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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.
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“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]
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“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]
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“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]
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“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]
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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
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Items 101–200 of 262
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Osgood, D., Miller, M. C., Messier, A. A., Gonzalez, L., & Silverberg, G. D. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.05.011 · Cited by 63
Vandal, M., White, P. J., Tournissac, M., Tremblay, C., St‐Amour, I., Drouin‐Ouellet, J., Bousquet, M., Traversy, M.-T., Planel, E., Marette, A., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.03.024 · Cited by 64
Sleep Deprivation Induced Plasma Amyloid-β Transport Disturbance in Healthy Young Adults
Meng, W., Zhao, B., Huo, K., Deng, Y., Shang, S., Liu, J., Li, Y., Ma, L., Jiang, Y., Dang, L., et al. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161213 · Cited by 60
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El-Hakim, Y., Bake, S., Mani, K. K., & Sohrabji, F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105627 · Cited by 54
Emerging role of HDL in brain cholesterol metabolism and neurodegenerative disorders
Turri, M., Marchi, C., Adorni, M. P., Calabresi, L., & Zimetti, F. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2022.159123 · Cited by 54
Liu, W., Cai, H., Lin, M., Zhu, L., Gao, L., Zhong, R., Bi, S., Xue, Y., & Shang, X. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2016.03.026 · Cited by 57
Bilousova, T. V., Melnik, M., Miyoshi, E., Gonzalez, B. L., Poon, W. W., Vinters, H. V., Miller, C. A., Corrada, M. M., Kawas, C. H., Hatami, A., et al. (2019) · American Journal Of Pathology · doi:10.1016/j.ajpath.2019.04.010 · Cited by 57
Anwar, M. M., Özkan, E., & Özdemir, Y. (2021) · European Journal of Neuroscience · doi:10.1111/ejn.15372 · Cited by 58
PCSK9 acts as a key regulator of Aβ clearance across the blood–brain barrier
Mazura, A. D., Ohler, A., Storck, S. E., Kurtyka, M., Scharfenberg, F., Weggen, S., Becker-Pauly, C., & Pietrzik, C. U. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04237-x · Cited by 53
“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].”
BackgroundThe role of neurovascular unit damage in the occurrence and development of Alzheimer’s disease
Liu, X., Hou, D., Lin, F., Luo, J., Xie, J., Wang, Y., & Tian, Y. (2018) · Reviews in the Neurosciences · doi:10.1515/revneuro-2018-0056 · Cited by 55
Shively, S. B., Edgerton, S. L., Iacono, D., Purohit, D. P., Qu, B.-X., Haroutunian, V., Davis, K. L., Diaz-Arrastia, R., & Perl, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-016-1649-7 · Cited by 52
Segatto, M., Di Giovanni, A., Marino, M., & Pallottini, V. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24315 · Cited by 52
Zolezzi, J. M., Candia, S. B., Santos, M. J., & Inestrosa, N. C. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00176 · Cited by 56
Li, S., Hayden, E. Y., Garcia, V. J., Fuchs, D.-T. S., Sheyn, J., Daley, D. A., Rentsendorj, A., Torbati, T., Black, K. L., Rutishauser, U., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00049 · Cited by 48
Apolipoprotein E, amyloid-ß clearance and therapeutic opportunities in Alzheimer's disease
Kline, A. D. (2012) · Alzheimer s Research & Therapy · doi:10.1186/alzrt135 · Cited by 53
Ullah, R., & Lee, E. J. (2023) · Experimental Neurobiology · doi:10.5607/en23014 · Cited by 51
Factors Responsible for Plasma β-Amyloid Accumulation in Chronic Kidney Disease
Gronewold, J., Klafki, H., Baldelli, E., Kaltwasser, B., Seidel, U. K., Todica, O., Volsek, M., Haußmann, U., Wiltfang, J., Kribben, A., et al. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9218-y · Cited by 48
Moon, J. H., Kim, H. J., Yang, A. H., Kim, H. M., Lee, B., Kang, E. S., Lee, H. C., & Soo, B. (2011) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145711001611 · Cited by 47
Targeting ApoE4/ApoE receptor LRP1 in Alzheimer's disease
Martiskainen, H., Haapasalo, A., Kurkinen, K. M. A., Pihlajamäki, J., Soininen, H. S., & Hiltunen, M. O. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.789862 · Cited by 49
Patel, P., & Shah, J. (2017) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2017.06.007 · Cited by 46
Rodrigues, R. O., Shin, S.-R., & Bañobre-López, M. (2024) · Journal of Nanobiotechnology · doi:10.1186/s12951-024-02720-0 · Cited by 44
Lue, L., Pai, M., Chen, T., Hu, C., Huang, L.-K., Lin, W., Wu, C., Jeng, J.-S., Blennow, K., Sabbagh, M. N., et al. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00222 · Cited by 46
Georgievska, B., Gustavsson, S., Lundkvist, J., Neelissen, J. A. M., Eketjäll, S., Ramberg, V., Bueters, T., Agerman, K., Juréus, A., Svensson, S., et al. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.12937 · Cited by 43
Petralla, S., Panayotova, M., Franchina, E., Fricker, G., & Puris, E. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16070948 · Cited by 46
Zhang, W., Xiong, H., Callaghan, D., Liu, H., Jones, A., Pei, K., Fatehi, D., Brunette, E., & Stanimirovic, D. B. (2013) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-10-13 · Cited by 43
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Yang, T., & Williams, B. O. (2017) · Physiological Reviews · doi:10.1152/physrev.00013.2016 · Cited by 41
Madadi, S., Schwarzenbach, H., Saidijam, M., Mahjub, R., & Soleimani, M. (2019) · Cell & Bioscience · doi:10.1186/s13578-019-0354-3 · Cited by 41
Sagare, A. P., Bell, R. D., Srivastava, A., Sengillo, J. D., Singh, I., Nishida, Y., Chow, N., & Zloković, B. V. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.439570 · Cited by 42
Self-citationVascular mTOR-dependent mechanisms linking the control of aging to Alzheimer's disease
Galván, V., & Hart, M. J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.11.010 · Cited by 41
Soto-Rojas, L. O., Campa-Córdoba, B. B., Harrington, C. R., Salas‐Casas, A., Hernándes‐Alejandro, M., Villanueva‐Fierro, I., Bravo-Muñoz, M., Garcés‐Ramírez, L., de la Cruz‐López, F., Ontiveros‐Torres, M. Á., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073654 · Cited by 41
Endocrine Risk Factors for Cognitive Impairment
Moon, J. H. (2016) · Endocrinology and Metabolism · doi:10.3803/enm.2016.31.2.185 · Cited by 39
Zhao, Q., Yu, J., Tan, M., & Tan, L. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8759-9 · Cited by 42
Plasma β-amyloid peptides levels: A pilot study in bipolar depressed patients
Piccinni, A., Origlia, N., Veltri, A., Vizzaccaro, C., Marazziti, D., Catena-Dell’Osso, M., Conversano, C., Moroni, I., Domenici, L., & Dell’Osso, L. (2012) · Journal of Affective Disorders · doi:10.1016/j.jad.2011.12.042 · Cited by 43
Neuroprotective potential of formononetin, a naturally occurring isoflavone phytoestrogen
Singh, L., Kaur, H., Arya, G. C., & Bhatti, R. (2023) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14353 · Cited by 39
Macrophages and the development and progression of non-alcoholic fatty liver disease
Alabdulaali, B., Al‐Rashed, F., Al‐Onaizi, M., Kandari, A., Razafiarison, J., Tonui, D., Williams, M. R., Blériot, C., Ahmad, R., & Alzaïd, F. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1195699 · Cited by 38
The Beneficial Role of Exercise on Treating Alzheimer’s Disease by Inhibiting β-Amyloid Peptide
Tan, Z., Dong, F., Wu, L., Feng, Y.-S., & Zhang, F. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02514-7 · Cited by 39
Passarella, D., Ciampi, S., Liberto, V. D., Zuccarini, M., Ronci, M., Medoro, A., Foderà, E., Frinchi, M., Mignogna, D., Russo, C., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23168921 · Cited by 38
Torrico, B., Shaw, A. D., Mosca, R., Vivó-Luque, N., Hervás, A., Fernàndez-Castillo, N., Aloy, P., Bayés, M., Fullerton, J. M., Cormand, B., et al. (2019) · Journal of Psychiatry and Neuroscience · doi:10.1503/jpn.180184 · Cited by 34
The Imbalance of Vascular Molecules in Alzheimer's Disease
Bell, R. D. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121060 · Cited by 37
Self-citationCapillary Amyloid-β Protein Deposition in a Population-Based Study (Vantaa 85+)
Mäkelä, M., Paetau, A., Polvikoski, T., Myllykangas, L., & Tanskanen, M. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-150241 · Cited by 31
Blood-brain barrier penetration of an Aβ-targeted, arginine-rich, d -enantiomeric peptide
Jiang, N., Frenzel, D., Schartmann, E., van Groen, T., Kadish, I., Shah, N. J., Langen, K., Willbold, D., & Willuweit, A. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.07.002 · Cited by 32
Interactions between nanoparticles and pathological changes of vascular in Alzheimer’s disease
Lei, T., Yang, Z., Li, H., Qin, M., & Gao, H. (2024) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2024.115219 · Cited by 34
Fabbro, S., Schaller, K., & Seeds, N. W. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07359.x · Cited by 31
Chen, Y., Huang, W., Jiang, W., Wu, X., Ye, B., & Zhou, X. (2016) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/4196572 · Cited by 31
Is Alzheimer's disease amyloidosis the result of a repair mechanism gone astray?
Kokjohn, T. A., Maarouf, C. L., & Roher, A. E. (2011) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2011.05.2429 · Cited by 31
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He, K., Zhao, Z., Zhang, J., Li, D., Wang, S., & Liu, Q. (2024) · Antioxidants and Redox Signaling · doi:10.1089/ars.2024.0674 · Cited by 30
Development of a Multicomponent Intervention to Prevent Alzheimer's Disease
Saitô, S., Yamamoto, Y., & Ihara, M. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00490 · Cited by 30
Sharp, F. R., DeCarli, C. S., Jin, L., & Zhan, X. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1096206 · Cited by 33
Meox2 haploinsufficiency increases neuronal cell loss in a mouse model of Alzheimer's disease
Soto, I., Grabowska, W. A., Onos, K. D., Graham, L. C., Jackson, H. M., Simeone, S. N., & Howell, G. R. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.02.025 · Cited by 32
Lue, L., Kuo, Y., & Sabbagh, M. N. (2019) · Neurology and Therapy · doi:10.1007/s40120-019-00167-2 · Cited by 29
Sagare, A. P., Winkler, E. A., Bell, R. D., Deane, R., & Zloković, B. V. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22670 · Cited by 30
Self-citationGarcia, J., Chang, R., Steinberg, R. A., Arce, A., Yang, J., Eb, P. V. D., Abdullah, T., Chandrashekar, D. V., Eck, S. M., Meza, P., et al. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.930402 · Cited by 26
Almeida, M. C., Eger, S. J., He, C., Audouard, M., Nikitina, A. A., Glasauer, S. M. K., Han, D., Mejía‐Cupajita, B., Acosta‐Uribe, J., Villalba‐Moreno, N. D., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.02.009 · Cited by 34
Unmasking BACE1 in aging and age-related diseases
Bao, H., & Shen, Y. (2022) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2022.11.008 · Cited by 28
Unraveling the genes implicated in Alzheimer's disease
Giri, M., Shah, A., Upreti, B., & Rai, J. C. (2017) · Biomedical Reports · doi:10.3892/br.2017.927 · Cited by 25
Hort, J., Vališ, M., Kuča, K., & Angelucci, F. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20102405 · Cited by 27
Wang, H., Xiao, L., Wang, G., & Wang, G. (2019) · Physiology & Behavior · doi:10.1016/j.physbeh.2019.112749 · Cited by 27
Chandrashekar, D. V., Roules, G. C., Jagadeesan, N., Panchal, U. R., Oyegbesan, A., Imiruaye, O. E., Zhang, H., Garcia, J., Kaur, K., Win, S., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106570 · Cited by 27
Amyloid Beta Hypothesis in Alzheimer's Disease: Major Culprits and Recent Therapeutic Strategies
Dileep, K. V., & Chandra, R. (2019) · Current Drug Targets · doi:10.2174/1389450120666190806153206 · Cited by 26
LRP1 Downregulates the Alzheimer’s β-Secretase BACE1 by Modulating Its Intraneuronal Trafficking
Tanokashira, D., Motoki, K., Minegishi, S., Hosaka, A., Mamada, N., Tamaoka, A., Okada, T., Lakshmana, M. K., & Araki, W. (2015) · eNeuro · doi:10.1523/eneuro.0006-15.2015 · Cited by 25
Amyloid futures in the expanding pathology of brain aging and dementia
Thorwald, M. A., Silva, J. A., Head, E., & Finch, C. E. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12896 · Cited by 24
Active vaccination with ankyrin G reduces β-amyloid pathology in APP transgenic mice
Chadha, A. S., Merlini, M., Shetty, A., Tackenberg, C., Bali, J., Ferretti, M. T., McAfoose, J., Kulic, L., Bernreuther, C., Welt, T., et al. (2012) · Molecular Psychiatry · doi:10.1038/mp.2012.70 · Cited by 25
Gao, X., Wang, Y., Liu, Y., Yue, Q., Liu, Z., Ke, M., Zhao, S., & Li, C. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16656198 · Cited by 24
Pan, X., Zz, L., Gg, J., Lp, W., Cm, B., Yl, W., Chen, M. F., & Li, W. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105417 · Cited by 26
Shin, Y. J., Evitts, K. M., Jin, S., Howard, C. C., Sharp-Milgrom, M., Schwarze‐Taufiq, T. A., Kinoshita, C., Young, J. E., & Zheng, Y. Y. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106125 · Cited by 25
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 23
Billnitzer, A., Barskaya, I. Y., Yin, C., & Perez, R. G. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12051 · Cited by 22
Blockx, I., Einstein, S., Guns, P., Audekerke, J. V., Guglielmetti, C., Zago, W. M., Roose, D., Verhoye, M., der Linden, A. V., & Bard, F. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160023 · Cited by 23
Alzheimer’s disease is an inherent, natural part of human brain aging: an integrated perspective
Ferrer, I. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-3806 · Cited by 25
Amyloid Beta Influences Vascular Smooth Muscle Contractility and Mechanoadaptation
Hald, E. S., Timm, C. D., & Alford, P. W. (2016) · Journal of Biomechanical Engineering · doi:10.1115/1.4034560 · Cited by 21
Wang, X., Miao, Y., Abulizi, J., Fu, L., Mo, Y., Wei-guo, X., & Li, Z. (2016) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2016/7603975 · Cited by 21
Brzdąk, P., Nowak, D., Wiera, G., & Mozrzymas, J. W. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00178 · Cited by 21
Lead (Pb) and the Risk of Alzheimer’s disease or cognitive decline: A systematic review
Loef, M., Mendoza, L. F., & Walach, H. (2011) · Toxin Reviews · doi:10.3109/15569543.2011.624664 · Cited by 20
Simino, J. M., Wang, Z., Bressler, J., Chouraki, V. A., Yang, Q., Younkin, S. G., Seshadri, S. S., Fornage, M., Boerwinkle, E., & Mosley, T. H. (2017) · PLoS ONE · doi:10.1371/journal.pone.0180046 · Cited by 20
GJ-4 alleviates Aβ25-35-induced memory dysfunction in mice through protecting the neurovascular unit
Zhang, Z., Liu, H., Zhao, Z., Zang, C., Ju, C., Li, F., Wang, L., Yang, H., Bao, X., Yu, Y., et al. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110131 · Cited by 19
Take, Y., Chikai, Y., Shimamori, K., Kuragano, M., Kurita, H., & Tokuraku, K. (2021) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2021.101189 · Cited by 20
Lv, C., Niu, S., Yan, S., Bai, C., Yu, X., Hou, J., Gao, W., Zhang, J., Zhao, Z., Yang, C., et al. (2019) · Poultry Science · doi:10.3382/ps/pez168 · Cited by 19
Assessing Neuroprotective Agents for Aβ-Induced Neurotoxicity
Forest, K. H., & Nichols, R. A. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.05.013 · Cited by 19
Wu, B., Liu, Y., Li, H., Zhu, L., Zeng, L., Zhang, Z., & Peng, W. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.391305 · Cited by 22
Gromadzka, G., Wilkaniec, A., Tarnacka, B., Hadrian, K., Bendykowska, M., Przybyłkowski, A. M., & Litwin, T. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147545 · Cited by 17
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Macura, I. J., Živanović, A., Perović, M., Ciric, J., Major, T., Kanazir, S., & Ivković, S. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241814092 · Cited by 17
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Gao, Y., Wei, S., Gao, F., Gao, L., Dang, L., Shang, S., Chen, C., Huo, K., Wang, J., Wang, J., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.615838 · Cited by 15
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Darabi, S., Gorgich, E. A. C., Moradi, F., & Rustamzadeh, A. (2025) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2025.01.004 · Cited by 13
Wang, J., Meng, X., Jialun, Y., Tang, Y., Zeng, F., Wang, Y., Chen, Z., Chen, D., Zou, R., & Liu, W. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04350-w · Cited by 15
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Self-citationShepherd, C. E., Affleck, A. J., Bahar, A. Y., Carew‐Jones, F., Gregory, G., Small, D. H., & Halliday, G. M. (2020) · Brain and Behavior · doi:10.1002/brb3.1672 · Cited by 11
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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
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