The DOI matches its Crossref record; 122 of the 125 references it cites were found in a registry or an index.
Low‐density lipoprotein receptor‐related protein‐1: a serial clearance homeostatic mechanism controlling Alzheimer’s amyloid β‐peptide elimination from the brain
Open accessAbstract
J. Neurochem. (2010) 115 , 1077–1089. Low‐density lipoprotein receptor‐related protein‐1 (LRP1), a member of the low‐density lipoprotein receptor family, has major roles in the cellular transport of cholesterol, endocytosis of 40 structurally diverse ligands, transcytosis of ligands across the blood–brain barrier, and transmembrane and nuclear signaling. Recent evidence indicates that LRP1 regulates brain and systemic clearance of Alzheimer’s disease (AD) amyloid β‐peptide (Aβ). According to the two‐hit vascular hypothesis for AD, vascular damage precedes cerebrovascular and brain Aβ accumulation ( hit 1 ) which then further amplifies neurovascular dysfunction ( hit 2 ) preceding neurodegeneration. In this study, we discuss the roles of LRP1 during the hit 1 and hit 2 stage of AD pathogenesis and describe a three‐level serial LRP1‐dependent homeostatic control of Aβ clearance including (i) cell‐surface LRP1 at the blood–brain barrier and cerebrovascular cells mediating brain‐to‐blood Aβ clearance (ii) circulating LRP1 providing a key endogenous peripheral ‘sink’ activity for plasma Aβ which prevents free Aβ access to the brain, and (iii) LRP1 in the liver mediating systemic Aβ clearance. Pitfalls in experimental Aβ brain clearance measurements with the concurrent use of peptides/proteins such as receptor‐associated protein and aprotinin are also discussed. We suggest that LRP1 has a critical role in AD pathogenesis and is an important therapeutic target in AD.
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.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“The brain-to-blood transfer of monomeric Aβ is highly dependent on low-density lipoprotein receptor-related protein 1 (LRP1) [13, 14], which in brain endothelium is primarily located at the abluminal side [13, 15].”
From PCSK9 acts as a key regulator of Aβ clearance across the blood–brain barrier (2022) · cites this paper as [13]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“a key mechanism by which A 𝛃 40 and 42 peptides are cleared from brain-toblood (696).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [696]
The cited source says what the claim attributes to it.
In the citing paper
“The brain-to-blood transfer of monomeric Aβ is highly dependent on low-density lipoprotein receptor-related protein 1 (LRP1) [13, 14], which in brain endothelium is primarily located at the abluminal side [13, 15].”
From PCSK9 acts as a key regulator of Aβ clearance across the blood–brain barrier (2022) · cites this paper as [13]
The cited source says what the claim attributes to it.
In the citing paper
“LRP1 is a key mediator of cerebral Aβ clearance by its rapid Aβ transport across the BBB into the periphery [13, 14].”
From PCSK9 acts as a key regulator of Aβ clearance across the blood–brain barrier (2022) · cites this paper as [13]
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×
“This in turn leads to a greater accumulation of different Ab species in the brain (Kayed et al. 2003) including neurotoxic Ab oligomers (Walsh et al. 2005; Lesné et al. 2006).”
RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064
Gupta, A., & Uribarri, J. (2016) · Hormone Research in Paediatrics · doi:10.1159/000444053 · Cited by 4,023
Harold, D., Abraham, R., Hollingworth, P., Sims, R., Gerrish, A., Hamshere, M. L., Pahwa, J. S., Moskvina, V., Dowzell, K., Williams, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.440 · Cited by 3,326
The Blood-Brain Barrier in Health and Chronic Neurodegenerative Disorders
Zlokovic, B. V. (2008) · Neuron · doi:10.1016/j.neuron.2008.01.003 · Cited by 3,280
The molecular pathology of Alzheimer's disease
Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708
Research works printed but not linked: 2
- 10.1172/JCI200113992 · DOI · Paper page
- 10.1016/S0896-6273(04)00533-1 · DOI
Cited by
Sorted by citations
Iliff, J. J., Wang, M., Liao, Y., Plogg, B. A., Peng, W., Gundersen, G. A., Benveniste, H., Vates, G. E., Deane, R., Goldman, S. A., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003748 · Cited by 5,824
Self-citationNeurovascular pathways to neurodegeneration in Alzheimer’s disease and other disorders
Zlokovic, B. V. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn3114 · Cited by 2,969
Blood-Brain Barrier: From Physiology to Disease and Back
Sweeney, M. D., Zhao, Z., Montagne, A., Nelson, A. R., & Zlokovic, B. V. (2019) · Physiological Reviews · doi:10.1152/physrev.00050.2017 · Cited by 2,312
Neuroinflammation and M2 Microglia: The Good, the Bad, and the Inflamed
Cherry, J. D., Olschowka, J. A., & O’Banion, M. K. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-98 · Cited by 1,748
Clearance systems in the brain—implications for Alzheimer disease
Tarasoff-Conway, J. M., Carare, R. O., Osorio, R. S., Glodzik, L., Butler, T., Fieremans, E., Axel, L., Rusinek, H., Nicholson, C., Zlokovic, B. V., et al. (2015) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.119 · Cited by 1,678
Establishment and Dysfunction of the Blood-Brain Barrier
Zhao, Z., Nelson, A. R., Betsholtz, C., & Zlokovic, B. V. (2015) · Cell · doi:10.1016/j.cell.2015.10.067 · Cited by 1,670
Cerebral blood flow regulation and neurovascular dysfunction in Alzheimer disease
Kisler, K., Nelson, A. R., Montagne, A., & Zlokovic, B. V. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.48 · Cited by 1,243
From blood–brain barrier to blood–brain interface: new opportunities for CNS drug delivery
Banks, W. A. (2016) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2015.21 · Cited by 1,204
Pericytes of the neurovascular unit: key functions and signaling pathways
Sweeney, M. D., Ayyadurai, S., & Zlokovic, B. V. (2016) · Nature Neuroscience · doi:10.1038/nn.4288 · Cited by 1,125
Functional morphology of the blood–brain barrier in health and disease
Liebner, S., Dijkhuizen, R. M., Reiss, Y., Plate, K. H., Agalliu, D., & Constantin, G. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1815-1 · Cited by 872
The blood-brain barrier in Alzheimer’s disease
Zenaro, E., Piacentino, G., & Constantin, G. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.07.007 · Cited by 767
Chin-Chan, M., Navarro-Yepes, J., & Quintanilla‐Vega, B. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00124 · Cited by 746
Zeppenfeld, D. M., Simon, M., Haswell, J. D., D’Abreo, D., Murchison, C., Quinn, J. F., Grafe, M. R., Woltjer, R. L., Kaye, J., & Iliff, J. J. (2017) · JAMA Neurology · doi:10.1001/jamaneurol.2016.4370 · Cited by 651
Understanding the functions and relationships of the glymphatic system and meningeal lymphatics
Louveau, A., Plog, B. A., Antila, S., Alitalo, K., Nedergaard, M., & Kipnis, J. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90603 · Cited by 640
Neurovascular dysfunction and neurodegeneration in dementia and Alzheimer's disease
Nelson, A. R., Sweeney, M. D., Sagare, A. P., & Zlokovic, B. V. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.016 · Cited by 559
Self-citationEmerging concepts in sporadic cerebral amyloid angiopathy
Charidimou, A., Boulouis, G., Gurol, M. E., Ayata, C., Bacskai, B. J., Frosch, M. P., Viswanathan, A., & Greenberg, S. M. (2017) · Brain · doi:10.1093/brain/awx047 · Cited by 555
Cholesterol metabolism in neurons and astrocytes
Pfrieger, F. W., & Ungerer, N. (2011) · Progress in Lipid Research · doi:10.1016/j.plipres.2011.06.002 · Cited by 500
Physiological blood–brain transport is impaired with age by a shift in transcytosis
Yang, A. C., Stevens, M. Y., Chen, M. B., Lee, D. P., Stähli, D., Gate, D., Contrepois, K., Chen, W., Iram, T., Zhang, L., et al. (2020) · Nature · doi:10.1038/s41586-020-2453-z · Cited by 477
Neurological Diseases in Relation to the Blood–Brain Barrier
Rosenberg, G. A. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2011.197 · Cited by 454
Grammas, P. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-26 · Cited by 432
Redzic, Z. B. (2011) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-8-3 · Cited by 455
Sehgal, N., Gupta, A., Valli, R. K., Joshi, S. D., Mills, J. T., Hamel, E., Khanna, P., Jain, S. C., Thakur, S. S., & Ravindranath, V. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1112209109 · Cited by 390
Brain Pericytes As Mediators of Neuroinflammation
Rustenhoven, J., Jansson, D., Smyth, L. C., & Dragunow, M. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.12.001 · Cited by 371
Pathophysiology of the Neurovascular Unit: Disease Cause or Consequence?
Stanimirovic, D. B., & Friedman, A. (2012) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2012.25 · Cited by 359
New Insights Into the Pathogenesis of Alzheimer's Disease
Fan, L., Mao, C., Hu, X., Zhang, S., Yang, Z., Hu, Z., Sun, H., Fan, Y., Dong, Y., Yang, J., et al. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2019.01312 · Cited by 362
Mikulska, P., Malinowska, M., Ignacyk, M., Szustowski, P., Nowak, J., Pesta, K., Szeląg, M., Szklanny, D., Judasz, E., Kaczmarek, G., et al. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15041057 · Cited by 387
Shinohara, M., Tachibana, M., Kanekiyo, T., & Bu, G. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075796 · Cited by 297
Cerebral small vessel disease: Capillary pathways to stroke and cognitive decline
Østergaard, L., Engedal, T. S., Moreton, F. C., Hansen, M. B., Wardlaw, J. M., Dalkara, T., Markus, H. S., & Muir, K. W. (2015) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x15606723 · Cited by 290
Kanekiyo, T., & Bu, G. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00093 · Cited by 281
Oxidative stress and β-amyloid protein in Alzheimer’s disease
Cai, Z., Zhao, B., & Ratka, A. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-011-8155-9 · Cited by 279
The Pericyte: A Forgotten Cell Type with Important Implications for A lzheimer's Disease?
Winkler, E. A., Sagare, A. P., & Zloković, B. V. (2014) · Brain Pathology · doi:10.1111/bpa.12152 · Cited by 284
Self-citationHay, J. R., Johnson, V. E., Young, A. M. H., Smith, D. H., & Stewart, W. B., Jr. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000261 · Cited by 275
Erickson, M. A., & Banks, W. A. (2011) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2011.06.006 · Cited by 262
The olfactory bulb as the entry site for prion-like propagation in neurodegenerative diseases
Rey, N. L., Wesson, D. W., & Brundin, P. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.12.013 · Cited by 257
Neurovascular Dysfunction and Faulty Amyloid -Peptide Clearance in Alzheimer Disease
Sagare, A. P., Bell, R. D., & Zlokovic, B. V. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011452 · Cited by 251
Self-citationNeuroinflammation: A Common Pathway in CNS Diseases as Mediated at the Blood-Brain Barrier
Erickson, M. A., Dohi, K., & Banks, W. A. (2012) · NeuroImmunoModulation · doi:10.1159/000330247 · Cited by 254
Carnevale, D., Mascio, G., D'Andrea, I., Fardella, V., Bell, R. D., Branchi, I., Pallante, F., Zlokovic, B., Yan, S. S., & Lembo, G. (2012) · Hypertension · doi:10.1161/hypertensionaha.112.195511 · Cited by 241
Self-citationBrain Microvascular Pericytes in Vascular Cognitive Impairment and Dementia
Uemura, M. T., Maki, T., Ihara, M., Lee, V. M. ‐., & Trojanowski, J. Q. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00080 · Cited by 246
Brain imaging of neurovascular dysfunction in Alzheimer’s disease
Montagne, A., Nation, D. A., Pa, J., Sweeney, M. D., Toga, A. W., & Zlokovic, B. V. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1570-0 · Cited by 239
Vandal, M., White, P. J., Tremblay, C., St‐Amour, I., Chevrier, G., Émond, V., Lefrançois, D., Virgili, J., Planel, E., Giguère, Y., et al. (2014) · Diabetes · doi:10.2337/db14-0375 · Cited by 243
Blood-derived amyloid-β protein induces Alzheimer’s disease pathologies
Bu, X., Xiang, Y., Jin, W.-S., Wang, J., Shen, L.-L., Huang, Z.-L., Zhang, K., Liu, Y.-H., Zeng, F., Liu, H., et al. (2017) · Molecular Psychiatry · doi:10.1038/mp.2017.204 · Cited by 233
Ramanathan, A., Nelson, A. R., Sagare, A. P., & Zlokovic, B. V. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00136 · Cited by 205
Self-citationThe capillary dysfunction hypothesis of Alzheimer's disease
Østergaard, L., Aamand, R., Gutiérrez‐Jiménez, E., Ho, Y.-C. L., Blicher, J. U., Madsen, S., Nagenthiraja, K., Dalby, R. B., Drasbek, K. R., Møller, A., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.09.011 · Cited by 203
Cherry, J. D., Liu, B., Frost, J. L., Lemere, C. A., Williams, J. P., Olschowka, J. A., & O’Banion, M. K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0053275 · Cited by 206
Alzheimer’s Disease: The Link Between Amyloid-β and Neurovascular Dysfunction
Solis, E., Hascup, K. N., & Hascup, E. R. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200473 · Cited by 192
How Do Meningeal Lymphatic Vessels Drain the CNS?
Raper, D. M. S., Louveau, A., & Kipnis, J. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.07.001 · Cited by 184
Sphingolipids: Critical players in Alzheimer’s disease
van Echten‐Deckert, G., & Walter, J. (2012) · Progress in Lipid Research · doi:10.1016/j.plipres.2012.07.001 · Cited by 171
Cerebrovascular pathology during the progression of experimental Alzheimer's disease
Giannoni, P., Arango-Lievano, M., das Neves, I., Rousset, M.-C., Baranger, K., Rivera, S., Jeanneteau, F. D., Claeysen, S., & Marchi, N. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.01.001 · Cited by 152
Erickson, M. A., Hartvigson, P. E., Morofuji, Y., Owen, J. B., Butterfield, D. A., & Banks, W. A. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-150 · Cited by 145
Neurovascular Defects and Faulty Amyloid-β Vascular Clearance in Alzheimer's Disease
Sagare, A. P., Bell, R. D., & Zloković, B. V. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129037 · Cited by 152
Self-citationSagare, A. P., Deane, R., & Zloković, B. V. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.07.008 · Cited by 150
Self-citationGoulay, R., Romo, L. M., Hol, E. M., & Dijkhuizen, R. M. (2019) · Translational Stroke Research · doi:10.1007/s12975-019-00755-2 · Cited by 144
Ren, H., Luo, C., Feng, Y., Yao, X., Shi, Z., Liang, F., Kang, J. X., Wan, J., Pei, Z., & Su, H. (2016) · The FASEB Journal · doi:10.1096/fj.201600896 · Cited by 142
PDGF/PDGFR axis in the neural systems
Sil, S., Periyasamy, P., Thangaraj, A., Chivero, E. T., & Buch, S. J. (2018) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2018.01.006 · Cited by 141
Is Alzheimer’s Disease a Liver Disease of the Brain?
Bassendine, M. F., Taylor-Robinson, S. D., Fertleman, M., Khan, M., & Neely, D. (2020) · Journal of Alzheimer's Disease · doi:10.3233/jad-190848 · Cited by 124
Revisiting the blood-brain barrier: A hard nut to crack in the transportation of drug molecules
Harilal, S., Jose, J., Parambi, D. G. T., Kumar, R., Unnikrishnan, M. K., Uddin, M. S., Mathew, G. E., Pratap, R., Marathakam, A., & Mathew, B. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.03.018 · Cited by 127
A Neurovascular Perspective for Long-Term Changes After Brain Trauma
Pop, V., & Badaut, J. (2011) · Translational Stroke Research · doi:10.1007/s12975-011-0126-9 · Cited by 125
Regina, A., Demeule, M., Tripathy, S., Lord-Dufour, S., Currie, J.-C., Iddir, M., Annabi, B., Castaigne, J.-P., & Lachowicz, J. E. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0399 · Cited by 112
Spuch, C., Ortolano, S., & Navarro, C. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00269 · Cited by 107
de Vries, H. E., Kooij, G., Frenkel, D., Georgopoulos, S., Monsonego, A., & Janigro, D. (2012) · Epilepsia · doi:10.1111/j.1528-1167.2012.03702.x · Cited by 116
Walker, J. M., Dixit, S., Saulsberry, A. C., May, J. M., & Harrison, F. E. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.01.004 · Cited by 110
Yang, C., & Chuang, K. (2012) · MedChemComm · doi:10.1039/c2md00279e · Cited by 107
Zhao, Y., Li, Y., Zhao, J., Song, J., & Zhao, Y. (2016) · Reviews in the Neurosciences · doi:10.1515/revneuro-2015-0069 · Cited by 109
The Blood–Brain Barrier in Alzheimer's Disease
Sharma, H. S., Castellani, R. J., Smith, M. A., & Sharma, A. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00003-x · Cited by 105
Li, X., & Buxbaum, J. N. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-79 · Cited by 104
Alzheimer's disease: β‐amyloid plaque formation in human brain
Seeman, P. M., & Seeman, N. (2011) · Synapse · doi:10.1002/syn.20957 · Cited by 103
The Role of Neurovascular System in Neurodegenerative Diseases
Ahmad, A., Patel, V., Xiao, J., & Khan, M. M. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02023-z · Cited by 97
Apolipoprotein E in Alzheimer’s disease: molecular insights and therapeutic opportunities
Belaidi, A. A., Bush, A. I., & Ayton, S. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00843-y · Cited by 91
The role of SLC transporters for brain health and disease
Nguyen, Y. T.-K., Ha, H. T. T., Nguyen, T. H., & Nguyen, L. N. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04074-4 · Cited by 95
Artificial apolipoprotein corona enables nanoparticle brain targeting
Magro, R. D., Albertini, B., Beretta, S., Rigolio, R., Donzelli, E., Chiorazzi, A., Ricci, M., Blasi, P., & Sancini, G. (2017) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2017.11.008 · Cited by 93
Seok, H., Lee, M., Shin, E., Yun, M. R., Lee, Y., Moon, J. H., Kim, E., Lee, P. H., Lee, B., Kang, E. S., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40736-x · Cited by 92
Aβ Internalization by Neurons and Glia
Mohamed, A., & Chaves, E. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/127984 · Cited by 94
Hayden, M. R. (2019) · Brain Sciences · doi:10.3390/brainsci9100262 · Cited by 95
Neural stem cell therapy for neurovascular injury in Alzheimer's disease
Boese, A. C., Hamblin, M. H., & Lee, J. (2019) · Experimental Neurology · doi:10.1016/j.expneurol.2019.113112 · Cited by 89
Santos, D. B., Peres, K. C., Ribeiro, R. P., Colle, D., dos Santos, A. A., Moreira, E. L. G., Souza, D. O., Figueiredo, C. P., & Farina, M. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.11.036 · Cited by 88
Fanlo-Ucar, H., Picón-Pagès, P., Herrera-Fernández, V., ILL‐Raga, G., & Muñoz, F. J. (2024) · Antioxidants · doi:10.3390/antiox13101208 · Cited by 94
The Abluminal Endothelial Membrane in Neurovascular Remodeling in Health and Disease
Hermann, D. M., & ElAli, A. (2012) · Science Signaling · doi:10.1126/scisignal.2002886 · Cited by 86
Wang, S., Mao, Y., Narimatsu, Y., Ye, Z., Tian, W., Goth, C. K., Lira‐Navarrete, E., Borbye‐Lorenzen, N., Benito‐Vicente, A., Martı́n, C., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.817981 · Cited by 86
Lipid Metabolism and Glial Lipoproteins in the Central Nervous System
Hayashi, H. (2011) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.34.453 · Cited by 80
Ullah, R., Park, T. J., Huang, X., & Kim, M. O. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101451 · Cited by 78
Cross-talk of membrane lipids and Alzheimer-related proteins
Walter, J., & van Echten‐Deckert, G. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-34 · Cited by 79
Remembering your A, B, C's: Alzheimer's disease and ABCA1
Lewandowski, C. T., Laham, M. S., & Thatcher, G. R. J. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.011 · Cited by 76
Divecha, Y. A., Rampes, S., Tromp, S., Boyanova, S., Fleckney, A. L., Fidanboylu, M., & Thomas, S. A. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100052 · Cited by 83
The emerging role of furin in neurodegenerative and neuropsychiatric diseases
Zhang, Y., Gao, X., Bai, X., Yao, S., Chang, Y., & Gao, G. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00313-1 · Cited by 80
Lipopolysaccharide endotoxemia induces amyloid-β and p-tau formation in the rat brain.
Wang, L., Wu, Q., Kirk, R. A., Horn, K. P., Salem, A. E., Hoffman, J. M., Yap, J. T., Sonnen, J. A., Towner, R. A., Bozza, F. A., et al. (2018) · Europe PMC (PubMed Central) · Cited by 74
P‐glycoprotein (ABCB1) and Oxidative Stress: Focus on Alzheimer’s Disease
Sita, G., Hrelia, P., Tarozzi, A., & Morroni, F. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7905486 · Cited by 73
Więckowska‐Gacek, A., Mietelska‐Porowska, A., Chutorański, D., Wydrych, M., Długosz, J., & Wojda, U. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.654509 · Cited by 70
Lacoste, B., Tong, X.-K., Lahjouji, K., Couture, R., & Hamel, E. (2013) · Journal of Neuroinflammation · doi:10.1186/1742-2094-10-57 · Cited by 73
Endothelial LRP1 – A Potential Target for the Treatment of Alzheimer’s Disease
Storck, S. E., & Pietrzik, C. U. (2017) · Pharmaceutical Research · doi:10.1007/s11095-017-2267-3 · Cited by 74
Shi, M. Y., Movius, J., Dator, R., Aro, P., Zhao, Y., Pan, C., Lin, X., Bammler, T. K., Stewart, T., Zabetian, C. P., et al. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m114.040576 · Cited by 68
Targeting Glioblastoma: Advances in Drug Delivery and Novel Therapeutic Approaches
Yeini, E., Ofek, P., Albeck, N., Ajamil, D. R., Neufeld, L., Eldar‐Boock, A., Kleiner, R., Vaskovich‐Koubi, D., Koshrovski‐Michael, S., Dangoor, S. I., et al. (2020) · Advanced Therapeutics · doi:10.1002/adtp.202000124 · Cited by 70
Zhang, Y., Zhao, Y., Ao, X., Yu, W., Zhang, L., Wang, Y., & Chang, W. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.654978 · Cited by 73
Revisiting the role of brain and peripheral Aβ in the pathogenesis of Alzheimer's disease
Uddin, M. S., Kabir, M. T., Tewari, D., Mamun, A. A., Mathew, B., Aleya, L., Barreto, G. E., Bin-Jumah, M. N., Abdel‐Daim, M. M., & Ashraf, G. M. (2020) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2020.116974 · Cited by 70
The Dual Role of Low-Density Lipoprotein Receptor-Related Protein 1 in Atherosclerosis
Chen, J., Su, Y., Pi, S., Hu, B., & Mao, L. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2021.682389 · Cited by 70
Segatto, M., Leboffe, L., Trapani, L., & Pallottini, V. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666140303142902 · Cited by 65
Amyloid beta accumulation in HIV‐1‐infected brain: The role of the blood brain barrier
Andras, I. E., & Toborek, M. J. (2012) · IUBMB Life · doi:10.1002/iub.1106 · Cited by 67
Insulin signaling: An opportunistic target to minify the risk of Alzheimer’s disease
Pardeshi, R., Bolshette, N. B., Gadhave, K., Ahire, A., Ahmed, S., Cassano, T., Gupta, V. B., & Lahkar, M. (2017) · Psychoneuroendocrinology · doi:10.1016/j.psyneuen.2017.05.004 · Cited by 67
Lin, J.-P., Mironova, Y. A., Shrager, P., & Giger, R. J. (2017) · eLife · doi:10.7554/elife.30498 · Cited by 64
Roles of Non-Coding RNA in Alzheimer’s Disease Pathophysiology
Olufunmilayo, E. O., & Holsinger, R. M. D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512498 · Cited by 68
Yuede, C. M., Lee, H. J., Restivo, J. L., Davis, T. A., Hettinger, J. C., Wallace, C. E., Young, K. L., Hayne, M. R., Bu, G., Li, C.-Z., et al. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151428 · Cited by 65
Metadata
- Authors
- Zlokovic, B. V., Deane, R., Sagare, A. P., Bell, R. D., & Winkler, E. A.
- Affiliations
- University of Rochester Medicine (US)
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2010-10-05
- Volume
- 115
- Issue
- 5
- Pages
- 1077-1089
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- PMC
- PMC2972355
- OpenAlex
- W1957213374
- Cited by
- 261
- References
- 125
- Citations by year
- 2026: 8 · 2025: 17 · 2024: 19 · 2023: 18 · 2022: 18 · 2021: 11 · 2020: 15 · 2019: 16 · 2018: 7 · 2017: 24 · 2016: 27 · 2015: 17 · 2014: 13 · 2013: 8 · 2012: 25
- FWCI
- 1.66
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute on Aging (R37AG023084)
- National Institute of Neurological Disorders and Stroke (R37NS034467, R01NS034467, R37NS34467)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- LRP1, Alzheimer's disease, blood-brain barrier, hepatic clearance, neurovascular dysfunction, receptor-associated protein, aprotinin, therapeutic target
- MeSH terms
- Alzheimer Disease, Animals, Brain, Homeostasis, Humans, Amyloid beta-Peptides, LDL-Receptor Related Protein-Associated Protein
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