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
Flagged first, then by citations
Cited by
Sorted by citations
Items 101–200 of 410
The Ras Superfamily of Small GTPases in Non-neoplastic Cerebral Diseases
Qu, L., Pan, C., He, S., Lang, B., Gao, G.-D., Wang, X., & Wang, Y. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00121 · Cited by 84
A “multi-omics” analysis of blood–brain barrier and synaptic dysfunction in APOE4 mice
Barisano, G., Kisler, K., Wilkinson, B., Nikolakopoulou, A. M., Sagare, A. P., Wang, Y., Gilliam, W., Huuskonen, M. T., Hung, S.-T., Ichida, J. K., et al. (2022) · Journal of Experimental Medicine · doi:10.1084/jem.20221137 · Cited by 78
Self-citationAn overview of the genes and biomarkers in Alzheimer’s disease
Krishnamurthy, H. K., Jayaraman, V., Krishna, K., Wang, T., Bei, K., Changalath, C., & Rajasekaran, J. J. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102599 · Cited by 89
Cao, J., Zhong, M. B., Toro, C. A., Zhang, L., & Cai, D. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.03.016 · Cited by 82
The Links between Cardiovascular Diseases and Alzheimer's Disease
Leszek, J., Вячеславовна, М. Е., Belousov, D. M., Koutsouraki, E., Szczechowiak, K., Kobusiak−Prokopowicz, M., Mysiak, A., Diniz, B. S., Somasundaram, S. G., Kirkland, C. E., et al. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200729093724 · Cited by 93
Marino, A., Camponovo, A., Degl’Innocenti, A., Bartolucci, M., Tapeinos, C., Martinelli, C., Pasquale, D. D., Santoro, F., Mollo, V., Arai, S., et al. (2019) · Nanoscale · doi:10.1039/c9nr07976a · Cited by 78
Bryant, A. G., Li, Z., Jayakumar, R., Serrano‐Pozo, A., Woost, B., Hu, M., Woodbury, M. E., Wachter, A., Lin, G., Kwon, T., et al. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.0237-23.2023 · Cited by 84
The Blood–Brain Barrier: Composition, Properties, and Roles in Brain HealthPreprint
Lacoste, B., Prat, A., Andrade, M. F., & Gu, C. (2024) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041422 · Cited by 83
Basal lamina changes in neurodegenerative disorders
Nguyen, B., Bix, G., & Yao, Y. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00502-y · Cited by 75
Genetic Markers of Alzheimer’s Disease
Perković, M. N., & Pivac, N. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9721-0_3 · Cited by 82
PICALM Rescues Endocytic Defects Caused by the Alzheimer’s Disease Risk Factor APOE4
Narayan, P., Sienski, G., Bonner, J. M., Lin, Y.-T., Seo, J., Baru, V., Haque, A., Milo, B., Akay, L. A., Graziosi, A., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108224 · Cited by 75
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
Wu, Y., Wu, H., Zeng, J., Pluimer, B. R., Dong, S., Xie, X., Guo, X., Ge, T., Liang, X., Feng, S., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01178-7 · Cited by 76
Self-citationModulation of the Blood–Brain Barrier for Drug Delivery to Brain
Han, L. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13122024 · Cited by 78
Lam, M. A., Hemley, S. J., Najafi, E., Vella, N. G. F., Bilston, L. E., & Stoodley, M. A. (2017) · Scientific Reports · doi:10.1038/s41598-017-13455-4 · Cited by 71
Vascular and Neurogenic Rejuvenation in Aging Mice by Modulation of ASM
Park, M., Lee, J. Y., Park, K. H., Jung, I. K., Kim, K., Lee, Y., Ryu, H.-H., Jeong, Y., Kang, M., Schwaninger, M., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.09.010 · Cited by 74
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
Ando, K., Tomimura, K., Sazdovitch, V., Suain, V., Yilmaz, Z., Authelet, M., Ndjim, M., Vergara, C., Belkouch, M., Potier, M., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.05.017 · Cited by 71
Dysregulation of Rab5‐mediated endocytic pathways in Alzheimer's disease
Xu, W. L., Fang, F., Ding, J., & Wu, C. (2018) · Traffic · doi:10.1111/tra.12547 · Cited by 71
Membrane Transport across Polarized EpitheliaPreprint
Garcia-Castillo, M. D., Chinnapen, D. J. ‐., & Lencer, W. I. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a027912 · Cited by 67
Wen, X., Xiao, L., Zhong, Z., Wang, L., Li, Z., Pan, X., & Liu, Z. (2017) · Oncotarget · doi:10.18632/oncotarget.20628 · Cited by 69
Dissecting the complexities of Alzheimer disease with in vitro models of the human brain
Blanchard, J., Victor, M. B., & Tsai, L. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-021-00578-6 · Cited by 68
Magnesium Reduces Blood-Brain Barrier Permeability and Regulates Amyloid-β Transcytosis
Zhu, D., Su, Y., Fu, B. M., & Xu, H. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0896-0 · Cited by 66
Self-citationVolmar, C., Salah-Uddin, H., Janczura, K. J., Halley, P., Lambert, G., Wodrich, A. P. K., Manoah, S., Patel, N. H., Sartor, G. C., Mehta, N., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1707544114 · Cited by 67
Aging alters mRNA expression of amyloid transporter genes at the blood-brain barrier
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
Alzheimer’s disease and the autophagic-lysosomal system
Chung, K. M., Hernández, N., Sproul, A. A., & Yu, W. H. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2018.05.017 · Cited by 63
Cao, Y., Zhao, L.-W., Chen, Z.-X., & Li, S.-H. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1430465 · Cited by 65
Bharadwaj, P., Solomon, T., Malajczuk, C. J., Mancera, R. L., Howard, M. J., Arrigan, D. W. M., Newsholme, P., & Martins, R. N. (2018) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2018.03.015 · Cited by 63
Presynaptic endocytic factors in autophagy and neurodegeneration
Tehran, D. A., Kuijpers, M., & Haucke, V. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.12.018 · Cited by 58
A New Hypothesis for Alzheimer’s Disease: The Lipid Invasion Model
Rudge, J. D. (2022) · Journal of Alzheimer's Disease Reports · doi:10.3233/adr-210299 · Cited by 58
Liang, X., Fa, W., Wang, N., Peng, Y., Liu, C., Zhu, M., Tian, N., Wang, Y., Han, X., Qiu, C., et al. (2022) · Aging Cell · doi:10.1111/acel.13748 · Cited by 60
Picalm rs3851179 variant confers susceptibility to alzheimer’s disease in chinese population
Liu, G., Xu, Y., Jiang, Y., Zhang, L., Feng, R., & Jiang, Q. (2017) · Molecular Neurobiology · doi:10.1007/s12035-016-9886-2 · Cited by 57
Babos, K. N., Galloway, K. E., Kisler, K., Zitting, M., Li, Y., Shi, Y., Quintino, B., Chow, R. H.-P., Zloković, B. V., & Ichida, J. K. (2019) · Cell stem cell · doi:10.1016/j.stem.2019.08.005 · Cited by 58
Self-citationTargeting Alzheimer’s disease with multimodal polypeptide-based nanoconjugates
Duro‐Castaño, A., Borrás, C., Herranz‐Pérez, V., Blanco-Gandía, M. C., Conejos‐Sánchez, I., Armiñán, A., Mas‐Bargues, C., Inglés, M., Miñarro, J., Rodríguez‐Arias, M., et al. (2021) · Science Advances · doi:10.1126/sciadv.abf9180 · Cited by 58
Vascular Contributions to Cognitive Impairment and Dementia
Madigan, J. B., Wilcock, D. M., & Hainsworth, A. H. (2016) · Stroke · doi:10.1161/strokeaha.116.012066 · Cited by 56
Blood-Brain Barrier Integrity and Clearance of Amyloid-β from the BBB
Cockerill, I., Oliver, J.-A. N., Xu, H., Fu, B. M., & Zhu, D. (2018) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-96445-4_14 · Cited by 60
Self-citationAP‐2 reduces amyloidogenesis by promoting BACE1 trafficking and degradation in neurons
Bera, S., Camblor‐Perujo, S., Barca, E. C., Negrete‐Hurtado, A., Racho, J., Bruyckere, E. D., Wittich, C., Ellrich, N., Martins, S., Adjaye, J., et al. (2020) · EMBO Reports · doi:10.15252/embr.201947954 · Cited by 55
Zou, C., Mifflin, L., Hu, Z., Zhang, T., Shan, B., Wang, H., Xing, X., Zhu, H., Adiconis, X., Levin, J. Z., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108447 · Cited by 61
Dong, H. K., Gim, J., Yeo, S. H., & Kim, H. (2016) · Gene · doi:10.1016/j.gene.2016.10.022 · Cited by 57
Gao, X., Xu, J., Yao, T., Liu, X., Zhang, H., & Zhan, C. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114362 · Cited by 56
Vascular and Metabolic Factors in Alzheimer’s Disease and Related Dementias: Introduction
Iadecola, C. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0319-y · Cited by 59
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].”
BackgroundRasmussen, K. L., Nordestgaard, B. G., Frikke‐Schmidt, R., & Nielsen, S. F. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.07.223 · Cited by 57
The 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
Dapsone protects brain microvascular integrity from high-fat diet induced LDL oxidation
Zhan, R., Zhao, M., Zhou, T., Chen, Y., Yu, W., Zhao, L., Zhang, T., Wang, H., Yang, H. M., Jin, Y., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0739-y · Cited by 53
Vesicular Transport Machinery in Brain Endothelial Cells: What We Know and What We Do not
Tóth, A. E., Holst, M. R., & Nielsen, M. S. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200212113421 · Cited by 56
Ikonomović, M. D., Mi, Z., & Abrahamson, E. E. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.11.003 · Cited by 53
Zhao, F. L., Deng, J., Xu, X., Cao, F., Lu, K., Li, D., Cheng, X., Wang, X., & Zhao, Y. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1203-8 · Cited by 52
The Alzheimer's disease risk factor CD2AP maintains blood–brain barrier integrity
Cochran, J. N., Rush, T., Buckingham, S. C., & Roberson, E. D. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv371 · Cited by 52
High Concentrations of Rosiglitazone Reduce mRNA and Protein Levels of LRP1 in HepG2 Cells
Rondón-Ortiz, A. N., Lino Cardenas, C. L., Martínez-Málaga, J., Gonzales-Urday, A. L., Gugnani, K. S., Böhlke, M., Maher, T. J., & Pino-Figueroa, A. J. (2017) · Frontiers in Pharmacology · doi:10.3389/fphar.2017.00772 · Cited by 51
Meta-analysis of the Association between Alzheimer Disease and Variants in GAB2, PICALM, and SORL1
Wang, Z., Lei, H., Zheng, M., Li, Y., Cui, Y., & Hao, F. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9546-y · Cited by 49
Impact of late-onset Alzheimer’s genetic risk factors on beta-amyloid endocytic production
Almeida, C. G., Mirfakhar, F. S., Perdigão, C., & Burrinha, T. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2825-9 · Cited by 53
Ullah, R., & Lee, E. J. (2023) · Experimental Neurobiology · doi:10.5607/en23014 · Cited by 51
Patel, R., & Al-Ahmad, A. J. (2016) · Fluids and Barriers of the CNS · doi:10.1186/s12987-016-0030-5 · Cited by 48
Natale, F., Fusco, S., & Grassi, C. (2022) · Translational Neurodegeneration · doi:10.1186/s40035-022-00326-w · Cited by 49
Transcriptional Networks of Microglia in Alzheimer’s Disease and Insights into Pathogenesis
Chew, G., & Petretto, E. G. (2019) · Genes · doi:10.3390/genes10100798 · Cited by 46
Jia, Y., Wang, N., Zhang, Y., Xue, D., Lou, H., & Liu, X. (2020) · Aging and Disease · doi:10.14336/ad.2019.0519 · Cited by 50
Alcendor, D. J. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9051490 · Cited by 47
Chen, J., Xiang, P., Duro-Castano, A., Cai, H., Guo, B., Liu, X., Yu, Y., Lui, S., Luo, K., Ke, B., et al. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02426-1 · Cited by 45
Haglund, A., Zuber, V., Abouzeid, M., Yang, Y., Ko, J. H., Wiemann, L., Otero‐Jimenez, M., Muhammed, L., Feleke, R., Nott, A., et al. (2025) · Nature Genetics · doi:10.1038/s41588-024-02050-9 · Cited by 46
Rasmussen, I. J., Tybjærg‐Hansen, A., Rasmussen, K. L., Nordestgaard, B. G., & Frikke‐Schmidt, R. (2019) · European Journal of Epidemiology · doi:10.1007/s10654-019-00498-2 · Cited by 46
Genetic risk factors for Alzheimer disease: emerging roles of microglia in disease pathomechanisms
Takatori, S., Wang, W., Iguchi, A., & Tomita, T. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-030-05542-4_5 · Cited by 44
Deák, F., Freeman, W. M., Ungvari, Z. I., Csiszár, A., & Sonntag, W. E. (2015) · The Journals of Gerontology Series A · doi:10.1093/gerona/glv206 · Cited by 45
Endocytic Adaptor Proteins in Health and Disease: Lessons from Model Organisms and Human Mutations
Azarnia Tehran, D., López-Hernández, T., & Maritzen, T. (2019) · Cells · doi:10.3390/cells8111345 · Cited by 44
Transport of Alzheimer’s associated amyloid-β catalyzed by P-glycoprotein
McCormick, J. W., McCormick, L. A., (党陈), G. C., Vogel, P. D., & Wise, J. G. (2021) · PLoS ONE · doi:10.1371/journal.pone.0250371 · Cited by 43
Peptide Mediated Brain Delivery of Nano- and Submicroparticles: A Synergistic Approach
McCully, M., Sánchez‐Navarro, M., Teixidò, M., & Giralt, E. (2018) · Current Pharmaceutical Design · doi:10.2174/1381612824666171201115126 · Cited by 45
Griffin, E. F., Scopel, S. E., Stephen, C. A., Holzhauer, A. C., Vaji, M. A., Tuckey, R. A., Berkowitz, L. A., Caldwell, K. A., & Caldwell, G. A. (2019) · Disease Models & Mechanisms · doi:10.1242/dmm.037218 · Cited by 48
Petralla, S., Panayotova, M., Franchina, E., Fricker, G., & Puris, E. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16070948 · Cited by 46
Wu, Q., Yuan, X., Bai, J., Han, R., Li, Z., Zhang, H., & Xiu, R. (2019) · Aging · doi:10.18632/aging.102171 · Cited by 44
Picalm reduction exacerbates tau pathology in a murine tauopathy model
Ando, K., Decker, R. D., Vergara, C., Yilmaz, Z., Mansour, S., Suain, V., Sleegers, K., de Fisenne, M.-A., Houben, S., Potier, M., et al. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02125-x · Cited by 46
Advanced Human BBB‐on‐a‐Chip: A New Platform for Alzheimer's Disease Studies
Yoon, J., Kim, J., Shah, Z., Awasthi, A., Mahajan, A., & Kim, Y. (2021) · Advanced Healthcare Materials · doi:10.1002/adhm.202002285 · Cited by 45
Raut, S., Patel, R., & Al-Ahmad, A. J. (2021) · Fluids and Barriers of the CNS · doi:10.1186/s12987-020-00235-y · Cited by 42
Uncovering the impact of noncoding variants in neurodegenerative brain diseases
Frydas, A., Wauters, E., van der Zee, J., & Broeckhoven, C. V. (2021) · Trends in Genetics · doi:10.1016/j.tig.2021.08.010 · Cited by 44
Afsar, A., Castro, M. D. C. C., Soladogun, A. S., & Li, Z. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24087258 · Cited by 45
Wang, X., Chen, S., Xia, X., Du, Y., Wei, Y., Yang, W., Zhang, Y., Song, Y., Lei, T., Huang, Q., et al. (2024) · Advanced Materials · doi:10.1002/adma.202411061 · Cited by 43
Vascular 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
Ramos, C. J., & Antonetti, D. A. (2017) · Tissue Barriers · doi:10.1080/21688370.2017.1339768 · Cited by 42
Mechanisms of neuronal survival safeguarded by endocytosis and autophagy
Overhoff, M., Bruyckere, E. D., & Kononenko, N. L. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15194 · Cited by 40
Unveiling the Complex Role of Exosomes in Alzheimer’s Disease
Sun, M., & Chen, Z. (2024) · Journal of Inflammation Research · doi:10.2147/jir.s466821 · Cited by 39
Lü, M., Williamson, N. R., Mishra, A., Michel, C. H., Kaminski, C. F., Tunnacliffe, A., & Schierle, G. S. K. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004511 · Cited by 41
Mazzitelli, S., Filipello, F., Rasile, M., Lauranzano, E., Cucuzza, C. S., Tamborini, M., Pozzi, D., Barajon, I., Toni Giorgino, A., Natalello, A., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0381-9 · Cited by 38
Wren, M. C., Lashley, T., Årstad, E., & Sander, K. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0535-z · Cited by 43
Targeting Beta-Amyloid at the CSF: A New Therapeutic Strategy in Alzheimer’s Disease
Menéndez‐González, M., Padilla-Zambrano, H., Alvarez, G., Capetillo‐Zarate, E., Tomás‐Zapico, C., & Costa, A. D. D. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00100 · Cited by 38
Modelling Sporadic Alzheimer’s Disease Using Induced Pluripotent Stem Cells
Rowland, H. A., Hooper, N. M., & Kellett, K. A. B. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2663-z · Cited by 38
Lee, J., Lee, H., Lee, H. G., Shin, M., Shin, M.-G., Seo, J., Lee, E. J., Park, S. A., & Park, S. (2023) · Nature Communications · doi:10.1038/s41467-023-44319-3 · Cited by 37
Wu, H., Brown, E. V., Acharya, N. K., Appelt, D. M., Marks, A., Nagele, R. G., & Venkataraman, V. (2016) · Brain Research · doi:10.1016/j.brainres.2016.02.026 · Cited by 37
A lymphatic waste-disposal system implicated in Alzheimer’s disease
Sweeney, M. D., & Zloković, B. V. (2018) · Nature · doi:10.1038/d41586-018-05763-0 · Cited by 35
Role of Rab GTPases in Alzheimer’s Disease
Zhang, X., Huang, T. Y., Yancey, J., Luo, H., & Zhang, Y. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00387 · Cited by 37
Hsu, H.-W., Rodríguez‐Ortiz, C. J., Lim, S., Zumkehr, J., Kilian, J., Vidal, J., & Kitazawa, M. (2019) · Toxicological Sciences · doi:10.1093/toxsci/kfz084 · Cited by 36
Fujikura, M., Iwahara, N., Hisahara, S., Kawamata, J., Matsumura, A., Yokokawa, K., Saito, T., Manabe, T., Matsushita, T., Suzuki, S., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180904 · Cited by 36
Relation between plasma and brain lipids
Wellington, C. L., & Frikke-Schmidt, R. (2016) · Current Opinion in Lipidology · doi:10.1097/mol.0000000000000291 · Cited by 33
Non-coding RNA influences in dementia
Ayers, D., & Scerri, C. (2018) · Non-coding RNA Research · doi:10.1016/j.ncrna.2018.09.002 · Cited by 32
Sharma, H. S., Muresanu, D. F., Nozari, A., Lafuente, J. V., Tian, Z. R., Ozkızılcık, A., Manzhulo, I., Mössler, H., & Sharma, A. (2019) · Progress in brain research · doi:10.1016/bs.pbr.2019.03.009 · Cited by 33
The Blood-Brain Barrier in Alzheimer’s Disease
Storck, S. E., Hartz, A. M. S., & Pietrzik, C. U. (2020) · Handbook of experimental pharmacology · doi:10.1007/164_2020_418 · Cited by 31
Endocytosis and Alzheimer’s disease
Zadka, Ł., Sochocka, M., Hachiya, N., Chojdak-Łukasiewicz, J., Dzięgiel, P., Piasecki, E., & Leszek, J. (2023) · GeroScience · doi:10.1007/s11357-023-00923-1 · Cited by 33
Zheng, Y., & Wyman, I. (2016) · Polymers · doi:10.3390/polym8050198 · Cited by 33
Griffin, E. F., Yan, X., Caldwell, K. A., & Caldwell, G. A. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddy308 · Cited by 34
Metabolite Clearance During Wakefulness and Sleep
Hladky, S. B., & Barrand, M. A. (2017) · Handbook of experimental pharmacology · doi:10.1007/164_2017_37 · Cited by 36
Neurovascular dysfunction in dementia – human cellular models and molecular mechanisms
Parkes, I., Chintawar, S., & Cader, M. Z. (2018) · Clinical Science · doi:10.1042/cs20160720 · Cited by 34
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
