Mechanism of Neuronal versus Endothelial Cell Uptake of Alzheimer's Disease Amyloid β Protein

In Vivo Protein Transduction: Delivery of a Biologically Active Protein into the Mouse

Schwarze, S. R., Ho, A. L., Vocero-Akbani, A. M., & Dowdy, S. F. (1999) · Science · doi:10.1126/science.285.5433.1569 · Cited by 2,418 · see citing works

Receptor-mediated endocytosis of transferrin and recycling of the transferrin receptor in rat reticulocytes

Harding, C., Heuser, J., & Stahl, P. (1983) · The Journal of Cell Biology · doi:10.1083/jcb.97.2.329 · Cited by 1,775 · see citing works

RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain

Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426 · see citing works

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 · see citing works

Neurovascular mechanisms of Alzheimer's neurodegeneration

Zloković, B. V. (2005) · Trends in Neurosciences · doi:10.1016/j.tins.2005.02.001 · Cited by 921 · see citing works

Filipin-sensitive caveolae-mediated transport in endothelium: reduced transcytosis, scavenger endocytosis, and capillary permeability of select macromolecules.

Schnitzer, J. E., Oh, P., Pinney, E., & Allard, J. F. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.5.1217 · Cited by 918 · see citing works

LRP/Amyloid β-Peptide Interaction Mediates Differential Brain Efflux of Aβ Isoforms

Deane, R., Wu, Z., Sagare, A., Davis, J., Du Yan, S., Hamm, K., Xu, F., Parisi, M., LaRue, B., Hu, H. W., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.017 · Cited by 828 · see citing works

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 · see citing works

Alzheimer disease and cerebrovascular pathology: an update

Jellinger, K. A. (2002) · Journal of Neural Transmission · doi:10.1007/s007020200068 · Cited by 680 · see citing works

Analysis of Heterogeneous βA4 Peptides in Human Cerebrospinal Fluid and Blood by a Newly Developed Sensitive Western Blot Assay

Ida, N., Hartmann, T., Pantel, J., Schrüder, J., Zerfaß, R., Fürstl, H., Sandbrink, R., Masters, C. L., & Beyreuther, K. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22908 · Cited by 476 · see citing works

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 456 · see citing works

Depletion of intracellular potassium arrests coated pit formation and receptor-mediated endocytosis in fibroblasts

Larkin, J. M., Brown, M. S., Goldstein, J. L., & Anderson, R. G. W. (1983) · Cell · doi:10.1016/0092-8674(83)90356-2 · Cited by 435 · see citing works

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 · see citing works

Early-onset and Robust Cerebral Microvascular Accumulation of Amyloid β-Protein in Transgenic Mice Expressing Low Levels of a Vasculotropic Dutch/Iowa Mutant Form of Amyloid β-Protein Precursor

Davis, J., Xu, F., Deane, R., Romanov, G., Previti, M. L., Zeigler, K., Zlokovic, B. V., & Van Nostrand, W. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312946200 · Cited by 373 · see citing works

Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation

Chui, D.-H., Tanahashi, H., Ozawa, K., Ikeda, S., Checler, F., Ueda, O., Suzuki, H., Araki, W., Inoue, H., Shirotani, K., et al. (1999) · Nature Medicine · doi:10.1038/8438 · Cited by 364 · see citing works

Aβ localization in abnormal endosomes: association with earliest Aβ elevations in AD and Down syndrome

Cataldo, A. M., Petanceska, S., Terio, N. B., Peterhoff, C. M., Durham, R., Mercken, M., Mehta, P. D., Buxbaum, J., Haroutunian, V., & Nixon, R. A. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.027 · Cited by 363 · see citing works

Aβ40 Inhibits Amyloid Deposition<i>In Vivo</i>

Kim, J., Onstead, L., Randle, S., Price, R., Smithson, L., Zwizinski, C., Dickson, D. W., Golde, T., & McGowan, E. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4849-06.2007 · Cited by 359 · see citing works

Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer’s disease

Crowther, D. C., Kinghorn, K. J., Miranda, E., Page, R., Curry, J. A., Duthie, F., Gubb, D., & Lomas, D. A. (2005) · Neuroscience · doi:10.1016/j.neuroscience.2004.12.025 · Cited by 351 · see citing works

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 349 · see citing works

Par-4 is a mediator of neuronal degeneration associated with the pathogenesis of Alzheimer disease

Guo, Q., Fu, W., Xie, J., Luo, H., Sells, S. F., Geddes, J. W., Bondada, V., Rangnekar, V. M., & Mattson, M. P. (1998) · Nature Medicine · doi:10.1038/nm0898-957 · Cited by 264 · see citing works

Acute stress increases interstitial fluid amyloid-β via corticotropin-releasing factor and neuronal activity

Kang, J.-E., Cirrito, J. R., Dong, H., Csernansky, J. G., & Holtzman, D. M. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0700148104 · Cited by 219 · see citing works

Diffusion of Epidermal Growth Factor in Rat Brain Extracellular Space Measured by Integrative Optical Imaging

Thorne, R. G., Hrabětová, S., & Nicholson, C. (2004) · Journal of Neurophysiology · doi:10.1152/jn.00352.2004 · Cited by 168 · see citing works

Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Abeta stabilization.

LaFerla, F. M., Troncoso, J. C., Strickland, D. K., Kawas, C. H., & Jay, G. D. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119536 · Cited by 162 · see citing works

Pathogenesis of cerebral amyloid angiopathy

Rensink, A. A. M., de Waal, R. M. W., Kremer, B. P. H., & Verbeek, M. M. (2003) · Brain Research Reviews · doi:10.1016/j.brainresrev.2003.08.001 · Cited by 159 · see citing works

Distribution and Fluidizing Action of Soluble and Aggregated Amyloid β-Peptide in Rat Synaptic Plasma Membranes

Mason, R. P., Jacob, R. F., Walter, M. F., Mason, P. E., Avdulov, N. A., Chochina, S. V., Igbavboa, U., & Wood, W. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.26.18801 · Cited by 123 · see citing works

Topographical distribution of cerebral amyloid angiopathy and its effect on cognitive decline are influenced by Alzheimer disease pathology

Attems, J., Quass, M., Jellinger, K. A., & Lintner, F. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.01.013 · Cited by 119 · see citing works

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 · see citing works

Preferential adsorption, internalization and resistance to degradation of the major isoform of the Alzheimer's amyloid peptide, Aβ1–42, in differentiated PC12 cells

Burdick, D., Kosmoski, J. V., Knauer, M. F., & Glabe, C. G. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01262-0 · Cited by 112 · see citing works

Permeability of proteins at the blood-brain barrier in the normal adult mouse and double transgenic mouse model of Alzheimer's disease.

Poduslo, J., Curran, G., Wengenack, T. M., Malester, B., & Duff, K. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0402 · Cited by 111 · see citing works

Determination of diffusion and partition coefficients of propofol in rat brain tissue: implications for studies of drug action in vitro

Gredell, J. A., Turnquist, P. A., MacIver, M. B., & Pearce, R. A. (2004) · British Journal of Anaesthesia · doi:10.1093/bja/aeh272 · Cited by 106 · see citing works

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 · see citing works

Aβ42-positive non-pyramidal neurons around amyloid plaques in Alzheimer's disease

Mochizuki, A., Tamaoka, A., Shimohata, A., Komatsuzaki, Y., & Shoji, S. (2000) · The Lancet · doi:10.1016/s0140-6736(99)04937-5 · Cited by 85 · see citing works

Metabolism of Alzheimer beta-amyloid precursor protein: regulation by protein kinase A in intact cells and in a cell-free system.

Xu, H., Sweeney, D. A., Greengard, P., & Gandy, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.9.4081 · Cited by 84 · see citing works

Translocation of Human Calcitonin in Respiratory Nasal Epithelium Is Associated with Self-Assembly in Lipid Membrane

Schmidt, M. C., Rothen‐Rutishauser, B., Rist, B., Beck‐Sickinger, A. G., Wunderli‐Allenspach, H., Rubas, W., Sadée, W., & Merkle, H. P. (1998) · Biochemistry · doi:10.1021/bi981219h · Cited by 79 · see citing works

The brain slice preparation: a tribute to the pioneer Henry McIlwain

Collingridge, G. L. (1995) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(94)00187-l · Cited by 75 · see citing works

Membrane-disordering effects of β-amyloid peptides

Müller, W. E. G., Kirsch, C., & Eckert, G. P. (2001) · Biochemical Society Transactions · doi:10.1042/bst0290617 · Cited by 69 · see citing works

Interaction between amyloid β‐protein aggregates and membranes

Kakio, A., Yano, Y., Takai, D., Kuroda, Y., Matsumoto, O., Kozutsumi, Y., & Matsuzaki, K. (2004) · Journal of Peptide Science · doi:10.1002/psc.570 · Cited by 68 · see citing works

The Effect of Cholesterol and Monosialoganglioside (GM1) on the Release and Aggregation of Amyloid β-Peptide from Liposomes Prepared from Brain Membrane-like Lipids

Tashima, Y., Oe, R., Lee, S., Sugihara, G., Chambers, E. J., Takahashi, M., & Yamada, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308622200 · Cited by 52 · see citing works

Reduced Membrane Lipids in the Cortex of Alzheimer’s Disease Transgenic Mice

Yao, J. K., Wengenack, T. M., Curran, G. L., & Poduslo, J. F. (2008) · Neurochemical Research · doi:10.1007/s11064-008-9673-1 · Cited by 48 · see citing works

What is the dominant aβ species in human brain tissue? A review

Gregory, G. C., & Halliday, G. M. (2005) · Neurotoxicity Research · doi:10.1007/bf03033774 · Cited by 40 · see citing works

Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding

Bateman, D. A., McLaurin, J., & Chakrabartty, A. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-29 · Cited by 36 · see citing works

Study of β-Amyloid Peptide (Aβ40) Insertion into Phospholipid Membranes Using Monolayer Technique

Ji, S., Wu, Y., & Sui, S. (2002) · Biochemistry (Moscow) · doi:10.1023/a:1021361607611 · Cited by 27 · see citing works

Cerebral amyloid angiopathy: Both viper and maggot in the brain

Weller, R. O., & Nicoll, J. A. R. (2005) · Annals of Neurology · doi:10.1002/ana.20622 · Cited by 25 · see citing works

Relative paucity of tau accumulation in the small areas with abundant Aβ42-positive capillary amyloid angiopathy within a given cortical region in the brain of patients with Alzheimer pathology

Oshima, K., Akiyama, H., Tsuchiya, K., Kondo, H., Haga, C., Shimomura, Y., Iseki, E., Uchikado, H., Kato, M., Niizato, K., et al. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0070-z · Cited by 22 · see citing works

Effect of Forskolin on Synaptotagmin IV Protein Trafficking in PC12 Cells

Fukuda, M. (2004) · The Journal of Biochemistry · doi:10.1093/jb/mvh116 · Cited by 16 · see citing works

Differential accumulation of soluble amyloid β peptides 1-40 and 1-42 in human monocytic and neuroblastoma cell lines

Morelli, L., Prat, M. I., & Castaño, E. M. (1999) · Cell and Tissue Research · doi:10.1007/s004419900109 · Cited by 11 · see citing works

Physiological and Biophysical Factors That Influence Alzheimer’s Disease Amyloid Plaque Targeting of Native and Putrescine Modified Human Amyloid β40

Kandimalla, K. K., Curran, G. L., Holasek, S. S., Gilles, E. J., Wengenack, T. M., Ramı́rez-Alvarado, M., & Poduslo, J. F. (2006) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.095711 · Cited by 10 · see citing works

Blood-brain barrier-associated pericytes internalize and clear aggregated amyloid-β42 by LRP1-dependent apolipoprotein E isoform-specific mechanism

Ma, Q., Zhao, Z., Sagare, A. P., Wu, Y., Wang, M., Owens, N. C., Verghese, P. B., Herz, J., Holtzman, D. M., & Zlokovic, B. V. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0286-0 · Cited by 281 · see citing works

Disruption of Arterial Perivascular Drainage of Amyloid-β from the Brains of Mice Expressing the Human APOE ε4 Allele

Hawkes, C. A., Sullivan, P. M., Hands, S. L., Weller, R. O., Nicoll, J. A. R., & Carare, R. O. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041636 · Cited by 177 · see citing works

Astrocytic Aβ1‐42 uptake is determined by Aβ‐aggregation state and the presence of amyloid‐associated proteins

Nielsen, H. M., Mulder, S. D., Beliën, J. A. M., Musters, R. J. P., Eikelenboom, P., & Veerhuis, R. (2010) · Glia · doi:10.1002/glia.21004 · Cited by 164 · see citing works

Synaptotoxicity of Alzheimer Beta Amyloid Can Be Explained by Its Membrane Perforating Property

Sepúlveda, F. J., Parodí, J., Peoples, R. W., Opazo, C., & Aguayo, L. G. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011820 · Cited by 155 · see citing works

The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration

Costanzo, M., & Zurzolo, C. (2013) · Biochemical Journal · doi:10.1042/bj20121898 · Cited by 151 · see citing works

Differences in amyloid-β clearance across mouse and human blood–brain barrier models: Kinetic analysis and mechanistic modeling

Qosa, H., Abuasal, B. S., Romero, I. A., Weksler, B., Couraud, P.-O., Keller, J. N., & Kaddoumi, A. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.01.023 · Cited by 146 · see citing works

Biochemically-defined pools of amyloid-β in sporadic Alzheimer’s disease: correlation with amyloid PET

Roberts, B. R., Lind, M., Wagen, A. Z., Rembach, A., Frugier, T., Li, Q.-X., Ryan, T. M., McLean, C. A., Doecke, J. D., Rowe, C. C., et al. (2017) · Brain · doi:10.1093/brain/awx057 · Cited by 143 · see citing works

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 145 · see citing works

Mechanisms of Amyloid‐Beta Peptide Uptake by Neurons: The Role of Lipid Rafts and Lipid Raft‐Associated Proteins

Lai, A. Y., & McLaurin, J. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/548380 · Cited by 130 · see citing works

Amyloid-β Acts as a Regulator of Neurotransmitter Release Disrupting the Interaction between Synaptophysin and VAMP2

Russell, C. L., Semerdjieva, S., Empson, R. M., Austen, B., Beesley, P. W., & Alifragis, P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043201 · Cited by 115 · see citing works

Endocytic uptake of monomeric amyloid-β peptides is clathrin- and dynamin-independent and results in selective accumulation of Aβ(1–42) compared to Aβ(1–40)

Wesén, E. V., Jeffries, G. D. M., Dzebo, M. M., & Esbjörner, E. K. (2017) · Scientific Reports · doi:10.1038/s41598-017-02227-9 · Cited by 114 · see citing works

Endothelial Mitochondrial Dysfunction in Cerebral Amyloid Angiopathy and Alzheimer’s Disease

Parodi‐Rullán, R. M., Sone, J. Y., & Fossati, S. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190357 · Cited by 108 · see citing works

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 · see citing works

Real-Time Imaging and Quantification of Amyloid-β Peptide Aggregates by Novel Quantum-Dot Nanoprobes

Tokuraku, K., Marquardt, M., & Ikezu, T. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008492 · Cited by 75 · see citing works

Amyloid beta protein-induced zinc sequestration leads to synaptic loss via dysregulation of the ProSAP2/Shank3 scaffold

Grabrucker, A. M., Schmeißer, M. J., Udvardi, P. T., Arons, M. H., Schoen, M., Woodling, N. S., Andreasson, K. I., Hof, P. R., Buxbaum, J. D., Garner, C. C., et al. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-65 · Cited by 77 · see citing works

Towards Understanding the Roles of Heparan Sulfate Proteoglycans in Alzheimer’s Disease

Zhang, G.-L., Zhang, X., Wang, X., & Li, J. (2014) · BioMed Research International · doi:10.1155/2014/516028 · Cited by 76 · see citing works

A yeast model for amyloid-β aggregation exemplifies the role of membrane trafficking and PICALM in cytotoxicity

D’Angelo, F., Vignaud, H., Martino, J. S. D., Salin, B., Devin, A., Cullin, C., & Marchal, C. (2012) · Disease Models & Mechanisms · doi:10.1242/dmm.010108 · Cited by 75 · see citing works

Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease

Viles, J. H. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202215785 · Cited by 72 · see citing works

Lutein protects against β-amyloid peptide-induced oxidative stress in cerebrovascular endothelial cells through modulation of Nrf-2 and NF-κb

Liu, T., Liu, W., Zhao, J., Meng, F., & Wang, H. (2016) · Cell Biology and Toxicology · doi:10.1007/s10565-016-9360-y · Cited by 70 · see citing works

Differences in the Cellular Uptake and Intracellular Itineraries of Amyloid Beta Proteins 40 and 42: Ramifications for the Alzheimer’s Drug Discovery

Omtri, R. S., Davidson, M. W., Arumugam, B., Poduslo, J. F., & Kandimalla, K. K. (2012) · Molecular Pharmaceutics · doi:10.1021/mp200530q · Cited by 68 · see citing works

Endocytic pathways mediating oligomeric Aβ42 neurotoxicity

Yu, C., Nwabuisi‐Heath, E., Laxton, K., & LaDu, M. J. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-19 · Cited by 61 · see citing works

3D-visualization of amyloid-β oligomer interactions with lipid membranes by cryo-electron tomography

Tian, Y., Liang, R., Kumar, A., Szwedziak, P., & Viles, J. H. (2021) · Chemical Science · doi:10.1039/d0sc06426b · Cited by 59 · see citing works

Coenzyme Q10 Protects Human Endothelial Cells from β-Amyloid Uptake and Oxidative Stress-Induced Injury

Durán‐Prado, M., Frontiñán-Rubio, J., Santiago‐Mora, R., Peinado, J. R., Parrado‐Fernández, C., Gómez, M. V., Moreno, M. C. R., Lopez-Dominguez, J. A., Villalba, J. M., & Alcain, F. J. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109223 · Cited by 57 · see citing works

ApoHRP-based assay to measure intracellular regulatory heme

Atamna, H., Brahmbhatt, M., Atamna, W., Shanower, G., & Dhahbi, J. M. (2014) · Metallomics · doi:10.1039/c4mt00246f · Cited by 56 · see citing works

Synapses, synaptic activity and intraneuronal Aβ in Alzheimer’s disease

Tampellini, D. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00013 · Cited by 54 · see citing works

Pharmacological inhibition and knockdown of O‐GlcNAcase reduces cellular internalization of α‐synuclein preformed fibrils

Tavassoly, O., Yue, J., & Vocadlo, D. J. (2020) · FEBS Journal · doi:10.1111/febs.15349 · Cited by 52 · see citing works

The uptake of tau amyloid fibrils is facilitated by the cellular prion protein and hampers prion propagation in cultured cells

Cecco, E. D., Celauro, L., Vanni, S., Grandolfo, M., Bistaffa, E., Moda, F., Aguzzi, A., & Legname, G. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15040 · Cited by 51 · see citing works

Differential effect of amyloid beta peptides on mitochondrial axonal trafficking depends on their state of aggregation and binding to the plasma membrane

Zhang, L., Trushin, S., Christensen, T. A., Tripathi, U., Hong, C. C., Geroux, R. E., Howell, K. G., Poduslo, J. F., & Trushina, E. V. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.02.003 · Cited by 47 · see citing works

MEGF10 functions as a receptor for the uptake of amyloid‐β

Singh, T. D., Park, S., Bae, J., Yun, Y., Bae, Y. C., Park, R., & Kim, I.-S. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.08.050 · Cited by 47 · see citing works

Development of a Novel DNA Aptamer Ligand Targeting to Primary Cultured Tumor Endothelial Cells by a Cell-Based SELEX Method

Ara, M. N., Hyodo, M., Ohga, N., Hida, K., & Harashima, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0050174 · Cited by 43 · see citing works

An apolipoprotein E4 fragment can promote intracellular accumulation of amyloid peptide beta 42

Dafnis, I., Stratikos, E., Tzinia, A., Tsilibary, E. C., Zannis, V. I., & Chroni, A. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06756.x · Cited by 41 · see citing works

Binding studies of truncated variants of the Aβ peptide to the V-domain of the RAGE receptor reveal Aβ residues responsible for binding

Gospodarska, E., Kupniewska-Kozak, A., Goch, G., & Dadlez, M. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.02.011 · Cited by 41 · see citing works

Distinct Internalization Pathways of Human Amylin Monomers and Its Cytotoxic Oligomers in Pancreatic Cells

Trikha, S., & Jeremic, A. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073080 · Cited by 34 · see citing works

Role of membrane biophysics in Alzheimer's–related cell pathways

Zhu, D., Bungart, B. L., Yang, X., Zhumadilov, Z. S., Lee, J. C., & Askarova, S. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00186 · Cited by 32 · see citing works

The Precapillary Segment of the Blood-Brain Barrier and Its Relation to Perivascular Drainage in Alzheimer's Disease and Small Vessel Disease.

Thal, D. R. (2009) · The Scientific World JOURNAL · doi:10.1100/tsw.2009.72 · Cited by 32 · see citing works

TOM1 Regulates Neuronal Accumulation of Amyloid-β Oligomers by FcγRIIb2 Variant in Alzheimer's Disease

Gwon, Y., Kam, T., Kim, S.-H., Song, S., Park, H., Lim, B., Lee, H., Lee, W., Jo, D., & Jung, Y. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1996-17.2018 · Cited by 32 · see citing works

Circadian control of heparan sulfate levels times phagocytosis of amyloid beta aggregates

Clark, G. T., Yu, Y., Urban, C. A., Fu, G., Wang, C., Zhang, F., Linhardt, R. J., & Hurley, J. M. (2022) · PLOS Genetics · doi:10.1371/journal.pgen.1009994 · Cited by 31 · see citing works

Traffic Jam at the Blood–Brain Barrier Promotes Greater Accumulation of Alzheimer’s Disease Amyloid-β Proteins in the Cerebral Vasculature

Agyare, E. K., Leonard, S. R., Curran, G. L., Yu, C. C., Lowe, V. J., Paravastu, A. K., Poduslo, J. F., & Kandimalla, K. K. (2012) · Molecular Pharmaceutics · doi:10.1021/mp300352c · Cited by 27 · see citing works

Novel mechanism regulating endothelial permeability via T-cadherin-dependent VE-cadherin phosphorylation and clathrin-mediated endocytosis

Semina, E. V., Rubina, K. A., Sysoeva, V., Rutkevich, P. N., Kashirina, N. M., & Va, T. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1867-4 · Cited by 25 · see citing works

Sequence-dependent Internalization of Aggregating Peptides

Couceiro, J. R., Gallardo, R. U., Smet, F. D., Baets, G. D., Baatsen, P., Annaert, W. G., Roose, K., Saelens, X., Schymkowitz, J. W. H., & Rousseau, F. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.586636 · Cited by 25 · see citing works

HH Domain of Alzheimer’s Disease Aβ Provides Structural Basis for Neuronal Binding in PC12 and Mouse Cortical/Hippocampal Neurons

Poduslo, J. F., Gilles, E. J., Ramakrishnan, M., Howell, K. G., Wengenack, T. M., Curran, G. L., & Kandimalla, K. K. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008813 · Cited by 23 · see citing works

Imaging the Dynamics of Endocytosis in Live Mammalian TissuesPreprint

Weigert, R. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a017012 · Cited by 20 · see citing works

LRP-1 polymorphism is associated with global and regional amyloid load in Alzheimer's disease in humans in-vivo

Grimmer, T., Goldhardt, O., Guo, L., Yousefi, B. H., Förster, S., Drzezga, A. E., Sorg, C., Alexopoulos, P., Förstl, H., Kurz, A., et al. (2014) · NeuroImage Clinical · doi:10.1016/j.nicl.2014.01.016 · Cited by 22 · see citing works

Endocytic pathways of pathogenic protein aggregates in neurodegenerative diseases

Hivare, P., Mujmer, K., Swarup, G., Gupta, S. K., & Bhatia, D. D. (2023) · Traffic · doi:10.1111/tra.12906 · Cited by 22 · see citing works

Lithium entrapped chitosan nanoparticles to reduce toxicity and increase cellular uptake of lithium

Geeva, & Narayan, S. (2018) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2018.05.017 · Cited by 20 · see citing works

Direct Observation of Internalization and ROS Generation of Amyloid β‐Peptide in Neuronal Cells at Subcellular Resolution

Jiao, Y., Zhang, Y., Wei, Y., Liu, Z., An, W., & Guo, M. (2012) · ChemBioChem · doi:10.1002/cbic.201200465 · Cited by 19 · see citing works

Alzheimer’s Disease Amyloid β-Protein Mutations and Deletions That Define Neuronal Binding/Internalization as Early Stage Nonfibrillar/Fibrillar Aggregates and Late Stage Fibrils

Poduslo, J. F., Howell, K. G., Olson, N., Ramı́rez-Alvarado, M., & Kandimalla, K. K. (2012) · Biochemistry · doi:10.1021/bi300275g · Cited by 18 · see citing works

Extracellular amyloid beta 42 causes necrosis, inhibition of nuclear division, and mitotic disruption under both folate deficient and folate replete conditions as measured by the cytokinesis‐block micronucleus cytome assay

Lee, S. L., Thomas, P., & Fenech, M. F. (2013) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21811 · Cited by 17 · see citing works

Distinct Uptake Kinetics of Alzheimer Disease Amyloid-β 40 and 42 at the Blood-Brain Barrier Endothelium

Sharda, N., Ahlschwede, K. M., Curran, G. L., Lowe, V. J., & Kandimalla, K. K. (2020) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.120.000086 · Cited by 13 · see citing works

Differential Effects of Alzheimer’s Disease Aβ40 and 42 on Endocytosis and Intraneuronal Trafficking

Omtri, R. S., Thompson, K. J., Tang, X., Gali, C. C., Panzenboeck, U., Davidson, M. W., Kalari, K. R., & Kandimalla, K. K. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.01.003 · Cited by 15 · see citing works

Internalized Amyloid-β (1-42) Peptide Inhibits the Store-Operated Calcium Entry in HT-22 Cells

Poejo, J., Orantos-Aguilera, Y., Martı́n-Romero, F. J., Mata, A. M., & Gutiérrez‐Merino, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012678 · Cited by 14 · see citing works

Amyloid Beta Peptide-Mediated Alterations in Mitochondrial Dynamics and its Implications for Alzheimer’s Disease

Monsalvo-Maraver, L. Á., Maya-López, M., Rangel‐López, E., Túnez, I., Tinkov, A. A., Skalny, A. V., Ferrer, B., Aschner, M., & Santamarı́a, A. (2022) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527321666220616094036 · Cited by 13 · see citing works

Infection of Primary Neurons Mediated by Nipah Virus Envelope Proteins: Role of Host Target Cells in Antiviral Action

Talekar, A., Pessi, A., & Porotto, M. (2011) · Journal of Virology · doi:10.1128/jvi.00452-11 · Cited by 13 · see citing works

The Pathological Nexus and Multipronged Approaches to Mitigate Ferroptosis and Alzheimer’s Disease

Moorthy, H., Sain, S., Padhi, D., & Govindaraju, T. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00917 · Cited by 12 · see citing works

Cell cycle markers have different expression and localization patterns in neuron-like PC12 cells and primary hippocampal neurons

Neğiş, Y., Yıldız, A., Korulu, Ş., & Karabay, A. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.03.100 · Cited by 12 · see citing works

C9ORF72-derived poly-GA DPRs undergo endocytic uptake in iAstrocytes and spread to motor neurons

Marchi, P. M., Marrone, L., Brasseur, L., Coens, A., Webster, C. P., Bousset, L., Destro, M., Smith, E. F., Walther, C. G., Alfred, V., et al. (2022) · Life Science Alliance · doi:10.26508/lsa.202101276 · Cited by 12 · see citing works

Protective effect of saffron carotenoids against amyloid b eta‐induced neurotoxicity in differentiated PC12 cells via the unfolded protein response and autophagy

Sanjari‐Pour, M., Faridi, N., Wang, P., & Bathaie, S. Z. (2023) · Phytotherapy Research · doi:10.1002/ptr.7773 · Cited by 11 · see citing works

Amyloid-Beta Peptides 40 and 42 Employ Distinct Molecular Pathways for Cell Entry and Intracellular Transit at the Blood–Brain Barrier Endothelium

Wang, Z., Sharda, N., Omtri, R. S., Li, L., & Kandimalla, K. K. (2023) · Molecular Pharmacology · doi:10.1124/molpharm.123.000670 · Cited by 11 · see citing works

Delivery of drugs to the brain via the blood brain barrier using colloidal carriers

Tucker, I. G., Yang, L., & Mujoo, H. (2012) · Journal of Microencapsulation · doi:10.3109/02652048.2012.658445 · Cited by 10 · see citing works

Semimechanistic Population Pharmacokinetic Modeling to Investigate Amyloid Beta Trafficking and Accumulation at the BBB Endothelium

Wang, Z., Sharda, N., Curran, G. L., Li, L., Lowe, V. J., & Kandimalla, K. K. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.1c00549 · Cited by 11 · see citing works

Could Intracrine Biology Play a Role in the Pathogenesis of Transmissable Spongiform Encephalopathies Alzheimer’s Disease and Other Neurodegenerative Diseases?

Ré, R. N. (2013) · The American Journal of the Medical Sciences · doi:10.1097/maj.0b013e3182a28af3 · Cited by 9 · see citing works

Imaging Amyloid‐β Membrane Interactions: Ion‐Channel Pores and Lipid‐Bilayer Permeability in Alzheimer's Disease

Viles, J. H. (2023) · Angewandte Chemie · doi:10.1002/ange.202215785 · Cited by 7 · see citing works

The Molecular Physiopathogenesis of Islet Amyloidosis

Bhowmick, D. C., Singh, S., Trikha, S., & Jeremic, A. M. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_62 · Cited by 8 · see citing works

Exercise-mediated cerebrovascular repair in Alzheimer's disease: from pathophysiology to therapeutic precision

Cai, M., Cai, K., Wei, Z., Zhou, J., Shu, J., Wang, W., Sun, W., & Hu, J. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1632365 · Cited by 5 · see citing works

A novel micellar carrier to reverse multidrug resistance of tumours: TPGS derivatives with end-grafted cholesterol

Qi, Z., Shi, J. D., Song, Y., & Deng, Y. (2023) · Journal of drug targeting · doi:10.1080/1061186x.2023.2205614 · Cited by 4 · see citing works

p75NTR is mainly responsible for Aβ toxicity but not for its internalization: a primary study

Yu, H., Yang, M., Wang, Y., Xiao, R., & Zhou, X. (2011) · Neurological Sciences · doi:10.1007/s10072-011-0892-x · Cited by 4 · see citing works

Differential accumulation of human β-amyloid and tau from enriched extracts in neuronal and endothelial cells

Rabanal‐Ruiz, Y., Pedrero-Prieto, C. M., Rodríguez, L. S., Flores‐Cuadrado, A., Saiz‐Sánchez, D., Frontiñán-Rubio, J., Úbeda‐Bañón, I., Durán‐Prado, M., Martı́nez-Marcos, A., & Peinado, J. R. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167204 · Cited by 3 · see citing works

Neurogliovascular alterations in brain pathologies across lifespan

Daigle, B., Bevilacqua, L. M., Noël, V. P., Lebel, M., Côté, D. C., Lévesque, L., & Ménard, C. (2024) · Glial health research. · doi:10.1016/j.ghres.2024.100004 · Cited by 4 · see citing works

Imaging of Amyloid-β Aggregation Using a Novel Quantum dot Nanoprobe and its Advanced Applications

Tokuraku, K., & Ikezu, T. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-394431-3.00011-0 · Cited by 5 · see citing works

A Toxicogenic Interaction between Intracellular Amyloid-β and Apolipoprotein-E

Dey, A., Verma, A., Bhaskar, U., Sarkar, B., Kallianpur, M., Vishvakarma, V., Das, A. K., Garai, K., Mukherjee, O., Ishii, K., et al. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00048 · Cited by 3 · see citing works

Neuroprotective Effects of Cinnamon (Cinnamomum Verum) Via Modulation of Stress Response Signaling

Gomada, Y. (2012) · Cited by 2 · see citing works

Inhibiting Phosphorylation of Tau (τ) Proteins at Ser262 Using Peptide-Based R1 Domain Mimetics

Alqaeisoom, N., Cheng, Q., Arachchige, D., Colvin, R. A., & Holub, J. M. (2018) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-018-9689-6 · Cited by 2 · see citing works

Hunting cellular mechanisms underlying the spreading of misfolded protein pathology in the brain

Pecho‐Vrieseling, E. (2016) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12264 · Cited by 2 · see citing works

Anti-amyloid β hydrophobic peptides in Alzheimer’s disease: biomarkers and therapeutic potential

Gutiérrez‐Merino, C. (2025) · Exploration of neuroscience · doi:10.37349/en.2025.100672 · Cited by 2 · see citing works

Aβ-driven nuclear pore complex dysfunction alters activation of necroptosis proteins in a mouse model of Alzheimer’s diseasePreprint

Bansal, V. A., Tan, J. M., Soon, H. R., Zainolabidin, N., Saido, T. C., & Ch’ng, T. H. (2024) · eLife · doi:10.7554/elife.92069.3 · Cited by 4 · see citing works

Amyloid-beta peptides 40 and 42 employ distinct molecular pathways for cell entry and intracellular transit at the BBB endotheliumPreprint

Wang, Z., Sharda, N., Omtri, R. S., Li, L., & Kandimalla, K. K. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.17.516996 · Cited by 1 · see citing works

Characterization of Amino Acid Residues Integral to Neuronal Binding of Amyloid Beta Protein in Alzheimer’s Disease

Olson, N. (2011) · DigitalCommons - CalPoly (California State Polytechnic University)

Mitochondria-targeted amyloid: Relevance to neurotoxicity and Alzheimer's disease

Tillement, L. (2011) · DigitalGeorgetown (Georgetown University Library)

C9orf72 -derived poly-GA DPRs undergo endocytic uptake in iNPC-derived astrocytes and spread to motor neuronsPreprint

Marchi, P. M., Marrone, L., Brasseur, L., Bousset, L., Webster, C. P., Destro, M., Smith, E. F., Walther, C. G., Alfred, V., Marroccella, R., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.10.11.463891

Dissimilar accumulation of human β-amyloid and tau from enriched extracts in neuronal and endothelial cellsPreprint

Rabanal‐Ruiz, Y., Pedrero-Prieto, C. M., Sanchez-Rodriguez, L., Flores‐Cuadrado, A., Saiz‐Sánchez, D., Frontiñán-Rubio, J., Úbeda‐Bañón, I., Durán‐Prado, M., Martı́nez-Marcos, A., & Peinado, J. R. (2023) · Research Square · doi:10.21203/rs.3.rs-3343553/v1

Aβ-driven nuclear pore complex dysfunction alters activation of necroptosis proteins in a mouse model of Alzheimer’s DiseasePreprint

Bansal, V. A., Tan, J. M., Soon, H. R., Zainolabidin, N., Saito, T., & Ch’ng, T. H. (2024) · eLife · doi:10.7554/elife.92069.1

Aβ-driven nuclear pore complex dysfunction alters activation of necroptosis proteins in a mouse model of Alzheimer’s DiseasePreprint

Bansal, V. A., Tan, J. M., Soon, H. R., Zainolabidin, N., Saito, T., & Ch’ng, T. H. (2024) · eLife · doi:10.7554/elife.92069.2

Brain Endothelial Cell Expression in Alzheimer’s Disease Showing Stage-Associated Changes

Zheng, Z.-K. (2025) · Advances in Alzheimer's Disease · doi:10.4236/aad.2025.143003

Estudi dels mecanismes moleculars implicats en el dany vascular induït per l'activitat catalítica de la SSAO en el context de l'angiopatia cerebral amiloide associada a la demència tipus Alzheimer

Piñol, M. S. (2009) · TDX (Tesis Doctorals en Xarxa)

Alzheimer’s disease PSEN-2 N141I variant alters trafficking of amyloid beta oligomers in iPSC-derived brain endothelial-like cellsPreprint

Lam, J., Takeuchi, L. E., Qi, K., & Simmons, C. A. (2026) · Research Square · doi:10.21203/rs.3.rs-8787446/v1

Etude des mécanismes physiοpathοlοgiques de la maladie d'Alzheimer : appοrt de l'étude des variants du gène SΟRL1

Castelot, R. (2024) · theses.fr (ABES) · doi:10.70675/c2a7ce1ez8caaz4593zbb3azae8add8055b5

3D nanoscale imaging of amyloid-β oligomer interactions with extracellular vesicles by cryo-ET

Khursheed, A., Shang, Q., Zhang, H., Tian, Y., Szwedziak, P., Volkov, V. A., & Viles, J. H. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2610068123

Mechanism of Neuronal versus Endothelial Cell Uptake of Alzheimer’s Disease Amyloid b Protein

K, K. K., Olenych, S. G., Fulzele, S., Davidson, M. W., & Poduslo, J. F. (2016)

How Neurons Internalize Alzheimer's Disease Amyloid β Protein

Worthy, P. N., Olenych, S. G., Fulzele, S., Davidson, M. W., Poduslo, J. F., & Kandimalla, K. K. (2009) · The FASEB Journal · doi:10.1096/fasebj.23.1_supplement.lb258

Differences in the Cellular Uptake and Intracellular Itineraries of Amyloid Beta Proteins 40 and 42: Ramifications for the Alzheimer’s Drug Discovery

Omtri, R. S., Davidson, M. W., Arumugam, B., Poduslo, J. F., & Kandimalla, K. K. (2012) · Molecular Pharmaceutics · doi:10.1021/mp200530q · Cited by 68 · see citing works

Perforin Promotes Amyloid Beta Internalisation in Neurons

Lana, E., Khanbolouki, M., Degavre, C., Samuelsson, E., Åkesson, E., Winblad, B. G., Alici, E., Lithner, C. U., & Behbahani, H. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9685-9 · Cited by 18 · see citing works

The uptake of β-amyloid by various brain cells exhibits heterogeneity and correlates with the CD14 expression

Shi, J., Ma, Y., Gao, L., Dai, Y., Chen, Q., Li, X., Liu, H., Li, R., Zhang, J., & Yan, C. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111699 · Cited by 2 · see citing works