A44671346)
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: Alzheimer's disease, amyloid-beta, protein-protein interaction, amyloid fibril formation, AD pathogenesis, therapeutic target
MeSH terms: Alzheimer Disease, Animals, Blood Proteins, Brain, Humans, Metals, Prions, Receptors, Cell Surface, Amyloid beta-Peptides, LDL-Receptor Related Proteins, Apolipoprotein E4

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

Amyloid β-interacting partners in Alzheimer's disease: From accomplices to possible therapeutic targets

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks