The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
Central role for PICALM in amyloid-β blood-brain barrier transcytosis and clearance
Open accessAbstract
PICALM is a highly validated genetic risk factor for Alzheimer's disease (AD). We found that reduced expression of PICALM in AD and murine brain endothelium correlated with amyloid-β (Aβ) pathology and cognitive impairment. Moreover, Picalm deficiency diminished Aβ clearance across the murine blood-brain barrier (BBB) and accelerated Aβ pathology in a manner that was reversible by endothelial PICALM re-expression. Using human brain endothelial monolayers, we found that PICALM regulated PICALM/clathrin-dependent internalization of Aβ bound to the low density lipoprotein receptor related protein-1, a key Aβ clearance receptor, and guided Aβ trafficking to Rab5 and Rab11, leading to Aβ endothelial transcytosis and clearance. PICALM levels and Aβ clearance were reduced in AD-derived endothelial monolayers, which was reversible by adenoviral-mediated PICALM transfer. Inducible pluripotent stem cell-derived human endothelial cells carrying the rs3851179 protective allele exhibited higher PICALM levels and enhanced Aβ clearance. Thus, PICALM regulates Aβ BBB transcytosis and clearance, which has implications for Aβ brain homeostasis and clearance therapy.
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
“Similarly, several genes reported to be involved in Aβ catabolism, such as RAB5A, RAB11A, CLU, and LRP2 (49–53), were also down-regulated in AD monocytes, suggesting the impaired Aβ catabolism in AD monocytes.”
From Understanding monocyte-driven neuroinflammation in Alzheimer’s disease using human cortical organoid microphysiological systems (2025) · cites this paper as [51]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“PICALM is enriched in the endothelium of human cerebral vessels including capillaries, but is downregulated in AD patients (683).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [683]
The cited source says what the claim attributes to it.
In the citing paper
“PICALM controls receptor internalization and subsequent intracellular trafficking (683), via R-SNARE-mediated fusion of clathrin-coated vesicles with endosomes (411).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [683]
The cited source says what the claim attributes to it.
In the citing paper
“Specifically, LRP1 facilitates clathrin-dependent, receptor-mediated endothelial endocytosis of A 𝛃 at the abluminal membrane of the BBB, which requires phosphatidylinositol binding clathrin assembly protein (PICALM) (683).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [683]
The cited source says what the claim attributes to it.
In the citing paper
“PICALM guides transendothelial trafficking of endocytotic A 𝛃 -containing vesicles to Rab5, and then to Rab11 small GTPase leading to exocytosis of A 𝛃 across the luminal membrane of the BBB into the blood (683).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [683]
The cited source says what the claim attributes to it.
In the citing paper
“As shown in the Picalm + / -; APP Swe mice, diminished PICALM levels at the BBB accelerate amyloid pathology and behavioral deficits, which can be ameliorated by endothelial re-expression of Picalm using an adeno-associated virus (AAV) (683).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [683]
The cited source says what the claim attributes to it.
In the citing paper
“Endothelial cells derived from human iPSCs carrying homozygous protective rs3851179 A alleles exhibited increased PICALM expression and improved transvascular clearance of A 𝛃 across human BBB in vitro, when compared with isogenic cells from iPSCs carrying homozygous risk rs3851179 G alleles (683).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [683]
The cited source says what the claim attributes to it.
In the citing paper
“Although most of the PICALM single nucleotide variants (SNPs) associated with late-onset AD are located outside of the coding regions (683), the risk alleles of rs3851179 (236) and rs10792832 (344) lead to lower expression of PICALM isoform 2 in the frontal and temporal cortex in the human brain on the expression quantitative trait loci (eQTLs) (586), indicating that lower PICALM levels may”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [683]
The cited source says what the claim attributes to it.
In the citing paper
“These functions are central to its role in the clearance of both tau through autophagy (423) and A 𝛃 via transvascular transport across the BBB (683).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [683]
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 [15]
The cited source says what the claim attributes to it.
In the citing paper
“More recently, PICALM has been described in vitro and in vivo to participate to Aβ transcytosis and clearance at the BBB through clathrin-dependent internalisation of Aβ after its binding to the LDLR-related protein-1 [157].”
From The new genetic landscape of Alzheimer’s disease: from amyloid cascade to genetically driven synaptic failure hypothesis? (2019) · cites this paper as [157]
In the citing paper
“For previously reported loci, applying the same prioritization approach highlights several genes, as described in Fig. 2, some of which are involved in APP metabolism (FERMT2, PICALM) or tau toxicity (BIN1, CD2AP, FERMT2, CASS4, PTK2B)98–101.”
From Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing (2019) · cites this paper as [101]
In the citing paper
“Several genes encoding proteins intimately associated with the endothelium and Aβ clearance are highly validated AD risk factors, such as APOEε4, PICALM, and CLU [50, 51].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [51]
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: Pericyte loss influences Alzheimer-like neurodegeneration in mice
Sagare, A. P., Bell, R. D., Zhao, Z., Ma, Q., Winkler, E. A., Ramanathan, A., & Zlokovic, B. V. (2013) · Nature Communications · doi:10.1038/ncomms3932 · Cited by 589
Self-citationRetractedThe 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
RNA-Guided Human Genome Engineering via Cas9
Mali, P., Yang, L., Esvelt, K. M., Aach, J., Guell, M., DiCarlo, J. E., Norville, J. E., & Church, G. M. (2013) · Science · doi:10.1126/science.1232033 · Cited by 9,210
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569
Meta-Analysis of 74,046 Individuals Identifies 11 New Susceptibility Loci for Alzheimer’s Disease
(EADI), E. A. D. I., Lambert, J.-C., (GERAD), G. A. E. R. I. A. D., Alzheimer's Disease Genetic Consortium (ADGC), (CHARGE), C. F. H. A. A. R. I. G. E., Ibrahim-Verbaas, C. A., Harold, D., Naj, A. C., Sims, R., Bellenguez, C., et al. (2013) · Nature Genetics · doi:10.1038/ng.2802 · Cited by 4,336
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Rab GTPases as coordinators of vesicle traffic
Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413
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
Neurovascular 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
Pericytes regulate the blood–brain barrier
Armulik, A., Genové, G., Mäe, M., Nisancioglu, M. H., Wallgard, E., Niaudet, C., He, L., Norlin, J., Lindblom, P., Strittmatter, K., et al. (2010) · Nature · doi:10.1038/nature09522 · Cited by 2,843
Genome-wide association study identifies variants at CLU and CR1 associated with Alzheimer's disease
the European Alzheimer's Disease Initiative Investigators, Lambert, J.-C., Heath, S., Even, G., Campion, D., Sleegers, K., Hiltunen, M., Combarros, O., Zelenika, D., Bullido, M. J., et al. (2009) · Nature Genetics · doi:10.1038/ng.439 · Cited by 2,234
Pericytes are required for blood–brain barrier integrity during embryogenesis
Daneman, R., Zhou, L., Kebede, A. A., & Barres, B. A. (2010) · Nature · doi:10.1038/nature09513 · Cited by 2,128
A more efficient method to generate integration-free human iPS cells
Okita, K., Matsumura, Y., Sato, Y., Okada, A., Morizane, A., Okamoto, S., Hong, H., Nakagawa, M., Tanabe, K., Tezuka, K.-I., et al. (2011) · Nature Methods · doi:10.1038/nmeth.1591 · Cited by 2,061
Bell, R. D., Winkler, E. A., Sagare, A. P., Singh, I., LaRue, B., Deane, R., & Zlokovic, B. V. (2010) · Neuron · doi:10.1016/j.neuron.2010.09.043 · Cited by 1,448
Self-citationRAGE 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
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
Self-citationApolipoprotein E controls cerebrovascular integrity via cyclophilin A
Bell, R. D., Winkler, E. A., Singh, I., Sagare, A. P., Deane, R., Wu, Z., Holtzman, D. M., Betsholtz, C., Armulik, A., Sallstrom, J., et al. (2012) · Nature · doi:10.1038/nature11087 · Cited by 1,293
Self-citationEndocytosis and signalling: intertwining molecular networks
Sorkin, A., & von Zastrow, M. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2748 · Cited by 1,064
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
Self-citationThe Genetics of Alzheimer's Disease
Bertram, L., & Tanzi, R. E. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00008-4 · Cited by 794
The genetics of Alzheimer disease
Tanzi, R. E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006296 · Cited by 727
Grimm, D., Lee, J. S., Wang, L., Desai, T., Akache, B., Storm, T. A., & Kay, M. A. (2008) · Journal of Virology · doi:10.1128/jvi.00254-08 · Cited by 696
Cirrito, J. R. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25247 · Cited by 660
Ford, M. G. J., Pearse, B. M. F., Higgins, M. K., Vallis, Y., Owen, D. J., Gibson, A., Hopkins, C. R., Evans, P. R., & McMahon, H. T. (2001) · Science · doi:10.1126/science.291.5506.1051 · Cited by 659
The Structural Era of Endocytosis
Marsh, M., & McMahon, H. T. (1999) · Science · doi:10.1126/science.285.5425.215 · Cited by 560
Treusch, S., Hamamichi, S., Goodman, J. L., Matlack, K. E. S., Chung, C. Y., Baru, V., Shulman, J. M., Parrado, A., Bevis, B. J., Valastyan, J. S., et al. (2011) · Science · doi:10.1126/science.1213210 · Cited by 379
Rab5 is necessary for the biogenesis of the endolysosomal system in vivo
Zeigerer, A., Gilleron, J., Bogorad, R. L., Marsico, G., Nonaka, H., Seifert, S., Epstein-Barash, H., Kuchimanchi, S., Peng, C. G., Ruda, V. M., et al. (2012) · Nature · doi:10.1038/nature11133 · Cited by 362
Winkler, E. A., Bell, R. D., & Zloković, B. V. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-32 · Cited by 354
Self-citationTebar, F., Bohlander, S. K., & Sorkin, A. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.8.2687 · Cited by 320
Dreyling, M. H., Martinez-Climent, J. A., Zheng, M., Mao, J., Rowley, J. D., & Bohlander, S. K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.10.4804 · Cited by 310
Role of the MEOX2 homeobox gene in neurovascular dysfunction in Alzheimer disease
Wu, Z., Guo, H., Chow, N., Sallstrom, J., Bell, R. D., Deane, R., Brooks, A. I., Kanagala, S., Rubio, A., Sagare, A., et al. (2005) · Nature Medicine · doi:10.1038/nm1287 · Cited by 280
Self-citationNeuronal Clearance of Amyloid-β by Endocytic Receptor LRP1
Kanekiyo, T., Cirrito, J. R., Liu, C.-C., Shinohara, M., Li, J., Schuler, D. R., Shinohara, M., Holtzman, D. M., & Bu, G. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.3487-13.2013 · Cited by 280
Self-citationSRF and myocardin regulate LRP-mediated amyloid-β clearance in brain vascular cells
Bell, R. D., Deane, R., Chow, N., Long, X., Sagare, A., Singh, I., Streb, J. W., Guo, H., Rubio, A., Van Nostrand, W., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1819 · Cited by 261
Self-citationMackic, J. B., Stins, M., McComb, J. G., Calero, M., Ghiso, J., Kim, K. S., Yan, S. D., Stern, D., Schmidt, A. M., Frangione, B., et al. (1998) · Journal of Clinical Investigation · doi:10.1172/jci2029 · Cited by 242
Tian, Y., Chang, J. C., Fan, E. Y., Flajolet, M., & Greengard, P. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1315110110 · Cited by 233
Rab11 regulates exocytosis of recycling vesicles at the plasma membrane
Takahashi, S., Kubo, K., Waguri, S., Yabashi, A., Shin, H.-W., Katoh, Y., & Nakayama, K. (2012) · Journal of Cell Science · doi:10.1242/jcs.102913 · Cited by 225
LRP1 in Brain Vascular Smooth Muscle Cells Mediates Local Clearance of Alzheimer's Amyloid-β
Kanekiyo, T., Liu, C.-C., Shinohara, M., Li, J., & Bu, G. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.3987-12.2012 · Cited by 211
Self-citationThe Molecular Basis for the Endocytosis of Small R-SNAREs by the Clathrin Adaptor CALM
Miller, S. E., Sahlender, D. A., Graham, S. C., Höning, S., Robinson, M. S., Peden, A. A., & Owen, D. J. (2011) · Cell · doi:10.1016/j.cell.2011.10.038 · Cited by 192
Li, J., Kanekiyo, T., Shinohara, M., Zhang, Y., LaDu, M. J., Xu, H., & Bu, G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.420224 · Cited by 179
Self-citationXiao, Q., Gil, S.-C., Yan, P., Wang, Y., Han, S., Gonzales, E., Perez, R., Cirrito, J. R., & Lee, J.-M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.338376 · Cited by 166
Functional Vascular Endothelium Derived from Human Induced Pluripotent Stem Cells
Adams, W. J., Zhang, Y., Cloutier, J. K., Kuchimanchi, P., Newton, G. A., Sehrawat, S., Aird, W. C., Mayadas, T. N., Luscinskas, F. W., & García‐Cardeña, G. (2013) · Stem Cell Reports · doi:10.1016/j.stemcr.2013.06.007 · Cited by 166
Ando, K., Brion, J.-P., Stygelbout, V., Suain, V., Authelet, M., Dedecker, R., Chanut, A., Lacor, P., Lavaur, J., Sazdovitch, V., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1111-z · Cited by 136
Li, Y., Lu, W., Marzolo, M. P., & Bu, G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101589200 · Cited by 131
Self-citationZhu, D., Wang, Y., Singh, I., Bell, R. D., Deane, R., Zhong, Z., Sagare, A. P., Winkler, E. A., & Zloković, B. V. (2010) · Blood · doi:10.1182/blood-2010-01-262386 · Cited by 118
Self-citationZloković, B. V., Mačkić, J. B., Wang, L., McComb, J. G., & McDonough, A. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53058-1 · Cited by 117
Distribution and Expression of Picalm in Alzheimer Disease
Baig, S., Joseph, S. A., Tayler, H., Abraham, R., Owen, M. J., Williams, J., Kehoe, P. G., & Love, S. (2010) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181f52e01 · Cited by 115
A simple method for isolation and characterization of mouse brain microvascular endothelial cells
Wu, Z., Hofman, F. M., & Zloković, B. V. (2003) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(03)00206-1 · Cited by 115
Kanatsu, K., Morohashi, Y., Suzuki, M., Kuroda, H., Watanabe, T., Tomita, T., & Iwatsubo, T. (2014) · Nature Communications · doi:10.1038/ncomms4386 · Cited by 99
Nucleocytoplasmic Shuttling of Endocytic Proteins
Vecchi, M., Polo, S., Poupon, V., van de Loo, J.-W., Benmerah, A., & Fiore, P. P. D. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.7.1511 · Cited by 96
Alzheimer Disease Susceptibility Loci: Evidence for a Protein Network under Natural Selection
Raj, T., Shulman, J. M., Keenan, B. T., Chibnik, L. B., Evans, D. A., Bennett, D. A., Stranger, B. E., & Jager, P. L. D. (2012) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2012.02.022 · Cited by 84
Genetics of PICALM Expression and Alzheimer's Disease
Parikh, I. J., Fardo, D. W., & Estus, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0091242 · Cited by 73
Bushlin, I., Petralia, R. S., Wu, F., Harel, A., Mughal, M. R., Mattson, M. P., & Yao, P. J. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2471-08.2008 · Cited by 67
Basolateral targeting and microtubule-dependent transcytosis of the aquaporin-2 water channel
Yui, N., Lu, H. A. J., Chen, Y., Nomura, N., Bouley, R., & Brown, D. (2012) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00109.2012 · Cited by 65
Late-onset Alzheimer disease genetic variants in posterior cortical atrophy and posterior AD
Carrasquillo, M. M., Khan, Q. U. A., Murray, M. E., Krishnan, S., Aakre, J. A., Pankratz, V. S., Nguyen, T., Ma, L., Bisceglio, G. D., Petersen, R. C., et al. (2014) · Neurology · doi:10.1212/wnl.0000000000000335 · Cited by 61
Role of the clathrin adaptor PICALM in normal hematopoiesis and polycythemia vera pathophysiology
Ishikawa, Y., Maeda, M., Pasham, M. R., Aguet, F., Tacheva-Grigorova, S. K., Masuda, T., Yi, H. F., Lee, S.-U., Xu, J., Teruya‐Feldstein, J., et al. (2014) · Haematologica · doi:10.3324/haematol.2014.119537 · Cited by 44
Self-citationPhosphorylation of Rab11-FIP2 regulates polarity in MDCK cells
Lapierre, L. A., Avant, K. M., Caldwell, C. M., Oztan, A., Apodaca, G. L., Knowles, B. C., Roland, J. T., Ducharme, N. A., & Goldenring, J. R. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-08-0681 · Cited by 36
CALM, A Clathrin Assembly Protein, Influences Cell Surface GluR2 Abundance
Harel, A., Mattson, M. P., & Yao, P. J. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-010-8142-6 · Cited by 23
Xu, S., Edman, M. C., Kothawala, M. S., Sun, G., Chiang, L., Mircheff, A. K., Zhu, L., Okamoto, C. T., & Hamm‐Alvarez, S. F. (2011) · Journal of Cell Science · doi:10.1242/jcs.088906 · Cited by 21
Flagged first, then by citations
Cited by
Sorted by citations
The amyloid hypothesis of Alzheimer's disease at 25 years
Selkoe, D. J., & Hardy, J. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201606210 · Cited by 6,164
Blood–brain barrier breakdown in Alzheimer disease and other neurodegenerative disorders
Sweeney, M. D., Sagare, A. P., & Zlokovic, B. V. (2018) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.188 · Cited by 3,076
Self-citationAlzheimer Disease Genetics Consortium (ADGC), Kunkle, B. W., The European Alzheimer’s Disease Initiative (EADI), Cohorts for Heart and Aging Research in Genomic Epidemiology Consortium (CHARGE), Genetic and Environmental Risk in AD/Defining Genetic, P. A. E. R. F. A. D. C. (., Grenier-Boley, B., Sims, R., Bis, J. C., Damotte, V., Naj, A. C., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0358-2 · Cited by 2,946
The Neurovascular Unit Coming of Age: A Journey through Neurovascular Coupling in Health and Disease
Iadecola, C. (2017) · Neuron · doi:10.1016/j.neuron.2017.07.030 · Cited by 2,480
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
Self-citation
Metadata
- Authors
- Zhao, Z., Sagare, A. P., Ma, Q., Halliday, M. R., Kong, P., Kisler, K., Winkler, E. A., Ramanathan, A., Kanekiyo, T., Bu, G., Owens, N. C., Rege, S. V., Si, G., Ahuja, A., Zhu, D., Miller, C. A., Schneider, J. A., Maeda, M., Maeda, T., Sugawara, T., Ichida, J. K., & Zlokovic, B. V.
- Affiliations
- University of Southern California (US)
- Mayo Clinic (US)
- North Carolina Agricultural and Technical State University (US)
- Rush University Medical Center (US)
- Brigham and Women's Hospital (US)
- ORCID
- Venue
- Nature Neuroscience
- Published
- 2015-05-25
- Volume
- 18
- Issue
- 7
- Pages
- 978-987
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC4482781
- OpenAlex
- W1516940938
- Cited by
- 410
- References
- 59
- Citations by year
- 2026: 26 · 2025: 24 · 2024: 32 · 2023: 36 · 2022: 31 · 2021: 36 · 2020: 50 · 2019: 48 · 2018: 50 · 2017: 30 · 2016: 33 · 2015: 14
- FWCI
- 31.19
- Type
- journal article
- Language
- en
- Update notices
- correction (2023-11-20)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- The Scholars Repository - LLU (Loma Linda University) (submittedVersion)
- Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
- Funders
- National Institute on Aging (P01AG030128, R01AG039452, R01AG027924, R37AG023084, P50AG005142, RF1AG046205, R37AG23084, R01AG046205, R01AG035355, P50AG016574)
- National Institute of Neurological Disorders and Stroke (R37NS034467, R00-NS07743, R37NS34467, P01NS074969)
- 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 › Clinical Neurology › Cerebrospinal fluid and hydrocephalus
- Keywords
- PICALM, amyloid-beta, blood-brain barrier, transcytosis, amyloid-beta clearance, Alzheimer's disease, brain endothelium, clathrin-mediated endocytosis, LRP1, Rab5, Rab11, cognitive impairment, iPSC-derived endothelial cells, adenoviral gene transfer
- MeSH terms
- Alzheimer Disease, Animals, Blood-Brain Barrier, Capillaries, Cerebral Cortex, Endothelium, Vascular, Homeostasis, Humans, Metabolic Clearance Rate, Amyloid beta-Peptides, Mice, Knockout, Monomeric Clathrin Assembly Proteins, Pluripotent Stem Cells, Mice, Transcytosis
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