The blood-brain barrier
Open accessAbstract
Blood vessels are critical to deliver oxygen and nutrients to all of the tissues and organs throughout the body. The blood vessels that vascularize the central nervous system (CNS) possess unique properties, termed the blood-brain barrier, which allow these vessels to tightly regulate the movement of ions, molecules, and cells between the blood and the brain. This precise control of CNS homeostasis allows for proper neuronal function and also protects the neural tissue from toxins and pathogens, and alterations of these barrier properties are an important component of pathology and progression of different neurological diseases. The physiological barrier is coordinated by a series of physical, transport, and metabolic properties possessed by the endothelial cells (ECs) that form the walls of the blood vessels, and these properties are regulated by interactions with different vascular, immune, and neural cells. Understanding how these different cell populations interact to regulate the barrier properties is essential for understanding how the brain functions during health and disease.
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
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?
CNS vessels at the levels of arteriole-capillary-venules are non-fenestrated and continuous and control the exchange of molecules, ions and cells between the blood and the brain.
“CNS vessels, at the levels of arteriole–capillary–venules, are non-fenestrated and continuous; they are able to control the exchange of molecules, ions and cells between the blood and the brain [1].”
From Nanoemulsions for “Nose-to-Brain” Drug Delivery (2019) · cites this paper as [1]
The Blood-Brain Barrier section states that CNS vessels are continuous and nonfenestrated and tightly regulate movement of molecules, ions, and cells between blood and the CNS. It defines the relevant microvasculature as capillaries and postcapillary venules, however, rather than explicitly extending those barrier properties to arterioles. The Endothelial Cells section also identifies fenestrated CNS capillaries in circumventricular organs, so the statement is too broad if read as applying to every CNS vessel. (LLM, conf=0.83)
Experimental — accuracy not yet measuredCarrier-mediated transport enables carbohydrates, amino acids, monocarboxylic acids, hormones, fatty acids, nucleotides, inorganic ions, amines, choline, and vitamins to cross the blood-brain barrier via substrate-specific transporters.
“Carrier-mediated transport (CMT) enables solutes such as carbohydrates, amino acids (AA), monocarboxylic acids, hormones, fatty acids, nucleotides, inorganic ions, amines, choline, and vitamins to cross the BBB via substrate-specific transporters (2, 128, 460, 682, 692, 693).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [128]
The transporters passage (section labeled “Tight Junctions”; page unavailable) describes substrate-specific solute carriers for glucose, lactate and pyruvate, and amino acids, supporting the claim for carbohydrates, monocarboxylic acids, and amino acids. The copy does not establish carrier-mediated BBB crossing for the full additional list, including hormones, fatty acids, nucleotides, choline, and vitamins; its discussion of ion transport does not establish that entire claim either. (LLM, conf=0.88)
Experimental — accuracy not yet measuredSodium-dependent multivitamin transporter (SMVT) transports multivitamins from blood to brain.
“and sodium-dependent multivitamin transporter (SMVT) transports multivitamins from blood-to-brain (2, 128, 460, 682).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [128]
The Endothelial Cells and Tight Junctions sections state that nutrient transporters deliver specific nutrients from blood into the CNS. They do not identify sodium-dependent multivitamin transporter (SMVT) or say that it transports multivitamins, so the transporter-specific claim is unsupported by this copy. (LLM, conf=0.78)
Experimental — accuracy not yet measuredCollagen IV and laminin localization matches in vivo organization where pericytes are embedded within the basement membrane.
“matches in vivo organization where pericytes are embedded within the basement membrane [1].”
From Role of iPSC-derived pericytes on barrier function of iPSC-derived brain microvascular endothelial cells in 2D and 3D (2019) · cites this paper as [1]
The blood-brain barrier is an active interface that controls the CNS microenvironment, communicates with CNS cells, responds to pathological conditions and can become a cause of disease progression.
“BBB is not only a cellular self-defense barrier but also an active interface that strictly controls the CNS microenvironment, allowing its normal neuronal functions. BBB cells are able to communicate with CNS cells and they adapt their behavior to the needs of the CNS, responding to pathological conditions and sometimes becoming a cause of the progression of the disease [1].”
From Nanoemulsions for “Nose-to-Brain” Drug Delivery (2019) · cites this paper as [1]
The microvasculature of the central nervous system is defined as the blood-brain barrier because it isolates the brain from the rest of the body.
“The microvasculature of the central nervous system (CNS) is defined as a blood–brain barrier (BBB) because it isolates the brain from the remaining part of the body.”
From Nanoemulsions for “Nose-to-Brain” Drug Delivery (2019) · cites this paper as [1]
The blood-brain barrier protects the brain from toxic substances and controls and restricts the entry of therapeutic agents.
“The blood–brain barrier (BBB) plays a fundamental role in protecting the brain from toxic substances and therefore also controls and restricts the entry of therapeutic agents.”
From Nanoemulsions for “Nose-to-Brain” Drug Delivery (2019) · cites this paper as [1]
The barrier structure of the BBB depends on specific properties of brain endothelial cells, which are polarized, held together by tight junctions that limit paracellular flux of solutes and restrict vesicle-mediated transcellular transport.
“The barrier structure of BBB depends on the specific properties of the brain endothelial cells (BECs) that constitute the walls of the blood vessels. BECs are different from endothelial cells of non-neural tissues—they are polarized cells, held together by tight junctions that strongly limit the paracellular flux of solutes (molecules and ions) and restrict vesicle-mediated transcellular transport”
From Nanoemulsions for “Nose-to-Brain” Drug Delivery (2019) · cites this paper as [1]
The blood-brain barrier protects the CNS from pathogens, toxins and external agents.
“This strong barrier capacity allows the BBB to protect the CNS from pathogens, toxins and external agents.”
From Nanoemulsions for “Nose-to-Brain” Drug Delivery (2019) · cites this paper as [1]
Brain endothelial cells express efflux and influx transporters, and P-glycoprotein activity has been associated with CNS diseases such as drug-resistant tumors and epilepsy.
“Among efflux transporters, P-glycoprotein plays an important role, as its activity has been associated with diseases of the CNS such as drug-resistant tumors and epilepsy [1].”
From Nanoemulsions for “Nose-to-Brain” Drug Delivery (2019) · cites this paper as [1]
Brain endothelial transport systems regulate molecular exchanges between blood and brain and between brain and blood.
“brain endothelial transport systems regulate molecular exchanges between blood-and-brain and brain-and-blood (2, 128, 460, 682, 692, 693).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [128]
The GLUT1 uniporter transports glucose down the concentration gradient.
“The GLUT1 uniporter transports glucose, the key energy metabolite for the CNS, down the concentration gradient (128, 460).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [128]
Plasma membrane monoamine transporter (PMAT) transports organic cations from brain to blood.
“Specifically, plasma membrane monoamine transporter (PMAT) transports organic cations from brain-to-blood, choline transporter like protein type 1 (CTL1) transports choline bidirectionally across the BBB, and sodium-dependent multivitamin transporter (SMVT) transports multivitamins from blood-to-brain (2, 128, 460, 682).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [128]
The Endothelial Cells and Tight Junctions passages describe transport toward the blood in general, but do not identify PMAT or say that it transports organic cations. Searches for PMAT, plasma membrane monoamine transporter, and organic cations found no passage addressing that specific claim; page numbers were not available in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredCholine transporter like protein type 1 (CTL1) transports choline bidirectionally across the blood-brain barrier.
“choline transporter like protein type 1 (CTL1) transports choline bidirectionally across the BBB, and sodium-dependent multivitamin transporter (SMVT) transports multivitamins from blood-to-brain (2, 128, 460, 682).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [128]
The transporter discussion (Tight Junctions; page unavailable) describes nutrient transport across the BBB but does not identify CTL1, choline, or bidirectional choline transport. Searches for CTL1 and choline found no passage addressing the claim. (LLM, conf=0.75)
Experimental — accuracy not yet measuredSepsis triggers a systemic inflammatory response releasing endotoxins such as LPS and proinflammatory cytokines such as IL-6, IL-1β, NO, and ROS, leading to cellular dysfunction and BBB integrity impairment, and neuronal degeneration and brain edema exacerbate neuroinflammation.
“Sepsis triggers a systemic inflammatory response, releasing endotoxins such as lipopolysaccharide (LPS) and proinflammatory cytokines such as IL-6, IL-1 β, NO, and ROS. This response leads to cellular dysfunction and BBB integrity impairment, and neuronal degeneration and brain edema exacerbate neuroinflammation (Daneman & Prat, 2015; Michinaga & Koyama, 2015).”
From The modulatory effects of gut microbes and metabolites on blood-brain barrier integrity and brain function in sepsis-associated encephalopathy (2023) · cites this paper as Daneman & Prat, 2015
Bacterial products and metabolites can pass the blood-brain barrier and shape CNS development and functions and the genesis of certain diseases.
“Among the molecules that can pass the BBB are also bacterial products and metabolites shaping not only the CNS development and functions (6, 15) but also the genesis of certain diseases (33–42).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [34]
Early experiments using germ-free or specific pathogen-free mice treated with antibiotics to reduce microbial diversity showed that several neurological problems occur in mice with reduced or lack of proper mature gut microbiota.
“Early experiments using germ-free (GF) or specific pathogen-free (SPF) mice treated with antibiotics, to reduce the microbial diversity within the intestine, showed that several neurological problems occur in mice with reduced or lack of proper mature gut microbiota (7, 10, 14, 15, 34, 80, 81).”
From The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology (2020) · cites this paper as [34]
Endothelial cells comprise the BBB and are highly selective in filtering the content that is available to neurons.
“Endothelial cells comprise the BBB and are highly selective in consequently filtering the content that is available to neurons [121].”
From Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology (2021) · cites this paper as [121]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Astrocyte-endothelial interactions at the blood-brain barrier
Abbott, N. J., Rönnbäck, L., & Hansson, E. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1824 · Cited by 5,595 · see citing works
Fate Mapping Analysis Reveals That Adult Microglia Derive from Primitive Macrophages
Ginhoux, F., Greter, M., Leboeuf, M., Nandi, S., See, P., Gokhan, S., Mehler, M. F., Conway, S. J., Ng, L. G., Stanley, E. R., et al. (2010) · Science · doi:10.1126/science.1194637 · Cited by 5,175 · see citing works
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 · see citing works
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 · see citing works
Pericytes: Developmental, Physiological, and Pathological Perspectives, Problems, and Promises
Armulik, A., Genové, G., & Betsholtz, C. (2011) · Developmental Cell · doi:10.1016/j.devcel.2011.07.001 · Cited by 2,653 · see citing works
FINE STRUCTURAL LOCALIZATION OF A BLOOD-BRAIN BARRIER TO EXOGENOUS PEROXIDASE
Reese, T. S., & Karnovsky, M. J. (1967) · The Journal of Cell Biology · doi:10.1083/jcb.34.1.207 · Cited by 2,629 · see citing works
Glial and neuronal control of brain blood flow
Attwell, D., Buchan, A. M., Charpak, S., Lauritzen, M., MacVicar, B. A., & Newman, E. A. (2010) · Nature · doi:10.1038/nature09613 · Cited by 2,511 · see citing works
JUNCTIONS BETWEEN INTIMATELY APPOSED CELL MEMBRANES IN THE VERTEBRATE BRAIN
Brightman, M., & Reese, T. S. (1969) · The Journal of Cell Biology · doi:10.1083/jcb.40.3.648 · Cited by 2,457 · see citing works
Schinkel, A. H., Smit, J., van Tellingen, O., Beijnen, J. H., Wagenaar, E., van Deemter, L., Mol, C. A. A. M., van der Valk, M. A., Robanus-Maandag, E. C., Riele, H. T., et al. (1994) · Cell · doi:10.1016/0092-8674(94)90212-7 · Cited by 2,284 · see citing works
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 · see citing works
Self-citationSize-selective loosening of the blood-brain barrier in claudin-5–deficient mice
Nitta, T., Hata, M., Gotoh, S., Seo, Y., Sasaki, H., Hashimoto, N., Furuse, M., & Tsukita, S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302070 · Cited by 1,917 · see citing works
Capillary pericytes regulate cerebral blood flow in health and disease
Hall, C. N., Reynell, C., Gesslein, B., Hamilton, N. B., Mishra, A., Sutherland, B. A., O’Farrell, F. M., Buchan, A. M., Lauritzen, M., & Attwell, D. (2014) · Nature · doi:10.1038/nature13165 · Cited by 1,870 · see citing works
The ageing systemic milieu negatively regulates neurogenesis and cognitive function
Villeda, S. A., Luo, J., Mosher, K. I., Zou, B., Britschgi, M., Bieri, G., Stan, T. M., Fainberg, N., Ding, Z., Eggel, A., et al. (2011) · Nature · doi:10.1038/nature10357 · Cited by 1,763 · see citing works
Kebir, H., Kreymborg, K., Ifergan, I., Dodelet-Devillers, A., Cayrol, R., Bernard, M., Giuliani, F., Arbour, N., Becher, B., & Prat, A. (2007) · Nature Medicine · doi:10.1038/nm1651 · Cited by 1,759 · see citing works
Self-citationCordon‐Cardo, C., O’Brien, J. P., Casals, D., Rittmann-Grauer, L., Biedler, J. L., Melamed, M. R., & Bertino, J. R. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.2.695 · Cited by 1,750 · see citing works
Phenotypic Heterogeneity of the Endothelium
Aird, W. C. (2007) · Circulation Research · doi:10.1161/01.res.0000255691.76142.4a · Cited by 1,744 · see citing works
Local self-renewal can sustain CNS microglia maintenance and function throughout adult life
Ajami, B., Bennett, J. L., Krieger, C., Tetzlaff, W., & Rossi, F. M. V. (2007) · Nature Neuroscience · doi:10.1038/nn2014 · Cited by 1,643 · see citing works
Astrocytes induce blood–brain barrier properties in endothelial cells
Janzer, R. C., & RAFF, M. C. (1987) · Nature · doi:10.1038/325253a0 · Cited by 1,634 · see citing works
Claudin-based tight junctions are crucial for the mammalian epidermal barrier
Furuse, M., Hata, M., Furuse, K., Yoshida, Y., Haratake, A., Sugitani, Y., Noda, T., Kubo, A., & Tsukita, S. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110122 · Cited by 1,512 · see citing works
Perivascular microglial cells of the CNS are bone marrow-derived and present antigen in vivo
Hickey, W. F., & Kimura, H. (1988) · Science · doi:10.1126/science.3276004 · Cited by 1,466 · see citing works
Martín-Padura, I., Lostaglio, S., Schneemann, M., Williams, L., Romano, M., Fruscella, P., Panzeri, C., Stoppacciaro, A., Ruco, L., Villa, A., et al. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.1.117 · Cited by 1,387 · see citing works
Schinkel, A. H., Wagenaar, E., Mol, C. A. A. M., & van Deemter, L. (1996) · Journal of Clinical Investigation · doi:10.1172/jci118699 · Cited by 1,265 · see citing works
Phenotypic Heterogeneity of the Endothelium
Aird, W. C. (2007) · Circulation Research · doi:10.1161/01.res.0000255690.03436.ae · Cited by 1,252 · see citing works
Complex Phenotype of Mice Lacking Occludin, a Component of Tight Junction Strands
Saitou, M., Furuse, M., Sasaki, H., Schulzke, J.-D., Fromm, M., Takano, H., Noda, T., & Tsukita, S. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.12.4131 · Cited by 1,195 · see citing works
Bidirectional control of CNS capillary diameter by pericytes
Peppiatt, C. M., Howarth, C., Mobbs, P., & Attwell, D. (2006) · Nature · doi:10.1038/nature05193 · Cited by 1,150 · see citing works
CLAUDINS AND EPITHELIAL PARACELLULAR TRANSPORT
Itallie, C. M. V., & Anderson, J. M. (2005) · Annual Review of Physiology · doi:10.1146/annurev.physiol.68.040104.131404 · Cited by 1,123 · see citing works
Schinkel, A. H., Wagenaar, E., van Deemter, L., Mol, C. A. A. M., & Borst, P. (1995) · Journal of Clinical Investigation · doi:10.1172/jci118214 · Cited by 1,108 · see citing works
Young blood reverses age-related impairments in cognitive function and synaptic plasticity in mice
Villeda, S. A., Plambeck, K. E., Middeldorp, J., Castellano, J. M., Mosher, K. I., Luo, J., Smith, L. K., Bieri, G., Lin, K., Berdnik, D., et al. (2014) · Nature Medicine · doi:10.1038/nm.3569 · Cited by 1,081 · see citing works
Autocrine VEGF Signaling Is Required for Vascular Homeostasis
Lee, S., Chen, T. T., Barber, C. L., Jordan, M. C., Murdock, J., Desai, S. P., Ferrara, N., Nagy, A., Roos, K. P., & Iruela‐Arispe, M. L. (2007) · Cell · doi:10.1016/j.cell.2007.06.054 · Cited by 1,046 · see citing works
Vascular and Neurogenic Rejuvenation of the Aging Mouse Brain by Young Systemic Factors
Katsimpardi, L., Litterman, N. K., Schein, P. A., Miller, C. M., Loffredo, F. S., Wojtkiewicz, G. R., Chen, J. W., Lee, R. T., Wagers, A. J., & Rubin, L. L. (2014) · Science · doi:10.1126/science.1251141 · Cited by 1,037 · see citing works
Furuse, M., Sasaki, H., Fujimoto, K., & Tsukita, S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.2.391 · Cited by 969 · see citing works
The impact of the extracellular matrix on inflammation
Sorokin, L. (2010) · Nature reviews. Immunology · doi:10.1038/nri2852 · Cited by 918 · see citing works
Balda, M. S., Whitney, J. A., Flores, C., González, S., Cereijido, M., & Matter, K. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.134.4.1031 · Cited by 876 · see citing works
Vascular Development in the Retina and Inner Ear
Xu, Q., Wang, Y., Dabdoub, A., Smallwood, P. M., Williams, J., Woods, C., Kelley, M. W., Jiang, L., Tasman, W., Zhang, K., et al. (2004) · Cell · doi:10.1016/s0092-8674(04)00216-8 · Cited by 875 · see citing works
Blood-brain barrier active efflux transporters: ATP-binding cassette gene family
Löscher, W., & Potschka, H. (2004) · NeuroRx · doi:10.1602/neurorx.2.1.86 · Cited by 873 · see citing works
Morita, K., Sasaki, H., Furuse, M., & Tsukita, S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.1.185 · Cited by 866 · see citing works
Rosenberg, G. A., Estrada, E. Y., & Dencoff, J. E. (1998) · Stroke · doi:10.1161/01.str.29.10.2189 · Cited by 861 · see citing works
The Hedgehog Pathway Promotes Blood-Brain Barrier Integrity and CNS Immune Quiescence
Alvarez, J. I., Dodelet-Devillers, A., Kebir, H., Ifergan, I., Fabre, P. J., Terouz, S., Sabbagh, M., Wosik, K., Bourbonnière, L., Bernard, M., et al. (2011) · Science · doi:10.1126/science.1206936 · Cited by 845 · see citing works
Self-citationVivo, D. C. D., Trifiletti, R. R., Jacobson, R. I., Ronen, G. M., Behmand, R. A., & Harik, S. I. (1991) · New England Journal of Medicine · doi:10.1056/nejm199109053251006 · Cited by 801 · see citing works
Wnt/β-catenin signaling controls development of the blood–brain barrier
Liebner, S., Corada, M., Bangsow, T., Babbage, J., Taddei, A., Czupalla, C. J., Reis, M., Felici, A., Wolburg, H., Fruttiger, M., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200806024 · Cited by 793 · see citing works
The blood–brain and the blood–cerebrospinal fluid barriers: function and dysfunction
Engelhardt, B., & Sorokin, L. M. (2009) · Seminars in Immunopathology · doi:10.1007/s00281-009-0177-0 · Cited by 792 · see citing works
The blood–brain barrier in health and disease
Daneman, R. (2012) · Annals of Neurology · doi:10.1002/ana.23648 · Cited by 756 · see citing works
Self-citationWnt/β-catenin signaling is required for CNS, but not non-CNS, angiogenesis
Daneman, R., Agalliu, D., Zhou, L., Kuhnert, F., Kuo, C. J., & Barres, B. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805165106 · Cited by 753 · see citing works
Self-citationDevelopmental Basis of Vascular Smooth Muscle Diversity
Majesky, M. W. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.141069 · Cited by 737 · see citing works
Astrocyte-derived VEGF-A drives blood-brain barrier disruption in CNS inflammatory disease
Argaw, A. T., Asp, L., Zhang, J., Navrazhina, K., Pham, T., Mariani, J. N., Mahase, S., Dutta, D. J., Seto, J., Kramer, E. G., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60842 · Cited by 733 · see citing works
Furuse, M., Furuse, K., Sasaki, H., & Tsukita, S. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.2.263 · Cited by 719 · see citing works
Knowland, D., Arac, A., Sekiguchi, K. J., Hsu, M., Lutz, S. E., Perrino, J., Steinberg, G. K., Barres, B. A., Nimmerjahn, A., & Agalliu, D. (2014) · Neuron · doi:10.1016/j.neuron.2014.03.003 · Cited by 703 · see citing works
CNS Myelin and Sertoli Cell Tight Junction Strands Are Absent in Osp/Claudin-11 Null Mice
Gow, A., Southwood, C. M., Li, J. S., Pariali, M., Riordan, G. P., Brodie, S. E., Danias, J., Bronstein, J. M., Kachar, B., & Lazzarini, R. A. (1999) · Cell · doi:10.1016/s0092-8674(00)81553-6 · Cited by 699 · see citing works
Stewart, P. A., & Wiley, M. J. (1981) · Developmental Biology · doi:10.1016/0012-1606(81)90382-1 · Cited by 684 · see citing works
VEGF-mediated disruption of endothelial CLN-5 promotes blood-brain barrier breakdown
Argaw, A. T., Gurfein, B. T., Zhang, Y., Zameer, A., & John, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808698106 · Cited by 666 · see citing works
Sheṕro, D., & Morel-Laurens, N. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.11.8370472 · Cited by 652 · see citing works
Oldendorf, W. H., Cornford, M. E., & Brown, W. J. (1977) · Annals of Neurology · doi:10.1002/ana.410010502 · Cited by 651 · see citing works
Inflammation in stroke and focal cerebral ischemia
Huang, J., Upadhyay, U. M., & Tamargo, R. J. (2006) · Surgical Neurology · doi:10.1016/j.surneu.2005.12.028 · Cited by 649 · see citing works
Canonical Wnt Signaling Regulates Organ-Specific Assembly and Differentiation of CNS Vasculature
Stenman, J. M., Rajagopal, J., Carroll, T. J., Ishibashi, M., McMahon, J., & McMahon, A. P. (2008) · Science · doi:10.1126/science.1164594 · Cited by 641 · see citing works
Occludin is a functional component of the tight junction
McCarthy, K. M., Skare, I. B., Stankewich, M. C., Furuse, M., Tsukita, S., Rogers, R. A., Lynch, R. D., & Schneeberger, E. E. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.9.2287 · Cited by 640 · see citing works
Thiebaut, F., TSURUO, T., Hamada, H., Gottesman, M. M., Pastan, I. H., & Willingham, M. C. (1989) · Journal of Histochemistry & Cytochemistry · doi:10.1177/37.2.2463300 · Cited by 603 · see citing works
Itallie, C. M. V., Rahner, C., & Anderson, J. M. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12464 · Cited by 601 · see citing works
Sims, D. (1986) · Tissue and Cell · doi:10.1016/0040-8166(86)90026-1 · Cited by 582 · see citing works
Daneman, R., Zhou, L., Agalliu, D., Cahoy, J. D., Kaushal, A., & Barres, B. A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013741 · Cited by 577 · see citing works
Self-citationAgrawal, S., Anderson, P., Durbeej, M., van Rooijen, N., Ivars, F., Opdenakker, G., & Sorokin, L. M. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20051342 · Cited by 559 · see citing works
Díaz‐Flores, L., Gutiérrez, R., Madrid, J. F., Varela, H., Valladares, F., Acosta, E., Martı́n-Vasallo, P., & Díaz-Flores, L. (2009) · PubMed · doi:10.14670/hh-24.909 · Cited by 547 · see citing works
Glial influence on the blood brain barrier
Alvarez, J. I., Katayama, T., & Prat, A. (2013) · Glia · doi:10.1002/glia.22575 · Cited by 542 · see citing works
Self-citationWong, V., & Gumbiner, B. M. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.2.399 · Cited by 540 · see citing works
Cayrol, R., Wosik, K., Berard, J. L., Dodelet-Devillers, A., Ifergan, I., Kebir, H., Haqqani, A. S., Kreymborg, K., Krug, S., Moumdjian, R., et al. (2008) · Nature Immunology · doi:10.1038/ni1551 · Cited by 444 · see citing works
Self-citationHypoxia-induced vascular endothelial growth factor expression causes vascular leakage in the brain
Schoch, H. (2002) · Brain · doi:10.1093/brain/awf257 · Cited by 433 · see citing works
Hadj-Rabia, S., Baala, L., Vabres, P., Hamel‐Teillac, D., Jacquemin, E., Fabrè, M., Lyonnet, S., Prost, Y. D., Münnich, A., Hadchouel, M., et al. (2004) · Gastroenterology · doi:10.1053/j.gastro.2004.07.022 · Cited by 426 · see citing works
Chen, X.-L., Dodd, G., Thomas, S., Zhang, X., Wasserman, M. A., Rovin, B. H., & Kunsch, C. (2006) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00651.2005 · Cited by 418 · see citing works
Molecular Basis of the Core Structure of Tight JunctionsPreprint
Furuse, M. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a002907 · Cited by 410 · see citing works
Itallie, C. M. V., Holmes, J. C., Bridges, A. S., Gookin, J. L., Coccaro, M. R., Proctor, W. R., Colegio, O. R., & Anderson, J. M. (2008) · Journal of Cell Science · doi:10.1242/jcs.021485 · Cited by 410 · see citing works
Norrin/Frizzled4 Signaling in Retinal Vascular Development and Blood Brain Barrier Plasticity
Wang, Y., Rattner, A., Zhou, Y., Williams, J., Smallwood, P. M., & Nathans, J. (2012) · Cell · doi:10.1016/j.cell.2012.10.042 · Cited by 406 · see citing works
How do immune cells overcome the blood-brain barrier in multiple sclerosis?
Larochelle, C., Alvarez, J. I., & Prat, A. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.04.066 · Cited by 405 · see citing works
Self-citationBetz, A. L., Firth, J. A., & Goldstein, G. W. (1980) · Brain Research · doi:10.1016/0006-8993(80)91004-5 · Cited by 400 · see citing works
Cerebral microvascular changes in permeability and tight junctions induced by hypoxia-reoxygenation
Mark, K. S., & Davis, T. P. (2002) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00645.2001 · Cited by 394 · see citing works
Colegio, O. R., Itallie, C. V., Rahner, C., & Anderson, J. M. (2003) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00547.2002 · Cited by 387 · see citing works
Kuroiwa, T., Ting, P., Martínez, H. R., & KLATZO, I. (1985) · Acta Neuropathologica · doi:10.1007/bf00688633 · Cited by 359 · see citing works
Cytokine-induced VCAM-1 and ICAM-1 expression in different organs of the mouse
Henninger, D. D., Panés, J., Eppihimer, M. J., Russell, J., Gerritsen, M. E., Anderson, D. C., & Granger, D. N. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.4.1825 · Cited by 346 · see citing works
Polarity of the Blood-Brain Barrier: Neutral Amino Acid Transport into Isolated Brain Capillaries
Betz, A. L., & Goldstein, G. W. (1978) · Science · doi:10.1126/science.211586 · Cited by 342 · see citing works
Disruption of central nervous system barriers in multiple sclerosis
Alvarez, J. I., Cayrol, R., & Prat, A. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.06.017 · Cited by 334 · see citing works
Self-citationFischer, S., Wobben, M., Marti, H. H., Renz, D., & Schaper, W. K. A. (2002) · Microvascular Research · doi:10.1006/mvre.2001.2367 · Cited by 317 · see citing works
The FGF system has a key role in regulating vascular integrity.
Murakami, M., Nguyen, L. T., Zhuang, Z. W., Moodie, K., Carmeliet, P., Stan, R., & Simons, M. (2008) · Journal of Clinical Investigation · doi:10.1172/jci35298 · Cited by 297 · see citing works
Transport of proteins across normal cerebral arterioles
Westergaard, E., & Brightman, M. W. (1973) · Journal of Comparative Neurology · doi:10.1002/cne.901520103 · Cited by 285 · see citing works
Persidsky, Y., Ghorpade, A., Rasmussen, J., Limoges, J., Liu, X. J., Stins, M. F., Fiala, M., Way, D., Kim, K. S., Witte, M. H., et al. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65476-4 · Cited by 284 · see citing works
Glial cell influence on the human blood‐brain barrier
Prat, A., Biernacki, K., Wosik, K., & Antel, J. P. (2001) · Glia · doi:10.1002/glia.1104 · Cited by 269 · see citing works
Self-citationOrłowski, M., Sessa, G., & Green, J. P. (1974) · Science · doi:10.1126/science.184.4132.66 · Cited by 269 · see citing works
LSR defines cell corners for tricellular tight junction formation in epithelial cells
Masuda, S., Oda, Y., Sasaki, H., Ikenouchi, J., Higashi, T., Akashi, M., Nishi, E., & Furuse, M. (2011) · Journal of Cell Science · doi:10.1242/jcs.072058 · Cited by 265 · see citing works
Wu, C., Ivars, F., Anderson, P. O., Hallmann, R., Vestweber, D., Nilsson, P., Robenek, H., Tryggvason, K., Song, J., Korpos, É., et al. (2009) · Nature Medicine · doi:10.1038/nm.1957 · Cited by 264 · see citing works
Wosik, K., Cayrol, R., Dodelet-Devillers, A., Berthelet, F., Bernard, M., Moumdjian, R. A., Bouthillier, A., Reudelhuber, T. L., & Prat, A. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.2088-07.2007 · Cited by 259 · see citing works
Self-citationRole of microglia in the central nervous system's immune response
Streit, W. J., Conde, J. R., Fendrick, S. E., Flanary, B. E., & Mariani, C. L. (2005) · Neurological Research · doi:10.1179/016164105x49463a · Cited by 258 · see citing works
Gu, Y., Zheng, G., Xu, M., Li, Y., Chen, X., Zhu, W., Tong, Y., Chung, S. K., Liu, K. J., & Shen, J. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07542.x · Cited by 251 · see citing works
Protein kinase signaling in the modulation of microvascular permeability
Yuan, S. Y. (2002) · Vascular Pharmacology · doi:10.1016/s1537-1891(03)00010-7 · Cited by 242 · see citing works
Huang, Z.-G., Xue, D., Karbalai, H., Buchan, A. M., Huang, Z.-G., Xue, D., & Preston, E. (1999) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100000421 · Cited by 241 · see citing works
Greenwood, J., Heasman, S. J., Alvarez, J. I., Prat, A., Lyck, R., & Engelhardt, B. (2011) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01140.x · Cited by 240 · see citing works
Self-citationWilliams, K. C., Alvarez, X. A., & Lackner, A. A. (2001) · Glia · doi:10.1002/glia.1105 · Cited by 237 · see citing works
Study of Claudin Function by RNA Interference
Hou, J., Gomes, A. S., Paul, D. L., & Goodenough, D. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608853200 · Cited by 231 · see citing works
Morphometric analysis of CNS microvascular endothelium
Coomber, B. L., & Stewart, P. A. (1985) · Microvascular Research · doi:10.1016/0026-2862(85)90042-1 · Cited by 211 · see citing works
The rat blood-brain barrier transcriptome
Enerson, B. E., & Drewes, L. R. (2006) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600249 · Cited by 205 · see citing works
Retinoic Acid Induces Blood–Brain Barrier Development
Mizee, M. R., Wooldrik, D., Lakeman, K. A. M., van het Hof, B., Drexhage, J. A. R., Geerts, D., Bugiani, M., Aronica, E., Mebius, R. E., Prat, A., et al. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.1338-12.2013 · Cited by 203 · cited 2× · see citing works
“In vivo, pharmacologic modulation of RAR-b resulted Cite this article as Cold Spring Harb Perspect Biol 2015;7:a020412 11 in a perturbed BBB (Mizee et al. 2013).”
BackgroundSelf-citationPotschka, H., Fedrowitz, M., & Löscher, W. (2001) · Neuroreport · doi:10.1097/00001756-200111160-00037 · Cited by 203 · see citing works
Contribution of claudin-5 to barrier properties in tight junctions of epithelial cells
Amasheh, S., Schmidt, T. P., Mahn, M., Florian, P., Mankertz, J., Tavalali, S., Gitter, A. H., Schulzke, J., & Fromm, M. (2005) · Cell and Tissue Research · doi:10.1007/s00441-005-1101-0 · Cited by 194 · see citing works
Male Donor-derived Cells in the Brains of Female Sex-mismatched Bone Marrow Transplant Recipients
Unger, E. R., SUNG, J. H., Manivel, J. C., Chenggis, M. L., Blazar, B. R., & Krivit, W. A. (1993) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199309000-00004 · Cited by 187 · see citing works
The Norrin/Frizzled4 signaling pathway in retinal vascular development and disease
Ye, X., Wang, Y., & Nathans, J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.07.003 · Cited by 183 · see citing works
Junctional adhesion molecule-2 (JAM-2) promotes lymphocyte transendothelial migration
Johnson‐Léger, C., Aurrand‐Lions, M., Beltraminelli, N., Fasel, N. J., & Imhof, B. A. (2002) · Blood · doi:10.1182/blood-2001-11-0098 · Cited by 182 · see citing works
Polfliet, M. M. J., Zwijnenburg, P. J. G., van Furth, A. M., van der Poll, T., Döpp, E. A., de Lavalette, C. R., van Kesteren-Hendrikx, E. M. L., van Rooijen, N., Dijkstra, C. D., & van den Berg, T. K. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.167.8.4644 · Cited by 180 · see citing works
Immune cell entry into the central nervous system: Involvement of adhesion molecules and chemokines
Engelhardt, B. (2008) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2008.05.019 · Cited by 179 · see citing works
Sharp, C. D., Hines, I. N., Houghton, J., Warren, A., Jackson, T. H., Jawahar, A., Nanda, A., Elrod, J. W., Long, A. C., Chi, A., et al. (2003) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00520.2003 · Cited by 175 · see citing works
Neutrophil-derived Glutamate Regulates Vascular Endothelial Barrier Function
Collard, C. D., Park, K. A., Montalto, M., Alapati, S., Buras, J. A., Stahl, G. L., & Colgan, S. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110557200 · Cited by 171 · see citing works
Li, J. Y., Boado, R. J., & Pardridge, W. M. (2001) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200101000-00008 · Cited by 164 · see citing works
Ghandour, M. S., Langley, O. K., Zhu, X. L., Waheed, A., & Sly, W. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.15.6823 · Cited by 160 · see citing works
Reuß, B., Dono, R., & Unsicker, K. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-16-06404.2003 · Cited by 159 · see citing works
Pericyte endothelial gap junctions in human cerebral capillaries
Cuevas, P., Gutiérrez-Díaz, J. A., Reimers, D., Dujovny, M., Diaz, F. G., & Ausman, J. I. (1984) · Anatomy and Embryology · doi:10.1007/bf00319000 · Cited by 157 · see citing works
Claudin interactions in and out of the tight junction
Itallie, C. M. V., & Anderson, J. M. (2013) · Tissue Barriers · doi:10.4161/tisb.25247 · Cited by 151 · see citing works
Fibronectin in the microvasculature: localization in the pericyte-endothelial interstitium
Courtoy, P. J., & Boyles, J. K. (1983) · Journal of Ultrastructure Research · doi:10.1016/s0022-5320(83)90133-8 · Cited by 148 · see citing works
Structure and Functions of Aquaporin-4-Based Orthogonal Arrays of Particles
Wolburg, H., Wolburg‐Buchholz, K., Fallier‐Becker, P., Noell, S., & Mack, A. F. (2011) · International review of cytology · doi:10.1016/b978-0-12-386043-9.00001-3 · Cited by 137 · see citing works
Cornford, E. M., Hyman, S., & Swartz, B. E. (1994) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.1994.15 · Cited by 136 · see citing works
Wnt Signaling Mediates Pathological Vascular Growth in Proliferative Retinopathy
Chen, J., Stahl, A., Krah, N. M., Seaward, M. R., Dennison, R. J., Sapieha, P. S., Hua, J., Hatton, C. J., Juan, A. M., Aderman, C. M., et al. (2011) · Circulation · doi:10.1161/circulationaha.111.040337 · Cited by 134 · see citing works
Evidence for a role of dystroglycan regulating the membrane architecture of astroglial endfeet
Noell, S., Wolburg‐Buchholz, K., Mack, A. F., Beedle, A. M., Satz, J. S., Campbell, K. P., Wolburg, H., & Fallier‐Becker, P. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07688.x · Cited by 121 · see citing works
Bidirectional control of arteriole diameter by astrocytes
Gordon, G. R., Howarth, C., & MacVicar, B. A. (2011) · Experimental Physiology · doi:10.1113/expphysiol.2010.053132 · Cited by 118 · see citing works
Drug Resistance in Epilepsy: The Role of the Blood–Brain Barrier
Abbott, N. J., Khan, E. U., Rollinson, C., Reichel, A., Janigro, D., Dombrowski, S. M., Dobbie, M. S., & Begley, D. J. (2002) · Novartis Foundation symposium · doi:10.1002/0470846356.ch4 · Cited by 109 · see citing works
Larson, D. M., Carson, M. P., & Haudenschild, C. C. (1987) · Microvascular Research · doi:10.1016/0026-2862(87)90052-5 · Cited by 109 · see citing works
Shue, E. H., Carson-Walter, E. B., Liu, Y., Winans, B., Ali, Z. S., Chen, J., & Walter, K. A. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-29 · Cited by 109 · see citing works
Fischer, S., Wiesnet, M., Marti, H. H., Renz, D., & Schaper, W. K. A. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10417 · Cited by 108 · see citing works
Wang, Y., Imitola, J., Rasmussen, S. O., O’Connor, K. C., & Khoury, S. J. (2008) · Annals of Neurology · doi:10.1002/ana.21457 · Cited by 108 · see citing works
Retinoids control anterior and dorsal properties in the developing forebrain.
Halilagic, A., Ribes, V., Ghyselinck, N., Zile, M., Dollé, P., & Studer, M. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2006.11.021 · Cited by 106 · see citing works
Altered Expression of Angiopoietins During Blood-Brain Barrier Breakdown and Angiogenesis
Nourhaghighi, N., Teichert-Kuliszewska, K., Davis, J., Stewart, D. J., & Nag, S. (2003) · Laboratory Investigation · doi:10.1097/01.lab.0000082383.40635.fe · Cited by 104 · see citing works
The prototype endothelial marker PAL-E is a leukocyte trafficking molecule
Keuschnigg, J., Henttinen, T. A., Auvinen, K., Karikoski, M., Salmi, M., & Jalkanen, S. (2009) · Blood · doi:10.1182/blood-2008-11-188763 · Cited by 98 · see citing works
Ludwig, R. J., Zollner, T. M., Santoso, S., Hardt, K., Gille, J., Baatz, H., Johann, P. S., Pfeffer, J., Radeke, H. H., Schön, M. P., et al. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2005.23912.x · Cited by 97 · see citing works
Dohgu, S., Yamauchi, A., Takata, F., Naito, M., Tsuruo, T., Higuchi, S., Sawada, Y., & Kataoka, Y. (2004) · Cellular and Molecular Neurobiology · doi:10.1023/b:cemn.0000022776.47302.ce · Cited by 96 · see citing works
Vascular matrix adhesion and the blood–brain barrier
del Zoppo, G. J., Milner, R., Mabuchi, T., Hung, S., Wang, X., & Koziol, J. A. (2006) · Biochemical Society Transactions · doi:10.1042/bst0341261 · Cited by 95 · see citing works
Glucose transporter 1 deficiency syndrome and other glycolytic defects.
Vivo, D. C. D., Leary, L., & Wang, D. (2002) · PubMed · Cited by 95 · see citing works
Tight junctions in Schwann cells of peripheral myelinated axons
Miyamoto, T., Morita, K., Takemoto, D., Takeuchi, K., Kitano, Y., Miyakawa, T., Nakayama, K., Okamura, Y., Sasaki, H., Miyachi, Y., et al. (2005) · Journal of Cell Biology · doi:10.1083/jcb.200501154 · Cited by 95 · see citing works
SOX-18 controls endothelial-specific claudin-5 gene expression and barrier function
Fontijn, R. D., Volger, O. L., Fledderus, J. O., Reijerkerk, A., de Vries, H. E., & Horrevoets, A. J. G. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01248.2007 · Cited by 89 · see citing works
Regulation of Th1 and Th2 Lymphocyte Migration by Human Adult Brain Endothelial Cells
Biernacki, K., Prat, A., Blain, M., & Antel, J. P. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.12.1127 · Cited by 88 · see citing works
Self-citationRecent Advances in Delivery Through the Blood-Brain Barrier
Larsen, J., Martin, D. R., & Byrne, M. E. (2014) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026614666140329230311 · Cited by 87 · see citing works
Claudins: unlocking the code to tight junction function during embryogenesis and in disease
Gupta, I., & Ryan, A. K. (2010) · Clinical Genetics · doi:10.1111/j.1399-0004.2010.01397.x · Cited by 85 · see citing works
Shen, F., Walker, E. J., Jiang, L., Degos, V., Li, J., Sun, B., Heriyanto, F., Young, W. L., & Su, H. (2011) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2011.97 · Cited by 82 · see citing works
Vass, K., Wf, H., Schmidt, R. E., & Lassmann, H. (1993) · PubMed · Cited by 77 · see citing works
Fan, X., Staitieh, B. S., Jensen, J. S., Mould, K. J., Greenberg, J. A., Joshi, P. C., Koval, M. H., & Guidot, D. M. (2013) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00288.2012 · Cited by 73 · see citing works
Functions of lipid raft membrane microdomains at the blood–brain barrier
Dodelet-Devillers, A., Cayrol, R., van Horssen, J., Haqqani, A. S., de Vries, H. E., Engelhardt, B., Greenwood, J., & Prat, A. (2009) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0488-6 · Cited by 70 · see citing works
Self-citationMartin, R. E. (1998) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19981215)54:6 · Cited by 66 · see citing works
Reoxygenation stress on blood–brain barrier paracellular permeability and edema in the rat
WITT, K. A., Mark, K. S., Sandoval, K. E., & Davis, T. P. (2007) · Microvascular Research · doi:10.1016/j.mvr.2007.06.004 · Cited by 64 · see citing works
Hudson, L. C., Bragg, D. C., Tompkins, M. B., et al. (2005) · Brain Research · doi:10.1016/j.brainres.2005.07.071 · Cited by 64 · see citing works
Hong, J. Y., Park, J., Cho, K., Gu, D., Ji, H. L., Artandi, S. E., & McCrea, P. D. (2010) · Journal of Cell Science · doi:10.1242/jcs.067199 · Cited by 64 · see citing works
Bioluminescence in vivo imaging of autoimmune encephalomyelitis predicts disease
Luo, J., Ho, P. P.-K., Steinman, L., & Wyss‐Coray, T. (2008) · Journal of Neuroinflammation · doi:10.1186/1742-2094-5-6 · Cited by 61 · see citing works
The diversity of endothelial cells: a challenge for therapeutic angiogenesis.
Conway, E. M., & Carmeliet, P. (2004) · Genome biology · doi:10.1186/gb-2004-5-2-207 · Cited by 59 · see citing works
Mittapalli, R. K., Manda, V. K., Adkins, C. E., Geldenhuys, W. J., & Lockman, P. R. (2010) · Therapeutic Delivery · doi:10.4155/tde.10.76 · Cited by 53 · see citing works
Lenglet, S., Montecucco, F., Mach, F., Schaller, K., Gasche, Y. G., & Copin, J. (2014) · Thrombosis and Haemostasis · doi:10.1160/th14-01-0007 · Cited by 52 · see citing works
Liu, L., Xue, Y., & Liu, Y. (2010) · Journal of Neuro-Oncology · doi:10.1007/s11060-010-0124-x · Cited by 47 · see citing works
Rat Blood–Brain Barrier Genomics. II
Li, J. Y., Boado, R. J., & Pardridge, W. M. (2002) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/01.wcb.0000040944.89393.0f · Cited by 46 · see citing works
Ohtsuki, S., Hirayama, M., Ito, S., Uchida, Y., Tachikawa, M., & Terasaki, T. (2014) · Expert Review of Proteomics · doi:10.1586/14789450.2014.893830 · Cited by 45 · see citing works
Ufnal, M., & Skrzypecki, J. (2014) · Neuropeptides · doi:10.1016/j.npep.2014.01.003 · Cited by 44 · see citing works
Mini Review on Molecular Modeling of P-Glycoprotein (Pgp)
Ha, S., Hochman, J. H., & Sheridan, R. (2007) · Current Topics in Medicinal Chemistry · doi:10.2174/156802607782194806 · Cited by 42 · see citing works
Zhao, L., Yang, Z., Liu, Y., Ying, H.-Q., Zhang, H., & Xue, Y. (2010) · Journal of Molecular Neuroscience · doi:10.1007/s12031-010-9487-x · Cited by 40 · see citing works
The blood-brain barrier in health and disease
SUCKLING, A. J., Rumsby, M. G., & Bradbury, M. W. B. (1986) · Medical Entomology and Zoology · Cited by 33 · see citing works
Hampson, G., Konrad, M., & Scoble, J. E. (2008) · BMC Nephrology · doi:10.1186/1471-2369-9-12 · Cited by 33 · see citing works
Retinoic Acid-Dependent Signaling Pathways and Lineage Events in the Developing Mouse Spinal Cord
Paschaki, M., Lin, S.-C., Wong, R. L. Y., Finnell, R. H., Dollé, P., & Niederreither, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032447 · Cited by 29 · see citing works
Knohl, S. J., & Scheinman, S. J. (2004) · Seminars in Nephrology · doi:10.1053/j.semnephrol.2003.08.011 · Cited by 28 · see citing works
Agrawal, S., Anderson, P. O., Durbeej, M., et al. (2006) · The Journal of Cell Biology · doi:10.1083/jcb1732oia2 · Cited by 18 · see citing works
宮本, 達. (2007) · Medical Entomology and Zoology · Cited by 12 · see citing works
The FGF system has a key role in regulating vascular integrity
Murakami, M., Nguyen, L. T., Zhuang, Z. W., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci35298c1 · Cited by 7 · see citing works
Pardridge, W. M. (2001) · Cambridge University Press eBooks · doi:10.1017/cbo9780511549571.011 · Cited by 6 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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 2,294 · see citing works
The blood–brain barrier: Structure, regulation and drug delivery
Wu, D., Chen, Q., Chen, X., Han, F., Chen, Z., & Wang, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01481-w · Cited by 1,906 · see citing works
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 · see citing works
The gut-brain axis: how microbiota and host inflammasome influence brain physiology and pathology
Rutsch, A., Kantsjö, J. B., & Ronchi, F. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.604179 · Cited by 821 · see citing works
A new look at cerebrospinal fluid circulation
Brinker, T., Stopa, E., Morrison, J., & Klinge, P. (2014) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-11-10 · Cited by 819 · see citing works
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 · see citing works
The blood-brain barrier in aging and neurodegeneration
Knox, E. G., Aburto, M. R., Clarke, G., Cryan, J. F., & O’Driscoll, C. M. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01511-z · Cited by 738 · see citing works
“The basement membrane is composed of both an inner vascular basement membrane, which is secreted by endothelial cells and pericytes and an outer parenchymal basement membrane, which is secreted by astrocytes [1].”
BackgroundThe blood-brain barrier: an engineering perspective
Wong, A. D., Ye, M., Levy, A. F., Rothstein, J. D., Bergles, D. E., & Searson, P. C. (2013) · Frontiers in Neuroengineering · doi:10.3389/fneng.2013.00007 · Cited by 662 · see citing works
The blood-brain barrier: Physiology and strategies for drug delivery
Pandit, R., Chen, L., & Götz, J. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2019.11.009 · Cited by 651 · see citing works
The progress of gut microbiome research related to brain disorders
Zhu, S., Jiang, Y., Xu, K., Cui, M., Ye, W., Zhao, G., Jin, L., & Chen, X. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-1705-z · Cited by 419 · see citing works
Macrophages at CNS interfaces: Ontogeny and function in health and disease
Kierdorf, K., Masuda, T., Jordão, M. J. C., & Prinz, M. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0201-x · Cited by 416 · see citing works
Progress in brain targeting drug delivery system by nasal route
Khan, A. R., Liu, M., Khan, M. W., & Zhai, G. (2017) · Journal of Controlled Release · doi:10.1016/j.jconrel.2017.09.001 · Cited by 402 · see citing works
Mamsen, L. S., Björvang, R. D., Mucs, D., Vinnars, M.-T., Papadogiannakis, N., Lindh, C. H., Andersen, C. Y., & Damdimopoulou, P. (2019) · Environment International · doi:10.1016/j.envint.2019.01.010 · Cited by 338 · see citing works
Tumor microenvironment differences between primary tumor and brain metastases
Cacho-Díaz, B., García-Botello, D. R., Wegman-Ostrosky, T., Reyes-Soto, G., Ortiz-Sánchez, E., & Herrera-Montalvo, L. A. (2020) · Journal of Translational Medicine · doi:10.1186/s12967-019-02189-8 · Cited by 310 · see citing works
Marchetti, L., & Engelhardt, B. (2020) · Vascular Biology · doi:10.1530/vb-19-0033 · Cited by 304 · see citing works
Blood-Brain Barrier Overview: Structural and Functional Correlation
Alahmari, A. (2021) · Neural Plasticity · doi:10.1155/2021/6564585 · Cited by 299 · see citing works
Emerging roles of innate and adaptive immunity in Alzheimer’s disease
Chen, X., & Holtzman, D. M. (2022) · Immunity · doi:10.1016/j.immuni.2022.10.016 · Cited by 297 · see citing works
D’Amato, A., Di Cesare Mannelli, L., Lucarini, E., Man, A. L., Le Gall, G., Branca, J. J. V., Ghelardini, C., Amedei, A., Bertelli, E., Regoli, M., et al. (2020) · Microbiome · doi:10.1186/s40168-020-00914-w · Cited by 269 · see citing works
Nanoemulsions for “Nose-to-Brain” Drug Delivery
Bonferoni, M. C., Rossi, S., Sandri, G., Ferrari, F., Gavini, E., Rassu, G., & Giunchedi, P. (2019) · Pharmaceutics · doi:10.3390/pharmaceutics11020084 · Cited by 269 · see citing works
Brain Endothelial Cells Are Exquisite Sensors of Age-Related Circulatory Cues
Chen, M. B., Yang, A. C., Yousef, H., Lee, D., Chen, W., Schaum, N., Lehallier, B., Quake, S. R., & Wyss-Coray, T. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.012 · Cited by 233 · see citing works
“Indeed, while age-related BBB dysfunction has been probed with a diverse toolkit of tracers (Bien-Ly et al., 2015; Marques et al., 2013; Montagne et al., 2015; Mooradian, 1988), the transcriptional response of vessel segment-specific BECs to aging and changes in the systemic environment have not yet been explored in-d…”
InfluentialInfectious immunity in the central nervous system and brain function
Klein, R. S., Garber, C., & Howard, N. (2017) · Nature Immunology · doi:10.1038/ni.3656 · Cited by 235 · see citing works
Development and Function of the Blood-Brain Barrier in the Context of Metabolic Control
Haddad-Tóvolli, R., Dragano, N. R. V., Ramalho, A. F. S., & Velloso, L. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00224 · Cited by 226 · see citing works
Schiweck, J., Eickholt, B. J., & Murk, K. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00261 · Cited by 223 · see citing works
Therapeutic Properties and Pharmacological Activities of Asiaticoside and Madecassoside: A Review
Bandopadhyay, S., Mandal, S., Ghorai, M., Jha, N. K., Kumar, M., Radha, Ghosh, A., Proćków, J., Pérez de la Lastra, J. M., & Dey, A. (2023) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.17635 · Cited by 220 · see citing works
Function of Green Tea Catechins in the Brain: Epigallocatechin Gallate and its Metabolites
Pervin, M., Unno, K., Takagaki, A., Isemura, M., & Nakamura, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153630 · Cited by 216 · see citing works
Blood–Brain Barrier Breakdown in Alzheimer’s Disease: Mechanisms and Targeted Strategies
Alkhalifa, A. E., Al-Ghraiybah, N. F., Odum, J., Shunnarah, J. G., Austin, N., & Kaddoumi, A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216288 · Cited by 212 · see citing works
Transport of Amino Acids Across the Blood-Brain Barrier
Zaragozá, R. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00973 · Cited by 202 · see citing works
Lipid nanoparticle-mediated drug delivery to the brain
Khare, P., Edgecomb, S. X., Hamadani, C. M., Tanner, E. E. L., & S Manickam, D. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.114861 · Cited by 187 · see citing works
Challenges and opportunities to penetrate the blood-brain barrier for brain cancer therapy
Upton, D. H., Ung, C., George, S. M., Tsoli, M., Kavallaris, M., & Ziegler, D. S. (2022) · Theranostics · doi:10.7150/thno.69682 · Cited by 182 · see citing works
Xiao, W., Wang, Y., Zhang, H., Liu, Y., Xie, R., He, X., Zhou, Y., Liang, L., & Gao, H. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.120888 · Cited by 174 · see citing works
Understanding the Gut–Brain Axis and Its Therapeutic Implications for Neurodegenerative Disorders
Zheng, Y., Bonfili, L., Wei, T., & Eleuteri, A. M. (2023) · Nutrients · doi:10.3390/nu15214631 · Cited by 175 · see citing works
Liang, Y., Iqbal, Z., Lu, J., Wang, J., Zhang, H., Chen, X., Duan, L., & Xia, J. (2023) · Molecular Therapy · doi:10.1016/j.ymthe.2022.10.008 · Cited by 162 · see citing works
Glycosphingolipids and Neuroinflammation in Parkinson’s Disease
Belarbi, K., Cuvelier, E., Bonte, M.-A., Desplanque, M., Gressier, B., Devos, D., & Chartier-Harlin, M.-C. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00408-1 · Cited by 155 · see citing works
Hyperactivation of P2X7 receptors as a culprit of COVID-19 neuropathology
Ribeiro, D. E., Oliveira-Giacomelli, Á., Glaser, T., Arnaud-Sampaio, V. F., Andrejew, R., Dieckmann, L., Baranova, J., Lameu, C., Ratajczak, M. Z., & Ulrich, H. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00965-3 · Cited by 145 · see citing works
Neurotheranostics as Personalized Medicines
Kevadiya, B. D., Ottemann, B. M., Thomas, M. B., Mukadam, I., Nigam, S., McMillan, J., Gorantla, S., Bronich, T. K., Edagwa, B., & Gendelman, H. E. (2019) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2018.10.011 · Cited by 124 · see citing works
Blood-brain barrier leakage in Alzheimer’s disease: From discovery to clinical relevance
Nehra, G., Bauer, B., & Hartz, A. M. S. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108119 · Cited by 127 · see citing works
Microglial diversity by responses and responders
Gertig, U., & Hanisch, U.-K. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00101 · Cited by 123 · see citing works
Jamieson, J. J., Linville, R. M., Ding, Y. Y., Gerecht, S., & Searson, P. C. (2019) · Fluids and Barriers of the CNS · doi:10.1186/s12987-019-0136-7 · Cited by 117 · see citing works
Laksitorini, M. D., Yathindranath, V., Xiong, W., Hombach-Klonisch, S., & Miller, D. W. (2019) · Scientific Reports · doi:10.1038/s41598-019-56075-w · Cited by 105 · see citing works
Faley, S. L., Neal, E. H., Wang, J. X., Bosworth, A. M., Weber, C. M., Balotin, K. M., Lippmann, E. S., & Bellan, L. M. (2019) · Stem Cell Reports · doi:10.1016/j.stemcr.2019.01.009 · Cited by 106 · see citing works
Knox, E. G., Aburto, M. R., Tessier, C., Nagpal, J., Clarke, G., O’Driscoll, C. M., & Cryan, J. F. (2022) · iScience · doi:10.1016/j.isci.2022.105648 · Cited by 97 · see citing works
Habashy, K. J., Mansour, R., Moussalem, C., Sawaya, R., & Massaad, M. J. (2022) · British Journal of Cancer · doi:10.1038/s41416-022-01864-w · Cited by 95 · see citing works
(2020) · International Review of Neurobiology · doi:10.1016/bs.irn.2020.02.006 · Cited by 87 · see citing works
The relationship between amyloid-beta and brain capillary endothelial cells in Alzheimer’s disease
Su, Q., Guo, J.-H., Zhang, Y.-L., Wang, J., & Zhang, Z.-N. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.335829 · Cited by 91 · see citing works
Del Amo, L., Cano, A., Ettcheto, M., Souto, E. B., Espina, M., Camins, A., García, M. L., & Sánchez-López, E. (2021) · Applied Sciences · doi:10.3390/app11094305 · Cited by 67 · see citing works
Liu, J., Jin, Y., Ye, Y., Tang, Y., Dai, S., Li, M., Zhao, G., Hong, G., & Lu, Z.-Q. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.626894 · Cited by 66 · see citing works
Jiao, Y., Yang, L., Wang, R., Song, G., Fu, J., Wang, J., Gao, N., & Wang, H. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16121611 · Cited by 63 · see citing works
Ding, L., Kshirsagar, P., Agrawal, P., & Murry, D. J. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17060706 · Cited by 62 · see citing works
Candida albicans at Host Barrier Sites: Pattern Recognition Receptors and Beyond
Swidergall, M. (2019) · Pathogens · doi:10.3390/pathogens8010040 · Cited by 59 · see citing works
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 · see citing works
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 · see citing works
“To overcome the highly selective BBB most molecules require carrier- or receptor-mediated transport systems [12].”
BackgroundMechanisms of myeloid cell entry to the healthy and diseased central nervous system
Amann, L., Masuda, T., & Prinz, M. (2023) · Nature Immunology · doi:10.1038/s41590-022-01415-8 · Cited by 50 · see citing works
Yue, J., Tan, Y., Huan, R., Guo, J., Yang, S., Deng, M., Xiong, Y., Han, G., Liu, L., Liu, J., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1090288 · Cited by 46 · see citing works
Li, Z., Zhang, F., Sun, M., Liu, J., Zhao, L., Liu, S., Li, S., & Wang, B. (2023) · PeerJ · doi:10.7717/peerj.15122 · Cited by 43 · see citing works
Wasiak, J., & Gawlik-Kotelnicka, O. (2023) · Behavioural Brain Research · doi:10.1016/j.bbr.2023.114459 · Cited by 47 · see citing works
Poly (ADP-ribose) polymerase 1 and neurodegenerative diseases: past, present, and future
Hu, M.-L., Pan, Y.-R., Yong, Y.-Y., Liu, Y., Yu, L., Qin, D.-L., Qiao, G., Law, B. Y.-K., Wu, J.-M., Zhou, X.-G., et al. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102078 · Cited by 44 · see citing works
Microglia and Sensitive Periods in Brain Development
Dziabis, J. E., & Bilbo, S. D. (2021) · Current Topics in Behavioral Neurosciences · doi:10.1007/7854_2021_242 · Cited by 42 · see citing works
Broos, J. Y., van der Burgt, R. T. M., Konings, J., Rijnsburger, M., Werz, O., de Vries, H. E., Giera, M., & Kooij, G. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02981-w · Cited by 41 · see citing works
COVID-19 as a Risk Factor for Alzheimer’s Disease
Golzari-Sorkheh, M., Weaver, D. F., & Reed, M. A. (2023) · Journal of Alzheimer's Disease · doi:10.3233/jad-220800 · Cited by 39 · see citing works
Zhu, C.-L., Xie, J., Liu, Q., Wang, Y., Li, H.-R., Yu, C.-M., Li, P., Deng, X.-M., Bian, J.-J., & Wang, J.-F. (2023) · International Journal of Biological Sciences · doi:10.7150/ijbs.79913 · Cited by 42 · see citing works
Yu, C.-C., Chen, H.-L., Chen, M.-H., Lu, C.-H., Tsai, N.-W., Huang, C.-C., Chang, Y.-Y., Li, S.-H., Chen, Y.-S., Chiang, P.-L., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/2591248 · Cited by 37 · see citing works
Jones, L., Kumar, J., Mistry, A., Sankar Chittoor Mana, T., Perry, G., Reddy, V. P., & Obrenovich, M. (2019) · Biomedicines · doi:10.3390/biomedicines7020024 · Cited by 34 · see citing works
Mullane, K., & Williams, M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.09.027 · Cited by 32 · see citing works
Elbaz, M., Ad-El, N., Chulanova, Y., Brier, D., Goldsmith, M., Bismuth, M., Brosque, A., Sher, D., Gutkin, A., Bar-On, D., et al. (2025) · doi:10.1101/2025.01.23.634427 · Cited by 28 · see citing works
Extracellular vesicles as nanotheranostic platforms for targeted neurological disorder interventions
Choi, H. K., Chen, M., Goldston, L. L., & Lee, K.-B. (2024) · Nano Convergence · doi:10.1186/s40580-024-00426-5 · Cited by 26 · see citing works
Challenges and Promise for Glioblastoma Treatment through Extracellular Vesicle Inquiry
Liguori, G. L. (2024) · Cells · doi:10.3390/cells13040336 · Cited by 24 · see citing works
The Role of Complement C3a Receptor in Stroke
Ahmad, S., Bhatia, K., Kindelin, A., & Ducruet, A. F. (2019) · NeuroMolecular Medicine · doi:10.1007/s12017-019-08545-7 · Cited by 21 · see citing works
The organizational effects of oxytocin and vasopressin: Behavioral implications
Cushing, B. S. (2013) · Oxytocin, Vasopressin and Related Peptides in the Regulation of Behavior · doi:10.1017/cbo9781139017855.006 · Cited by 9 · see citing works
Mazura, A. D., & Pietrzik, C. U. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15041268 · Cited by 9 · see citing works
“The BBB is formed of specific endothelial cells lining the inside of brain microvasculature vessels [3], while the BCSFB is established by the epithelial layer of the choroid plexus of each ventricle [4].”
BackgroundCai, M., Chen, S., Du, Y., Li, S., Dong, P., Wang, L., Yang, R., Hu, J., & Zhu, L. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02052-4 · Cited by 4 · see citing works
Yin, H., Lu, Z., Deng, Y., Tian, X., & Gong, Q. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102952 · Cited by 6 · see citing works
- Authors
- Daneman, R., & Prat, A.
- Affiliations
- University of California San Diego (US)
- Université de Montréal (CA)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2015-01
- Volume
- 7
- Issue
- 1
- Pages
- a020412
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC4292164
- OpenAlex
- W2125411036
- Cited by
- 3,437
- References
- 161
- Citations by year
- 2026: 331 · 2025: 405 · 2024: 455 · 2023: 463 · 2022: 482 · 2021: 433 · 2020: 310 · 2019: 285 · 2018: 107 · 2017: 49 · 2016: 30 · 2015: 30 · 2014: 26 · 2013: 24 · 2012: 3
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Extracellular vesicles in disease
- Keywords
- blood-brain barrier, endothelial cells, CNS homeostasis, barrier permeability, blood-brain barrier dysfunction, neurological disorders, neuroimmune interactions
- MeSH terms
- Astrocytes, Basement Membrane, Blood-Brain Barrier, Central Nervous System Diseases, Homeostasis, Humans, Muscle, Smooth, Vascular, Tight Junctions, Endothelial Cells
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