GLUT1 reductions exacerbate Alzheimer's disease vasculo-neuronal dysfunction and degeneration
Open accessAbstract
The glucose transporter GLUT1 at the blood-brain barrier (BBB) mediates glucose transport into the brain. Alzheimer's disease is characterized by early reductions in glucose transport associated with diminished GLUT1 expression at the BBB. Whether GLUT1 reduction influences disease pathogenesis remains, however, elusive. Here we show that GLUT1 deficiency in mice overexpressing amyloid β-peptide (Aβ) precursor protein leads to early cerebral microvascular degeneration, blood flow reductions and dysregulation and BBB breakdown, and to accelerated amyloid β-peptide (Aβ) pathology, reduced Aβ clearance, diminished neuronal activity, behavioral deficits, and progressive neuronal loss and neurodegeneration that develop after initial cerebrovascular degenerative changes. We also show that GLUT1 deficiency in endothelium, but not in astrocytes, initiates the vascular phenotype as shown by BBB breakdown. Thus, reduced BBB GLUT1 expression worsens Alzheimer's disease cerebrovascular degeneration, neuropathology and cognitive function, suggesting that GLUT1 may represent a therapeutic target for Alzheimer's disease vasculo-neuronal dysfunction and degeneration.
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?
Slc2a1+/- mice with haploid deficiency in glucose transporter GLUT1 in brain endothelial cells develop microvascular reductions with BBB breakdown including loss of TJ and basement membrane proteins.
“The Slc2a1 + / -mice with haploid deficiency in glucose transporter GLUT1 in brain endothelial cells develop microvascular reductions with BBB breakdown including loss of TJ and basement membrane proteins (649), whereas knockout of murine Mfsd2a gene results in not only diminished brain uptake of docosahexaenoic acid (DHA) in the form of lysophosphatidylcholine, but also leads to dysregulated cave”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
The Results sections on microvascular reductions and early BBB breakdown report reduced capillary length, BBB leakage, and loss of tight-junction proteins in Slc2a1+/− mice, although the microvascular reductions in those mice appeared only at 6 months. The paper also shows that endothelial-specific GLUT1 deficiency causes BBB breakdown, but Slc2a1+/− is a global deficiency, not one confined to endothelial cells. The passages found do not support the claimed loss of basement-membrane proteins (no page numbers are available in our copy). (LLM, conf=0.87)
Experimental — accuracy not yet measuredGlucose concentration is lower in brain interstitial fluid compared with plasma.
“Since glucose concentration is lower in the brain interstitial fluid (ISF) compared with plasma, GLUT1 favors blood-to-brain transport of circulating glucose (141, 390, 649).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
The Introduction says GLUT1 mediates glucose transport into the brain. The Results report CSF glucose levels and CSF-to-blood glucose ratios in mice, but do not compare brain interstitial-fluid glucose concentration with plasma glucose concentration. Thus the transport portion of the citing sentence is supported, while its stated concentration gradient is not established by this paper. (LLM, conf=0.82)
Experimental — accuracy not yet measuredGlut1+/- mice phenocopy human pathology and develop initially within 2-3 weeks of age blood-brain barrier breakdown with loss of tight junctions and diminished glucose uptake by the brain, followed by microvascular regression, reduced brain perfusion, secondary neurodegenerative changes, microcephaly, and loss of cortical and hippocampal neurons.
“Glut1 + / -mice phenocopy human pathology, and develop initially within 2-3 wk of age BBB breakdown with loss of tight junctions and diminished glucose uptake by the brain, which is followed by microvascular regression, reduced brain perfusion and development of secondary neurodegenerative changes, microcephaly, and loss of cortical and hippocampal neurons (649).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredExperimental studies support diminished transport of 14C-labeled glucose across the BBB in haploinsufficient Slc2a1+/- mice lacking approximately 50% copies of the GLUT1 BBB transporter.
“Experimental studies also support diminished transport of 14 C-labeled glucose across the BBB in haploinsufficient Slc2a1 + / -mice lacking ~50% copies of the GLUT1 BBB transporter (649).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
The Results section (‘Microvascular reductions and diminished cerebral blood flow and glucose uptake’) reports reduced brain uptake of 2-[14C]-deoxyglucose in Slc2a1+/− mice and interprets it as suggesting reduced glucose transport across the BBB. It measured uptake of a labeled glucose analog, however, not transport of labeled glucose itself; the same section reports approximately 50% lower endothelial GLUT1 levels. (LLM, conf=0.84)
Experimental — accuracy not yet measuredReduced activity and expression of the GLUT-1 transporter in the BBB suggest decreased glucose uptake and utilization by the brain, which may further exacerbate cerebrovascular degeneration, BBB breakdown, and Aβ pathology in models overexpressing APP, inducing neurodegeneration and cognitive deficits.
“Reduced activity and expression of the GLUT-1 transporter in the BBB suggest decreased glucose uptake and utilization by the brain,360,363 which may further exacerbate cerebrovascular degeneration, BBB breakdown, and Aβ pathology in models overexpressing APP, inducing neurodegeneration and cognitive deficits (Fig. 4).364”
From Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies. (2024) · cites this paper as [364]
Reduced GLUT1 levels may inhibit LRP1 transcriptionally via sterol regulatory element binding protein 2 (SREBP2).
“reduced GLUT1 levels may also inhibit LRP1 transcriptionally via sterol regulatory element binding protein 2 (SREBP2) (649).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
Brain endothelial specific or enriched transporters are often indispensable for BBB barriergenesis, as for example, GLUT1, MFSD2A, and MCT8.
“Brain endothelial specific or enriched transporters are often indispensable for BBB barriergenesis, as for example, the glucose transporter-1 (GLUT1) (649), sodium-dependent lysophosphatidylcholine (LPC) symporter, the major facilitator superfamily (MFS) domain-containing protein 2a (MFSD2A) (62), and monocarboxylic acid transporter MCT8 (611).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
GLUT1 favors blood-to-brain transport of circulating glucose.
“Since glucose concentration is lower in the brain interstitial fluid (ISF) compared with plasma, GLUT1 favors blood-to-brain transport of circulating glucose (141, 390, 649).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
GLUT1 is expressed in endothelial cells but not in neurons.
“GLUT1 is expressed in endothelial cells, but not in neurons (141, 649).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
LRP1 minigene delivery to the BBB by viral vectors facilitates Aβ clearance and attenuates Aβ pathology.
“For example, LRP1 minigene delivery to the BBB by viral vectors facilitates A 𝛃 clearance and attenuates A 𝛃 pathology (649).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
GLUT1 deficiency leads to severe neurological phenotype in GLUT1-deficiency syndrome.
“which we know leads to severe neurological phenotype in the GLUT1-deficiency syndrome (630, 649).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [649]
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
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 · see citing works
Self-citationRetractedCorrelative 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 · 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
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 · see citing works
Bell, R. D., Winkler, E. A., Sagare, A. P., Singh, I., LaRue, B., Deane, R., & Zlokovic, B. V. (2010) · Neuron · doi:10.1016/j.neuron.2010.09.043 · Cited by 1,448 · see citing works
Self-citationRAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426 · see citing works
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413 · see citing works
Apolipoprotein E controls cerebrovascular integrity via cyclophilin A
Bell, R. D., Winkler, E. A., Singh, I., Sagare, A. P., Deane, R., Wu, Z., Holtzman, D. M., Betsholtz, C., Armulik, A., Sallstrom, J., et al. (2012) · Nature · doi:10.1038/nature11087 · Cited by 1,293 · see citing works
Self-citationAssessing nest building in mice
Deacon, R. M. J. (2006) · Nature Protocols · doi:10.1038/nprot.2006.170 · Cited by 1,115 · see citing works
Mfsd2a is a transporter for the essential omega-3 fatty acid docosahexaenoic acid
Nguyen, L. N., Ma, D., Shui, G., Wong, P., Cazenave-Gassiot, A., Zhang, X., Wenk, M. R., Goh, E. L. K., & Silver, D. L. (2014) · Nature · doi:10.1038/nature13241 · Cited by 1,048 · see citing works
Mfsd2a is critical for the formation and function of the blood-brain barrier
Ben-Zvi, A., Lacoste, B., Kur, E., Andreone, B. J., Mayshar, Y., Yan, H., & Gu, C. (2014) · Nature · doi:10.1038/nature13324 · Cited by 1,037 · see citing works
LRP/Amyloid β-Peptide Interaction Mediates Differential Brain Efflux of Aβ Isoforms
Deane, R., Wu, Z., Sagare, A., Davis, J., Du Yan, S., Hamm, K., Xu, F., Parisi, M., LaRue, B., Hu, H. W., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.017 · Cited by 828 · see citing works
Self-citationSupply and demand in cerebral energy metabolism: the role of nutrient transporters
Simpson, I. A., Carruthers, A., & Vannucci, S. J. (2007) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/sj.jcbfm.9600521 · Cited by 812 · see citing works
Crystal structure of the human glucose transporter GLUT1
Deng, D., Xu, C., Sun, P., Wu, J., Yan, C., Hu, M., & Yan, N. (2014) · Nature · doi:10.1038/nature13306 · Cited by 777 · see citing works
Amyloid Deposition, Hypometabolism, and Longitudinal Cognitive Decline
Landau, S. M., Mintun, M., Joshi, A. D., Koeppe, R., Petersen, R. C., Aisen, P., Weiner, M., & Jagust, W. J. (2012) · Annals of Neurology · doi:10.1002/ana.23650 · Cited by 723 · see citing works
IRIZARRY, M. C., MCNAMARA, M., FEDORCHAK, K., HSIAO, K., & HYMAN, B. T. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199709000-00002 · Cited by 649 · see citing works
Comparing predictors of conversion and decline in mild cognitive impairment
Landau, S. M., Harvey, D., Madison, C. M., Reiman, E. M., Foster, N. L., Aisen, P. S., Petersen, R. C., Shaw, L. M., Trojanowski, J. Q., Jack, C. R., et al. (2010) · Neurology · doi:10.1212/wnl.0b013e3181e8e8b8 · Cited by 616 · see citing works
Simpson, I. A., Chundu, K. R., Davies‐Hill, T., Honer, W. G., & Davies, P. (1994) · Annals of Neurology · doi:10.1002/ana.410350507 · Cited by 490 · see citing works
Mosconi, L., Mistur, R., Switalski, R., Tsui, W. H., Glodzik, L., Li, Y., Pirraglia, E., De Santi, S., Reisberg, B., Wisniewski, T., et al. (2009) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-008-1039-z · Cited by 487 · see citing works
Isolation and Culture of Mouse Cortical Astrocytes
Schildge, S., Bohrer, C., Beck, K., & Schachtrup, K. (2013) · Journal of Visualized Experiments · doi:10.3791/50079 · Cited by 453 · see citing works
SOD1 rescues cerebral endothelial dysfunction in mice overexpressing amyloid precursor protein
Iadecola, C., Zhang, F., Niwa, K., Eckman, C., Turner, S. K., Fischer, E., Younkin, S., Borchelt, D. R., Hsiao, K. K., & Carlson, G. A. (1999) · Nature Neuroscience · doi:10.1038/5715 · Cited by 399 · see citing works
GLUT-1 deficiency syndrome caused by haploinsufficiency of the blood-brain barrier hexose carrier
Seidner, G. A., Alvarez, M. B. G., Yeh, J., O’Driscoll, K. R., Klepper, J., Stump, T., Wang, D., Spinner, N. B., Birnbaum, M. J., & Vivo, D. C. D. (1998) · Nature Genetics · doi:10.1038/ng0298-188 · Cited by 383 · see citing works
Reduced Glucose Transporter at the Blood‐Brain Barrier and in Cerebral Cortex in Alzheimer Disease
Kalaria, R. N., & Harik, S. I. (1989) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1989.tb07399.x · Cited by 338 · see citing works
Paul, J., Strickland, S., & Melchor, J. P. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070304 · Cited by 319 · see citing works
Role of the MEOX2 homeobox gene in neurovascular dysfunction in Alzheimer disease
Wu, Z., Guo, H., Chow, N., Sallstrom, J., Bell, R. D., Deane, R., Brooks, A. I., Kanagala, S., Rubio, A., Sagare, A., et al. (2005) · Nature Medicine · doi:10.1038/nm1287 · Cited by 280 · see citing works
Self-citationThe Pericyte: A Forgotten Cell Type with Important Implications for A lzheimer's Disease?
Winkler, E. A., Sagare, A. P., & Zloković, B. V. (2014) · Brain Pathology · doi:10.1111/bpa.12152 · Cited by 275 · see citing works
Self-citation(2006) · PubMed · Cited by 269 · see citing works
SRF and myocardin regulate LRP-mediated amyloid-β clearance in brain vascular cells
Bell, R. D., Deane, R., Chow, N., Long, X., Sagare, A., Singh, I., Streb, J. W., Guo, H., Rubio, A., Van Nostrand, W., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1819 · Cited by 261 · see citing works
Self-citationAβ1–40-related reduction in functional hyperemia in mouse neocortex during somatosensory activation
Niwa, K., Younkin, L. H., Ebeling, C., Turner, S. K., Westaway, D. A., Younkin, S. G., Ashe, K. H., Carlson, G. A., & Iadecola, C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.17.9735 · Cited by 244 · see citing works
Phenotypic Spectrum of Glucose Transporter Type 1 Deficiency Syndrome (Glut1 DS)
Pearson, T. S., Akman, Ç. I., Hinton, V. J., Engelstad, K., & Vivo, D. C. D. (2013) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-013-0342-7 · Cited by 226 · see citing works
Developmental Expression of GLUT1 and GLUT3 Glucose Transporters in Rat Brain
Vannucci, S. J. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.62010240.x · Cited by 223 · see citing works
Uchida, Y., Tachikawa, M., Obuchi, W., Hoshi, Y., Tomioka, Y., Ohtsuki, S., & Terasaki, T. (2013) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-10-21 · Cited by 222 · see citing works
Niwa, K., Kazama, K., Younkin, S. G., Carlson, G. A., & Iadecola, C. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0460 · Cited by 218 · see citing works
Chow, N., Bell, R. D., Deane, R., Streb, J. W., Chen, J., Brooks, A., Van Nostrand, W., Miano, J. M., & Zlokovic, B. V. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608251104 · Cited by 209 · see citing works
Self-citationGLUT-1 Expression in the Cerebra of Patients with Alzheimer’s Disease
Mooradian, A. D., Chung, H. C., & Shah, G. N. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00111-5 · Cited by 199 · see citing works
Young, C. D., Lewis, A. S., Rudolph, M. C., Ruehle, M. D., Jackman, M. R., Yun, U. J., Ilkun, O. L., Pereira, R. O., Abel, E. D., & Anderson, S. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023205 · Cited by 194 · see citing works
Self-citationDiminished Glucose Transport in Alzheimer's Disease: Dynamic PET Studies
Jagust, W. J., Seab, J. P., Huesman, R. H., Valk, P. E., Mathis, C. A., Reed, B., Coxson, P. G., & Budinger, T. F. (1991) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.1991.65 · Cited by 187 · see citing works
A mouse model for Glut-1 haploinsufficiency
Wang, D., Pascual, J. M., Yang, H., Engelstad, K., Mao, X., Cheng, J., Yoo, J. H., Noebels, J. L., & Vivo, D. C. D. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl032 · Cited by 185 · see citing works
Fowler, S. C., Birkestrand, B., Chen, R., Moss, S. J., Vorontsova, E., Wang, G., & Zarcone, T. J. (2001) · Journal of Neuroscience Methods · doi:10.1016/s0165-0270(01)00359-4 · Cited by 182 · see citing works
Protas, H. D., Chen, K., Langbaum, J. B. S., Fleisher, A. S., Alexander, G. E., Lee, W., Bandy, D., de Leon, M. J., Mosconi, L., Buckley, S., et al. (2013) · JAMA Neurology · doi:10.1001/2013.jamaneurol.286 · Cited by 161 · see citing works
Inhibition of Angiogenesis by Aβ Peptides
Paris, D., Townsend, K., Quadros, A., Humphrey, J., Sun, J., Brem, S., Wotoczek-Obadia, M., DelleDonne, A., Patel, N., Obregon, D. F., et al. (2004) · Angiogenesis · doi:10.1023/b:agen.0000037335.17717.bf · Cited by 148 · see citing works
Impaired angiogenesis in a transgenic mouse model of cerebral amyloidosis
Paris, D., Patel, N. S., DelleDonne, A., Quadros, A., Smeed, R., & MULLAN, M. J. (2004) · Neuroscience Letters · doi:10.1016/j.neulet.2004.05.017 · Cited by 133 · see citing works
Piert, M., Koeppe, R. A., Giordani, B., Berent, S., & KUHL, D. E. (1996) · PubMed · Cited by 131 · see citing works
Obermoeller, L. M., Li, Y., Osaka, H., FitzGerald, D. J., Schwartz, A. L., & Bu, G. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.899 · Cited by 125 · see citing works
Benarroch, E. E. (2014) · Neurology · doi:10.1212/wnl.0000000000000328 · Cited by 124 · see citing works
Glut1/SLC2A1 is crucial for the development of the blood‐brain barrier in vivo
Zheng, P., Romme, E., van der Spek, P. J., Dirven, C. M. F., Willemsen, R., & Kros, J. M. (2010) · Annals of Neurology · doi:10.1002/ana.22318 · Cited by 119 · see citing works
Zloković, B. V., Mačkić, J. B., Wang, L., McComb, J. G., & McDonough, A. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53058-1 · Cited by 117 · see citing works
Regulation of glycolysis and pentose–phosphate pathway by nitric oxide: Impact on neuronal survival
Bolaños, J. P., Delgado‐Esteban, M., Herrero-Méndez, Á., Fernández-Fernández, S., & Almeida, Á. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.04.011 · Cited by 116 · see citing works
Differential effect of <i>APOE</i> genotype on amyloid load and glucose metabolism in AD dementia
Ossenkoppele, R., van der Flier, W. M., Zwan, M. D., Adriaanse, S. F., Boellaard, R., Windhorst, A. D., Barkhof, F., Lammertsma, A. A., Scheltens, P., & van Berckel, B. N. M. (2013) · Neurology · doi:10.1212/wnl.0b013e31827f0889 · Cited by 112 · see citing works
Zeller, K., Rahner-Welsch, S., & Kuschinsky, W. (1997) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199702000-00010 · Cited by 106 · see citing works
Muneer, P. M. A., Alikunju, S., Szlachetka, A. M., Murrin, L. C., & Haorah, J. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-23 · Cited by 104 · see citing works
Horwood, N., & Davies, D. C. (1994) · Virchows Archiv · doi:10.1007/bf00193951 · Cited by 97 · see citing works
Comparison of three commercially available ektacytometers with different shearing geometries
Baskurt, O. K., Hardeman, M. R., Üyüklü, M., Ülker, P., Cengiz, M., Németh, N., Shin, S., Alexy, T., & Meiselman, H. J. (2009) · Biorheology · doi:10.3233/bir-2009-0536 · Cited by 94 · see citing works
Self-citationGlucose transporter plasticity during memory processing
Choeiri, C., Staines, W. A., Miki, T., Seino, S., & Messier, C. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.09.011 · Cited by 76 · see citing works
Llorente‐Cortés, V., Costales, P., Bernués, J., Camino-López, S., & Badimón, L. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.04.008 · Cited by 67 · see citing works
Mosconi, L., Rinne, J. O., Tsui, W. H., Murray, J., Li, Y., Glodzik, L., McHugh, P. F., Williams, S., Cummings, M., Pirraglia, E., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.03.002 · Cited by 67 · see citing works
Blood-Brain Barrier: A Dual Life of MFSD2A?
Zhao, Z., & Zlokovic, B. V. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.012 · Cited by 59 · see citing works
Self-citationLaRue, B., Hogg, E., Sagare, A. P., Jovanovic, S. S., Maness, L. M., Maurer, C. R., Deane, R., & Zloković, B. V. (2004) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2004.04.026 · Cited by 57 · see citing works
Self-citationAllen, A., & Messier, C. (2012) · Behavioural Brain Research · doi:10.1016/j.bbr.2012.11.025 · Cited by 53 · see citing works
Maeda, K., Mies, G., Oláh, L., & Hossmann, K.-A. (2000) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200001000-00003 · Cited by 44 · see citing works
Impaired spine formation and learning in GPCR kinase 2 interacting protein-1 (GIT1) knockout mice
Menon, P., Deane, R., Sagare, A. P., Lane, S. M., Zarcone, T. J., O’Dell, M. R., Chen, Y., Zloković, B. V., & Berk, B. C. (2010) · Brain Research · doi:10.1016/j.brainres.2009.11.084 · Cited by 42 · see citing works
Self-citationUllner, P. M., Nardo, A. D., Goldman, J. E., Schobel, S., Yang, H., Engelstad, K., Wang, D., Şahin, M., & Vivo, D. C. D. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.06.014 · Cited by 34 · see citing works
Agarwal, N., Mojica-Henshaw, M. P., Simmons, E. D., Hussey, D., Ou, C., & Prchal, J. T. (2007) · International Journal of Medical Sciences · doi:10.7150/ijms.4.232 · Cited by 32 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Neuroinflammation and microglial activation in Alzheimer disease: where do we go from here?
Leng, F., & Edison, P. (2021) · Nature Reviews Neurology · doi:10.1038/s41582-020-00435-y · Cited by 3,179 · see citing works
Blood–brain barrier breakdown in Alzheimer disease and other neurodegenerative disorders
Sweeney, M. D., Sagare, A. P., & Zlokovic, B. V. (2018) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.188 · Cited by 3,076 · see citing works
Self-citationBlood-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
Self-citationThe Cellular Phase of Alzheimer’s Disease
De Strooper, B., & Karran, E. (2016) · Cell · doi:10.1016/j.cell.2015.12.056 · Cited by 1,990 · 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
Self-citationSaraiva, C., Praça, C., Ferreira, R., Santos, T., Ferreira, L., & Bernardino, L. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.05.044 · Cited by 1,609 · see citing works
Zhang, J., Zhang, Y., Wang, J., Xia, Y., Zhang, J., & Chen, L. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01911-3 · Cited by 1,138 · see citing works
The role of brain vasculature in neurodegenerative disorders
Sweeney, M. D., Kisler, K., Montagne, A., Toga, A. W., & Zlokovic, B. V. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0234-x · Cited by 998 · 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
Brain metabolism in health, aging, and neurodegeneration
Camandola, S., & Mattson, M. P. (2017) · The EMBO Journal · doi:10.15252/embj.201695810 · Cited by 752 · see citing works
Vascular dysfunction—The disregarded partner of Alzheimer's disease
Sweeney, M. D., Montagne, A., Sagare, A. P., Nation, D. A., Schneider, L. S., Chui, H. C., Harrington, M. G., Pa, J., Law, M., Wang, D. J. J., et al. (2019) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2018.07.222 · Cited by 711 · see citing works
Self-citationAlzheimer’s disease: A matter of blood–brain barrier dysfunction?
Montagne, A., Zhao, Z., & Zlokovic, B. V. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20171406 · Cited by 672 · see citing works
Self-citationVascular heterogeneity and specialization in development and disease
Potente, M., & Mäkinen, T. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.36 · Cited by 653 · see citing works
The dynamic blood–brain barrier
Keaney, J., & Campbell, M. (2015) · The FEBS Journal · doi:10.1111/febs.13412 · Cited by 616 · see citing works
Neurovascular dysfunction and neurodegeneration in dementia and Alzheimer's disease
Nelson, A. R., Sweeney, M. D., Sagare, A. P., & Zlokovic, B. V. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.12.016 · Cited by 559 · see citing works
Self-citationFibrinogen in neurological diseases: mechanisms, imaging and therapeutics
Petersen, M. A., Ryu, J. K., & Akassoglou, K. (2018) · Nature reviews. Neuroscience · doi:10.1038/nrn.2018.13 · Cited by 527 · see citing works
Development and Cell Biology of the Blood-Brain Barrier
Langen, U. H., Ayloo, S., & Gu, C. (2019) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062608 · Cited by 517 · see citing works
Astrocytic Insulin Signaling Couples Brain Glucose Uptake with Nutrient Availability
García‐Cáceres, C., Quarta, C., Varela, L., Gao, Y., Gruber, T., Legutko, B., Jastroch, M., Johansson, P., Ninkovic, J., Yi, C., et al. (2016) · Cell · doi:10.1016/j.cell.2016.07.028 · Cited by 516 · see citing works
Pericyte degeneration leads to neurovascular uncoupling and limits oxygen supply to brain
Kisler, K., Nelson, A. R., Rege, S. V., Ramanathan, A., Wang, Y., Ahuja, A., Lazic, D., Tsai, P. S., Zhao, Z., Zhou, Y., et al. (2017) · Nature Neuroscience · doi:10.1038/nn.4489 · Cited by 497 · see citing works
Self-citationGejl, M., Gjedde, A., Egefjord, L., Møller, A., Hansen, S. B., Vang, K., Rodell, A., Brændgaard, H., Gottrup, H., Schacht, A., et al. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00108 · Cited by 480 · see citing works
Blood-Brain Barrier Dysfunction and the Pathogenesis of Alzheimer’s Disease
Yamazaki, Y., & Kanekiyo, T. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091965 · Cited by 451 · see citing works
Lochhead, J. J., Yang, J., Ronaldson, P. T., & Davis, T. P. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00914 · Cited by 445 · see citing works
Neuronal regulation of the blood–brain barrier and neurovascular coupling
Kaplan, L., Chow, B. W., & Gu, C. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-020-0322-2 · Cited by 431 · see citing works
Age-associated Physiological and Pathological Changes at the Blood-Brain Barrier: A Review
Erdő, F., Denes, L., & de Lange, E. (2017) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16679420 · Cited by 426 · see citing works
Pericyte loss leads to circulatory failure and pleiotrophin depletion causing neuron loss
Nikolakopoulou, A. M., Montagne, A., Kisler, K., Dai, Z., Wang, Y., Huuskonen, M. T., Sagare, A. P., Lazić, D., Sweeney, M. D., Kong, P., et al. (2019) · Nature Neuroscience · doi:10.1038/s41593-019-0434-z · Cited by 382 · see citing works
Self-citationThe Molecular Constituents of the Blood–Brain Barrier
Chow, B. W., & Gu, C. (2015) · Trends in Neurosciences · doi:10.1016/j.tins.2015.08.003 · Cited by 374 · see citing works
Glucose Transporters at the Blood-Brain Barrier: Function, Regulation and Gateways for Drug Delivery
Patching, S. (2017) · Molecular Neurobiology · doi:10.1007/s12035-015-9672-6 · Cited by 315 · see citing works
Han, L., & Jiang, C. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.11.023 · Cited by 358 · see citing works
Astrocyte Biomarkers in Alzheimer’s Disease
Carter, S. F., Herholz, K., Rosa-Neto, P., Pellerin, L., Nordberg, A., & Zimmer, E. R. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2018.11.006 · Cited by 355 · see citing works
Montagne, A., Nikolakopoulou, A. M., Zhao, Z., Sagare, A. P., Si, G., Lazic, D., Barnes, S. R., Daianu, M., Ramanathan, A., Go, A., et al. (2018) · Nature Medicine · doi:10.1038/nm.4482 · Cited by 344 · see citing works
Self-citationRetractedRom, S., Zuluaga‐Ramirez, V., Gajghate, S., Seliga, A., Winfield, M., Heldt, N. A., Kolpakov, M. A., Bashkirova, Y. V., Sabri, A. K., & Persidsky, Y. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1195-5 · Cited by 329 · see citing works
Douce, J. L., Maugard, M., Veran, J., Matos, M., Jégo, P., Vigneron, P.-A., Faivre, É., Toussay, X., Vandenberghe, M. E., Balbastre, Y., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2020.02.004 · Cited by 326 · see citing works
Ketogenic Diet in Alzheimer’s Disease
Rusek, M., Pluta, R., Ułamek-Kozioł, M., & Czuczwar, S. J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20163892 · Cited by 319 · see citing works
Factors influencing the blood-brain barrier permeability
Zhao, Y., Gan, L., Ren, L., Lin, Y., Ma, C., & Lin, X. (2022) · Brain Research · doi:10.1016/j.brainres.2022.147937 · Cited by 291 · see citing works
Govindpani, K., McNamara, L. G., Smith, N. R., Vinnakota, C., Waldvogel, H. J., Faull, R. L. M., & Kwakowsky, A. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8050651 · Cited by 271 · see citing works
Blood-Brain Barrier Disruption by Lipopolysaccharide and Sepsis-Associated Encephalopathy
Peng, X., Luo, Z., He, S., Zhang, L., & Li, Y. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.768108 · Cited by 271 · see citing works
Role of the Blood-Brain Barrier in Central Nervous System Insulin Resistance
Rhea, E. M., & Banks, W. A. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00521 · Cited by 263 · see citing works
Bridging barriers: a comparative look at the blood–brain barrier across organismsPreprint
O’Brown, N. M., Pfau, S. J., & Gu, C. (2018) · Genes & Development · doi:10.1101/gad.309823.117 · Cited by 261 · see citing works
The Impact of Disease Comorbidities in Alzheimer’s Disease
Santiago, J. A., & Potashkin, J. A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.631770 · Cited by 259 · see citing works
Blood-brain barrier transport machineries and targeted therapy of brain diseases
Barar, J., Rafi, M. A., Pourseif, M. M., & Omidi, Y. (2016) · Bioimpacts · doi:10.15171/bi.2016.30 · Cited by 259 · see citing works
Myelin dynamics: protecting and shaping neuronal functions
Saab, A. S., & Nave, K. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.09.013 · Cited by 259 · see citing works
Andersen, J. V., Schousboe, A., & Verkhratsky, A. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102331 · Cited by 259 · see citing works
Myeloid-Cell-Derived VEGF Maintains Brain Glucose Uptake and Limits Cognitive Impairment in Obesity
Jaïs, A., Solas, M., Backes, H., Chaurasia, B., Kleinridders, A., Theurich, S., Mauer, J., Steculorum, S. M., Hampel, B., Goldau, J., et al. (2016) · Cell · doi:10.1016/j.cell.2016.03.033 · Cited by 253 · see citing works
Hussain, B., Fang, C., & Chang, J. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.688090 · Cited by 251 · see citing works
Gpr124 is essential for blood–brain barrier integrity in central nervous system disease
Chang, J., Mancuso, M. R., Maier, C. M., Liang, X., Yuki, K., Yang, L., Kwong, J. W., Wang, J., Rao, V., Vallon, M., et al. (2017) · Nature Medicine · doi:10.1038/nm.4309 · Cited by 250 · see citing works
Tight junction modulation of the blood brain barrier: CNS delivery of small molecules
Greene, C., & Campbell, M. (2016) · Tissue Barriers · doi:10.1080/21688370.2015.1138017 · Cited by 247 · see citing works
Veys, K., Fan, Z., Ghobrial, M., Bouché, A., García‐Caballero, M., Vriens, K., Conchinha, N. V., Seuwen, A., Schlegel, F., Gorski, T., et al. (2020) · Circulation Research · doi:10.1161/circresaha.119.316463 · Cited by 246 · see citing works
Self-citationDewanjee, S., Chakraborty, P., Bhattacharya, H., Chacko, L., Singh, B., Chaudhary, A., Javvaji, K., Pradhan, S. R., Vallamkondu, J., Dey, A., et al. (2022) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2022.09.032 · Cited by 235 · see citing works
Review of Current Strategies for Delivering Alzheimer’s Disease Drugs across the Blood-Brain Barrier
Wong, K. H., Riaz, M. K., Xie, Y., Zhang, X., Liu, Q., Chen, H., Bian, Z., Chen, X., Lü, A., & Yang, Z. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20020381 · Cited by 219 · see citing works
Activation of Wnt/β-catenin pathway mitigates blood–brain barrier dysfunction in Alzheimer’s disease
Wang, Q., Huang, X., Su, Y., Yin, G., Wang, S., Yu, B., Li, H., Qi, J., Chen, H., Zeng, W., et al. (2022) · Brain · doi:10.1093/brain/awac236 · Cited by 219 · see citing works
Clearance of Amyloid Beta and Tau in Alzheimer’s Disease: from Mechanisms to Therapy
Xin, S.-H., Tan, L., Cao, X., Yu, J.-T., & Tan, L. (2018) · Neurotoxicity Research · doi:10.1007/s12640-018-9895-1 · Cited by 213 · 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
Li, Y., Zhang, J., Wan, J., Liu, A., & Sun, J. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110887 · Cited by 212 · see citing works
Glucose Transporters in Brain: In Health and in Alzheimer’s Disease
Szablewski, L. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-160841 · Cited by 211 · see citing works
Castelli, V., Benedetti, E., Antonosante, A., Catanesi, M., Pitari, G., Ippoliti, R., Cimini, A., & d’Angelo, M. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00132 · Cited by 211 · see citing works
Tian, Z., Ji, X., & Liu, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116224 · Cited by 210 · see citing works
Ramanathan, A., Nelson, A. R., Sagare, A. P., & Zlokovic, B. V. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00136 · Cited by 205 · see citing works
Self-citationGlucose metabolic crosstalk and regulation in brain function and diseases
Zhang, S., Lachance, B. B., Mattson, M. P., & Jia, X. (2021) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2021.102089 · Cited by 205 · see citing works
Yamazaki, Y., Shinohara, M., Shinohara, M., Yamazaki, A., Murray, M. E., Liesinger, A. M., Heckman, M. G., Lesser, E. R., Parisi, J. E., Petersen, R. C., et al. (2019) · Brain · doi:10.1093/brain/awz011 · Cited by 202 · see citing works
Development of Novel Therapeutics Targeting the Blood–Brain Barrier: From Barrier to Carrier
Li, J., Zheng, M., Shimoni, O., Banks, W. A., Bush, A. I., Gamble, J. R., & Shi, B. (2021) · Advanced Science · doi:10.1002/advs.202101090 · Cited by 202 · see citing works
Cedernaes, J., Osorio, R. S., Varga, A. W., Kam, K., Schiöth, H. B., & Benedict, C. (2016) · Sleep Medicine Reviews · doi:10.1016/j.smrv.2016.02.002 · Cited by 200 · see citing works
Chen, T., Dai, Y., Hu, C., Lin, Z., Wang, S., Yang, J., Zeng, L., Li, S., & Li, W. (2024) · Fluids and Barriers of the CNS · doi:10.1186/s12987-024-00557-1 · Cited by 201 · see citing works
Human pluripotent stem cell–derived brain pericyte–like cells induce blood-brain barrier properties
Stebbins, M. J., Gastfriend, B. D., Canfield, S. G., Lee, M.-S., Richards, D., Faubion, M. G., Li, W.-J., Daneman, R., Palecek, S. P., & Shusta, E. V. (2019) · Science Advances · doi:10.1126/sciadv.aau7375 · Cited by 195 · see citing works
Montagne, A., Nikolakopoulou, A. M., Huuskonen, M. T., Sagare, A. P., Lawson, E. J., Lazic, D., Rege, S. V., Grond, A., Zuniga, E., Barnes, S. R., et al. (2021) · Nature Aging · doi:10.1038/s43587-021-00073-z · Cited by 188 · see citing works
Self-citationVascular contributions to Alzheimer's disease
Eisenmenger, L. B., Peret, A., Famakin, B. M., Spahic, A., Roberts, G. S., Bockholt, J. H., Johnson, K. M., & Paulsen, J. S. (2022) · Translational research · doi:10.1016/j.trsl.2022.12.003 · Cited by 179 · see citing works
Gut commensal derived-valeric acid protects against radiation injuries
Li, Y., Dong, J., Xiao, H., Zhang, S., Wang, B., Cui, M., & Fan, S. (2020) · Gut Microbes · doi:10.1080/19490976.2019.1709387 · Cited by 174 · see citing works
A Systematic Review of Glucose Transport Alterations in Alzheimer's Disease
Kyrtata, N., Emsley, H. C. A., Sparasci, O., Parkes, L. M., & Dickie, B. R. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.626636 · Cited by 171 · see citing works
Timper, K., del Río-Martín, A., Cremer, A. L., Bremser, S., Alber, J., Giavalisco, P., Varela, L., Heilinger, C., Nolte, H., Trifunovic, A., et al. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.05.001 · Cited by 170 · see citing works
Sato, N., & Morishita, R. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00199 · Cited by 164 · see citing works
Blood-Brain Glucose Transfer in Alzheimer’s disease: Effect of GLP-1 Analog Treatment
Gejl, M., Brock, B., Egefjord, L., Vang, K., Rungby, J., & Gjedde, A. (2017) · Scientific Reports · doi:10.1038/s41598-017-17718-y · Cited by 163 · see citing works
Precision drug delivery to the central nervous system using engineered nanoparticles
Gao, J., Xia, Z. J., Gunasekar, S., Jiang, C., Karp, J. M., & Joshi, N. (2024) · Nature Reviews Materials · doi:10.1038/s41578-024-00695-w · Cited by 162 · see citing works
Endothelial response to glucose: dysfunction, metabolism, and transport
Clyne, A. M. (2021) · Biochemical Society Transactions · doi:10.1042/bst20200611 · Cited by 160 · see citing works
Blood–brain barrier link to human cognitive impairment and Alzheimer’s disease
Barisano, G., Montagne, A., Kisler, K., Schneider, J. A., Wardlaw, J. M., & Zlokovic, B. V. (2022) · Nature Cardiovascular Research · doi:10.1038/s44161-021-00014-4 · Cited by 157 · see citing works
Microglia-Specific Metabolic Changes in Neurodegeneration
Aldana, B. I. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.03.006 · Cited by 153 · see citing works
Blood-Brain Barriers in Obesity
Rhea, E. M., Salameh, T. S., Logsdon, A. F., Hanson, A. J., Erickson, M. A., & Banks, W. A. (2017) · The AAPS Journal · doi:10.1208/s12248-017-0079-3 · Cited by 152 · see citing works
Polymer-Based Drug Delivery Systems for Cancer Therapeutics
Ding, L., Agrawal, P. P., Singh, S. K., Chhonker, Y. S., Sun, J., & Murry, D. J. (2024) · Polymers · doi:10.3390/polym16060843 · Cited by 152 · see citing works
Blood brain barrier: A review of its anatomy and physiology in health and disease
Sharif, Y., Jumah, F., Coplan, L., Krosser, A., Sharif, Κ., & Tubbs, R. S. (2018) · Clinical Anatomy · doi:10.1002/ca.23083 · Cited by 143 · see citing works
Emerging links between cerebrovascular and neurodegenerative diseases—a special role for pericytes
Lendahl, U., Nilsson, P., & Betsholtz, C. (2019) · EMBO Reports · doi:10.15252/embr.201948070 · Cited by 141 · see citing works
Neuroketotherapeutics: A modern review of a century-old therapy
Koppel, S. J., & Swerdlow, R. H. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.05.019 · Cited by 140 · see citing works
Skike, C. E. V., Jahrling, J. B., Dorigatti, A. O., Sayre, N. L., Hussong, S. A., Ungvari, Z. I., Lechleiter, J. D., & Galván, V. (2017) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00570.2017 · Cited by 140 · see citing works
Current and emerging avenues for Alzheimer's disease drug targets
Loera‐Valencia, R., Cedazo-Mı́nguez, Á., Kenigsberg, P.-A., Page, G., Duarte, A. I., Giusti, P., Zusso, M., Robert, P. H., Frisoni, G. B., Cattaneo, A., et al. (2019) · Journal of Internal Medicine · doi:10.1111/joim.12959 · Cited by 139 · see citing works
Restraint stress-induced morphological changes at the blood-brain barrier in adult rats
Sántha, P., Veszelka, S., Hoyk, Z., Mészáros, M., Walter, F. R., Tóth, A. E., Kiss, L., Kincses, A., Oláh, Z., Seprényi, G., et al. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00088 · Cited by 136 · see citing works
Brain Metabolic Alterations in Alzheimer’s Disease
Ardanaz, C. G., Ramírez, M. J., & Solas, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23073785 · Cited by 130 · see citing works
Blood-brain barrier integrity in the pathogenesis of Alzheimer’s disease
Huang, Z., Wong, L., Su, Y., Huang, X., Wang, N., Chen, H., & Yi, C. (2020) · Frontiers in Neuroendocrinology · doi:10.1016/j.yfrne.2020.100857 · Cited by 130 · see citing works
High-speed volumetric two-photon fluorescence imaging of neurovascular dynamics
Fan, J. L., Rivera, J. A., Sun, W., Peterson, J., Haeberle, H., Rubin, S., & Ji, N. (2020) · Nature Communications · doi:10.1038/s41467-020-19851-1 · Cited by 129 · see citing works
Endothelial LRP1 protects against neurodegeneration by blocking cyclophilin A
Nikolakopoulou, A. M., Wang, Y., Ma, Q., Sagare, A. P., Montagne, A., Huuskonen, M. T., Rege, S. V., Kisler, K., Dai, Z., Körbelin, J., et al. (2021) · The Journal of Experimental Medicine · doi:10.1084/jem.20202207 · Cited by 128 · see citing works
Self-citationKetogenic Diets for Adult Neurological Disorders
McDonald, T. J. W., & Cervenka, M. C. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-0666-8 · Cited by 127 · see citing works
Pathological changes within the cerebral vasculature in Alzheimer’s disease: New perspectives
Fisher, R. A., Miners, J. S., & Love, S. (2022) · Brain Pathology · doi:10.1111/bpa.13061 · Cited by 127 · see citing works
Blood–Brain Barrier Dysfunction in the Pathogenesis of Major Depressive Disorder
Wu, S., Yin, Y., & Du, L. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-021-01153-9 · Cited by 126 · see citing works
Revisiting the blood-brain barrier: A hard nut to crack in the transportation of drug molecules
Harilal, S., Jose, J., Parambi, D. G. T., Kumar, R., Unnikrishnan, M. K., Uddin, M. S., Mathew, G. E., Pratap, R., Marathakam, A., & Mathew, B. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.03.018 · Cited by 124 · see citing works
Fatty acids and their therapeutic potential in neurological disorders
Lei, E., Vacy, K., & Boon, W. C. (2016) · Neurochemistry International · doi:10.1016/j.neuint.2016.02.014 · Cited by 123 · see citing works
Diversity of astroglial responses across human neurodegenerative disorders and brain aging
Ferrer, I. (2017) · Brain Pathology · doi:10.1111/bpa.12538 · Cited by 123 · see citing works
Kim, S., Jung, U. J., & Kim, S. R. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14020386 · Cited by 123 · see citing works
Swarup, A., Samuels, I. S., Bell, B. A., Han, J. Y. S., Du, J., Massenzio, E., Abel, E. D., Boesze-Battaglia, K., Peachey, N. S., & Philp, N. J. (2019) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00410.2018 · Cited by 122 · see citing works
Self-citationMattishent, K., & Loke, Y. K. (2015) · Diabetes Obesity and Metabolism · doi:10.1111/dom.12587 · Cited by 121 · see citing works
Contributions of Aging to Cerebral Small Vessel Disease
Silva, T. M. D., & Faraci, F. M. (2019) · Annual Review of Physiology · doi:10.1146/annurev-physiol-021119-034338 · Cited by 120 · see citing works
Neuropathogenesis-on-chips for neurodegenerative diseases
Amartumur, S., Nguyen, H. M., Huynh, T., Kim, T. S., Woo, R., Oh, E., Kim, K. K., Lee, L. P., & Heo, C. (2024) · Nature Communications · doi:10.1038/s41467-024-46554-8 · Cited by 120 · see citing works
Zhao, L., Li, Z., Vong, J. S. L., Chen, X., Lai, H. M., Yan, L. Y. C., Huang, J., Sy, S. K. H., Tian, X. Y., Huang, Y., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-18249-3 · Cited by 119 · see citing works
Cognitive dysfunction in diabetes: abnormal glucose metabolic regulation in the brain
Zhang, S., Zhang, Y., Wen, Z., Yang, Y., Bu, T., Bu, X., & Ni, Q. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1192602 · Cited by 119 · see citing works
Tang, M., Gao, G., Rueda, C. B., Yu, H., Thibodeaux, D. N., Awano, T., Engelstad, K., Sanchez‐Quintero, M. J., Yang, H., Li, F., et al. (2017) · Nature Communications · doi:10.1038/ncomms14152 · Cited by 118 · see citing works
- Authors
- Winkler, E. A., Nishida, Y., Sagare, A. P., Rege, S. V., Bell, R. D., Perlmutter, D., Sengillo, J. D., Hillman, S., Kong, P., Nelson, A. R., Sullivan, J. S., Zhao, Z., Meiselman, H. J., Wenby, R. B., Soto, J., Abel, E. D., Makshanoff, J., Zuniga, E., De Vivo, D. C., & Zlokovic, B. V.
- Affiliations
- University of Southern California (US)
- Tokyo Medical and Dental University (JP)
- University of Rochester Medicine (US)
- University of Iowa (US)
- ORCID
- Venue
- Nature Neuroscience
- Published
- 2015-03-02
- Volume
- 18
- Issue
- 4
- Pages
- 521-530
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- PMC
- PMC4734893
- OpenAlex
- W1974266381
- Cited by
- 689
- References
- 63
- Citations by year
- 2026: 65 · 2025: 72 · 2024: 65 · 2023: 62 · 2022: 79 · 2021: 78 · 2020: 62 · 2019: 49 · 2018: 52 · 2017: 47 · 2016: 38 · 2015: 20
- FWCI
- 27.97
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- University of Southern California
- National Institutes of Health
- National Institute on Aging (R01AG023084, R01AG039452, R37AG023084, AG039452, RF1AG039452, AG023084)
- National Heart, Lung, and Blood Institute (U01HL087947)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK092065)
- National Institute of Neurological Disorders and Stroke (NS034467, R37NS034467, R01NS034467)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neurological Disease Mechanisms and Treatments
- Keywords
- GLUT1, Alzheimer's disease, blood-brain barrier, brain endothelium, amyloid-beta, amyloid-beta clearance, glucose transport, neurodegeneration, cerebrovascular dysfunction, cognitive impairment, therapeutic target
- MeSH terms
- Alzheimer Disease, Animals, Blood-Brain Barrier, Cerebrovascular Circulation, Disease Models, Animal, Endothelium, Vascular, Mice, Inbred C57BL, Mice, Transgenic, Amyloid beta-Peptides, Glucose Transporter Type 1, Mice
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
