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P-glycoprotein deficiency at the blood-brain barrier increases amyloid- deposition in an Alzheimer disease mouse model
Open accessAbstract
Accumulation of amyloid-beta (Abeta) within extracellular spaces of the brain is a hallmark of Alzheimer disease (AD). In sporadic, late-onset AD, there is little evidence for increased Abeta production, suggesting that decreased elimination from the brain may contribute to elevated levels of Abeta and plaque formation. Efflux transport of Abeta across the blood-brain barrier (BBB) contributes to Abeta removal from the brain. P-glycoprotein (Pgp) is highly expressed on the luminal surface of brain capillary endothelial cells and contributes to the BBB. In Pgp-null mice, we show that [I]Abeta40 and [I]Abeta42 microinjected into the CNS clear at half the rate that they do in WT mice. When amyloid precursor protein-transgenic (APP-transgenic) mice were administered a Pgp inhibitor, Abeta levels within the brain interstitial fluid significantly increased within hours of treatment. Furthermore, APP-transgenic, Pgp-null mice had increased levels of brain Abeta and enhanced Abeta deposition compared with APP-transgenic, Pgp WT mice. These data establish a direct link between Pgp and Abeta metabolism in vivo and suggest that Pgp activity at the BBB could affect risk for developing AD as well as provide a novel diagnostic and therapeutic target.
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“Before injection of tracer molecules, animals recovered for 4 to 6 hours, a time point that precedes the start of the substantial inflammatory process, as assessed by histological analysis of tissue (negative staining for reactive astrocytes [GFAP] and reactive microglia [antiphosphotyrosine]), but allows partial BBB repair for large molecules, as reported previously (15,61).”
From Endothelial LRP1 transports amyloid-β1–42 across the blood-brain barrier (2015) · cites this paper as [61]
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“ABCB1 contributes to Alzheimer's A 𝛃 toxin clearance from brain-to-blood (115, 632).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [115]
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“but it is now clear that ABCB1 is also involved in A peptide transport across the BBB.”
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“Whereas some studies have reported a role for ABCB1 in A peptide elimination from the brain [37,67]”
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Citations
Cites
Multidrug resistance in cancer: role of ATP–dependent transporters
Gottesman, M. M., Fojo, T., & Bates, S. E. (2002) · Nature Reviews Cancer · doi:10.1038/nrc706 · Cited by 5,536
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Hoffmeyer, S., Burk, O., von Richter, O., Arnold, H., Brockmöller, J., Johne, A., Cascorbi, I., Gerloff, T., Roots, I., Eichelbaum, M. F., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.7.3473 · Cited by 2,366
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
BIOCHEMICAL, CELLULAR, AND PHARMACOLOGICAL ASPECTS OF THE MULTIDRUG TRANSPORTER
Ambudkar, S. V., Dey, S., Hrycyna, C. A., Ramachandra, M., Pastan, I. H., & Gottesman, M. M. (1999) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.39.1.361 · Cited by 2,059
Farris, W., Mansourian, S., Chang, Y., Lindsley, L., Eckman, E. A., Frosch, M. P., Eckman, C. B., Tanzi, R. E., Selkoe, D. J., & Guénette, S. Y. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0230450100 · Cited by 1,526
RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain
Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426
Shibata, M., Yamada, S., Kumar, S. R., Calero, M., Bading, J., Frangione, B., Holtzman, D. M., Miller, C. A., Strickland, D. K., Ghiso, J., et al. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10498 · Cited by 1,413
Polymorphisms in human MDR1 (P-glycoprotein): recent advances and clinical relevance
Marzolini, C. (2004) · Clinical Pharmacology & Therapeutics · doi:10.1016/j.clpt.2003.09.012 · Cited by 907
Lack of apolipoprotein E dramatically reduces amyloid β-peptide deposition
Bales, K. R., Verina, T., Dodel, R. C., Du, Y., Altstiel, L., Bender, M., Hyslop, P., Johnstone, E. M., Little, S. P., Cummins, D. J., et al. (1997) · Nature Genetics · doi:10.1038/ng1197-263 · Cited by 830
Cited by
Sorted by citations
Items 501–600 of 662
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García-Varela, L., Mossel, P., Benadiba, M., Savolainen, H., Colabufo, N. A., Windhorst, A. D., Elsinga, P. H., van Waarde, A., & Luurtsema, G. (2020) · Springer eBooks · doi:10.1007/978-3-030-53176-8_22 · Cited by 8
Microtubule-Stabilizing Agents for Alzheimer’s and Other Tauopathies
Ballatore, C., Smith, A. B., Lee, V. M. ‐., Trojanowski, J. Q., & Brunden, K. R. (2016) · Topics in medicinal chemistry · doi:10.1007/7355_2016_15 · Cited by 7
Aspectos celulares e fisiológicos da Barreira Hematoencefálica
Vieira, G. D. D., & de Sousa, C. M. (2013) · Journal of Health & Biological Sciences · doi:10.12662/2317-3076jhbs.v1i4.38.p166.2013 · Cited by 8
A Set of Dysregulated Target Genes to Reduce Neuroinflammation at Molecular Level
Massimini, M., Bachetti, B., Vedove, E. D., Benvenga, A., Pierro, F. D., & Bernabò, N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137175 · Cited by 7
Ji, B., Cen, J., Liu, L., & He, L. (2013) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2013.10.005 · Cited by 7
Fat and Lipid Metabolism and the Involvement of Apolipoprotein E in Alzheimer's Disease
Hone, E., Lim, F., & Martins, I. J. (2019) · Wiley eBooks · doi:10.1002/9781119356752.ch7 · Cited by 8
Shao, X., Shou, Q., Felix, K., Ojogho, B., Jiang, X., Gold, B. T., Herting, M. M., Goldwaser, E. L., Kochunov, P., Hong, L. E., et al. (2024) · eLife · doi:10.7554/elife.96155.2 · Cited by 10
The glycosaminoglycan chains of perlecan regulate the perivascular fluid transport
Singh, A., Kaakinen, M., Elamaa, H., Kiviniemi, V. J., & Eklund, L. (2025) · Fluids and Barriers of the CNS · doi:10.1186/s12987-025-00648-7 · Cited by 7
SHARMA, A. K., Mannan, A., & Singh, T. G. (2025) · Metabolic Brain Disease · doi:10.1007/s11011-025-01642-6 · Cited by 7
Duong, Q.-V., Kintzing, M. L., Kintzing, W. E., Abdallah, I. M., Brannen, A. D., & Kaddoumi, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061489 · Cited by 6
Recent advances in drug transporter sciences: highlights from the year 2020
Chothe, P. P., Nakakariya, M., Rotter, C. J., Sandoval, P., & Tohyama, K. (2021) · Drug Metabolism Reviews · doi:10.1080/03602532.2021.1963270 · Cited by 6
Wölfl‐Duchek, M., Mairinger, S., Hernández-Lozano, I., Filip, T., Zoufal, V., Löbsch, M., Stanek, J., Kuntner, C., Wanek, T., Bauer, M., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23126514 · Cited by 6
Dudchenko, N. G., Chimagomedova, A. S., Васенина, Е. Е., & Levin, O. S. (2022) · S S Korsakov Journal of Neurology and Psychiatry · doi:10.17116/jnevro202212207120 · Cited by 6
Rai, A., Ojiakor, O. A., & Rylett, R. J. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15904 · Cited by 6
Manda, S., Wani, A., Bharate, S. S., Vishwakarma, R. A., Kumar, A., & Bharate, S. B. (2016) · MedChemComm · doi:10.1039/c6md00300a · Cited by 6
Nanoformulations of Antiepileptic Drugs: In Vitro and In Vivo Studies
Ruiz, M. E., & Castro, G. R. (2016) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-6355-3_16 · Cited by 7
Krohn, M., Wanek, T., Menet, M., Noack, A., Declèves, X., Langer, O., Löscher, W., & Pahnke, J. (2018) · European Journal of Microbiology and Immunology · doi:10.1556/1886.2018.00008 · Cited by 6
[Guideline for hyperlipidemia].
Seishima, M. (2003) · PubMed · Cited by 6
Cheow, H., Ruparelia, P. R., Shankar, S., Szczepura, K. R., Ballinger, J. R., Hartman, N., Chilvers, E. R., & Peters, A. M. (2009) · Nuclear Medicine Communications · doi:10.1097/mnm.0b013e32832b9a2d · Cited by 6
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Ramkissoon, A., Shapiro, A. M., Loniewska, M. M., & Wells, P. G. (2013) · Wiley eBooks · doi:10.1002/9781118355886.ch10 · Cited by 6
Age-Related Decline in BBB Function is More Pronounced in Males than FemalesPreprint
Shao, X., Shou, Q., Felix, K., Ojogho, B., Jiang, X., Gold, B. T., Herting, M. M., Goldwaser, E. L., Kochunov, P., Hong, L. E., et al. (2024) · eLife · doi:10.7554/elife.96155.1 · Cited by 6
Chen, Y., Sun, X., Xi, Y., Luo, Z., Lai, H., Zhu, D., Zhang, Y., Xu, F., Li, J., Zhou, J., et al. (2025) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2025.10.016 · Cited by 9
Aging Reduces ATP-Binding Cassette Transporter Expression in Brain Microvessels of Mice
Wada, Y., Inoko, M., Ishihara, K., Fukumoto, K., Tsurudome, Y., Horiguchi, M., Fujimura, A., & Ushijima, K. (2025) · Pharmaceuticals · doi:10.3390/ph18020191 · Cited by 5
The Expression and Function of ABC Transporters at the Blood-Brain Barrier
Zhang, W., Bamji‐Mirza, M., Chang, N., Haqqani, A. S., & Stanimirovic, D. B. (2015) · CRC Press eBooks · doi:10.1201/b18606-8 · Cited by 5
Latina, V., Atlante, A., Malerba, F., Regina, F. L., Balzamino, B. O., Micera, A., Pignataro, A., Stigliano, E., Cavallaro, S., Calissano, P., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119683 · Cited by 5
Yasutaka, Y., Watanabe, T., Nakashima, A., Matsumoto, J., Futagami, K., Yamauchi, A., & Kataoka, Y. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.12.007 · Cited by 5
Spampinato, S. F., Takeshita, Y., & Obermeier, B. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2289-6_20 · Cited by 5
Blood-Brain Barrier Dysfunction in the Detrimental Brain Function
González‐Candia, A., Rogers, N. K., & Castillo, R. L. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.94572 · Cited by 5
Drugs and Drug Delivery Systems Targeting Amyloid-\b{eta} in Alzheimers DiseasePreprint
Robinson, M. J., Lee, B. Y., & Leonenko, Z. (2017) · arXiv (Cornell University) · doi:10.48550/arxiv.1704.08313 · Cited by 5
Sangha, V., Williams, E. I., Ronaldson, P. T., & Bendayan, R. (2022) · Wiley eBooks · doi:10.1002/9781119739883.ch14 · Cited by 5
Transport pathways across the blood-brain barrier for waste clearance and drug delivery
Gröbner, L. S., & Pietrzik, C. U. (2026) · Fluids and Barriers of the CNS · doi:10.1186/s12987-026-00812-7 · Cited by 4
Li, M.-S., Cen, J., He, L., Liu, L., & Ji, B. (2013) · Journal of Chemotherapy · doi:10.1179/1973947813y.0000000094 · Cited by 6
Modulating Role of TTR in Aβ Toxicity, from Health to Disease
Cardoso, I., Santos, L. M., & Alemi, M. (2016) · InTech eBooks · doi:10.5772/63194 · Cited by 7
Kuai, Z., Xu, Y., Zhao, Q., Liu, J., Guan, S., Qiao, Y., Gong, X., Nie, J., Li, P., Liu, D., et al. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26744 · Cited by 4
Extracellular Amyloid-β Protein Dynamics in Alzheimer’s Disease
Cirrito, J. R. (2012) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-1-4614-4815-0_9 · Cited by 4
Self-citationRegulation of the Blood–Brain Barrier in Health and DiseasePreprint
Rada, C. C., Yuki, K., Ding, J., & Kuo, C. J. (2023) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a041191 · Cited by 4
Kreutzer, E., Short, J. L., & Nicolazzo, J. A. (2024) · Pharmaceutical Research · doi:10.1007/s11095-024-03731-0 · Cited by 4
The Tetrapeptide HAEE Promotes Amyloid-Beta Clearance from the Brain
Mukhina, K. A., Varshavskaya, K. B., Rybak, A. D., Grishchenko, V. V., Kuzubova, E. V., Корокин, М. В., Kechko, O. I., & Mitkevich, V. A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262311591 · Cited by 4
A Age Related Vascular Senescence: Mystery of Blood-brain Barrier Dysfunction in Neurodegeneration
Behl, T., Jayabalan, K., Ballal, S., Sahoo, S., Chellammal, H. S. J., Gulati, M., Anand, K., Jha, S. K., & Gasmi, A. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05984-9 · Cited by 3
Efflux Transporters in the Brain
Potschka, H., & Löscher, W. (2007) · Springer eBooks · doi:10.1007/978-0-387-30380-2_23 · Cited by 3
Greenberg, S. M. (2009) · Cambridge University Press eBooks · doi:10.1017/cbo9780511691836.005 · Cited by 3
Drug transport into the central nervous system: using newer findings about the blood–brain barriers
Banks, W. A. (2012) · Drug Delivery and Translational Research · doi:10.1007/s13346-012-0058-2 · Cited by 4
Dizdarevic, S., Aplin, M., Newport, M. J., Ryan, N., Holt, S. G., Goubet, S., GOLDBERG, L. C., Miles, K. A., & Peters, A. M. (2014) · Nuclear Medicine Communications · doi:10.1097/mnm.0000000000000165 · Cited by 3
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Svetlana, M., Sladojević, N., Richard, F., & Anuska, V. (2011) · InTech eBooks · doi:10.5772/18938 · Cited by 3
Sundaram, G. S. M., Sharma, M., Kaganov, D., Cho, J., Harpstrite, S. E., & Sharma, V. (2016) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2016.02.022 · Cited by 3
Jiang, J., Okochi, M., Tagami, S., Nishitomi, K., Yanagida, K., NAKAYAMA, T., Tatsumi, S., Mori, K., & Takeda, M. (2008) · Psychogeriatrics · doi:10.1111/j.1479-8301.2008.00259.x · Cited by 3
Romanova, L. G., Phillips, H., Calip, G. S., Hauser, K., Peterson, D. A., Lazarov, O., Predescu, D., Predescu, S. A., Schneider, J. A., Kordower, J. H., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/427617 · Cited by 3
In vitro cell models in predicting blood-brain barrier permeability of drugs
Hakkarainen, J. J. (2013) · UEF eRepo (University of Eastern Finland) · Cited by 3
Positron Emission Tomography in Animal Models of Alzheimer’s Disease AmyloidosisPreprint
Ni, R. (2021) · Preprints.org · doi:10.20944/preprints202110.0222.v1 · Cited by 2
Chaves, J. C. S., Wasielewska, J. M., Cuní‐López, C., Rantanen, L. M., Lee, S., Koıstınaho, J., White, A. R., & Oikari, L. E. (2023) · Research Square · doi:10.21203/rs.3.rs-2605800/v1 · Cited by 3
Yin, H., Lu, Z., Deng, Y., Tian, X., & Gong, Q. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102952 · Cited by 6
Ko, H., Lam, B. Y. K., & Mok, V. (2020) · Stroke revisited · doi:10.1007/978-981-10-1433-8_8 · Cited by 2
A circadian clock regulates the blood-brain barrier across phylogeny
Avila, A., & Zhang, S. (2024) · Vitamins and hormones · doi:10.1016/bs.vh.2024.04.004 · Cited by 2
Apolipoprotein E (APOE) Isoforms and Neurobiology of Sporadic Alzheimer’s Disease
Mollica, A., Berardino, G., Bellomo, A., Altamura, M., Panza, F., & Lozupone, M. (2024) · Springer eBooks · doi:10.1007/978-3-031-32035-4_155-1 · Cited by 2
Asante, J., Nagel, C., & Barger, S. W. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251351629 · Cited by 2
Matsumoto, A., Matsumoto, R., Kadoyama, K., Nishimoto, T., Matsuyama, S., & Midorikawa, O. (2009) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-009-9174-3 · Cited by 2
PLGA-based nanoparticles for treatment of cerebral diseases
Chacko, J. B., & Jose, S. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-91215-0.00018-2 · Cited by 2
Blood–Brain Barrier in Alzheimer's Disease
Brito, M. A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813146-6.00025-4 · Cited by 3
Vascular Dysfunction and Neurodegenerative Disease
Gao, Z., Cilento, E. M., Stewart, T., & Zhang, J. (2019) · Springer eBooks · doi:10.1007/978-3-030-25249-6_1 · Cited by 2
Koroev, D. O., Titova, M. A., Volkova, T. D., Oboznaya, M. B., Филатова, М. П., Fufacheva, E. N., Zhmak, M. N., Tsetlin, V. I., Бобкова, Н. В., & Volpina, O. M. (2007) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162007040061 · Cited by 2
Neuroprotective Effects of Extra‐Virgin Olive Oil and its Components in Alzheimer's Disease
Abuznait, A. H., Qosa, H., Mohamed, L. A., Batarseh, Y. S., & Kaddoumi, A. (2017) · Wiley eBooks · doi:10.1002/9781119155195.ch14 · Cited by 2
Leite, D. M., Seifi, M., Ruiz‐Pérez, L., Nguemo, F., Plomann, M., Swinny, J. D., & Battaglia, G. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.07.12.199869 · Cited by 2
ABC Transporters: P-Glycoprotein
Koehn, L. M. (2022) · Springer eBooks · doi:10.1007/978-3-030-84860-6_78 · Cited by 2
Adhicary, S., Nakisli, S., Fanelli, K., & Nielsen, C. M. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-818872-9.00106-0 · Cited by 2
Nimjee, S. M., Grant, G. A., Winn, H. R., & Janigro, D. (2011) · Elsevier eBooks · doi:10.1016/b978-1-4160-5316-3.00009-5 · Cited by 1
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Kong, W., Miao, X., Dang, R., Jiang, P., & Feng, L. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05364-9 · Cited by 1
Seelig, A. (2025) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2025.184483 · Cited by 1
Boundary homogenization and numerical modeling of solute transport across the blood-brain barrier
Yousofvand, R., Handy, G., & Tithof, J. (2025) · Physical review. E · doi:10.1103/qr7v-btpp · Cited by 1
Pyun, J., Noor, A., Runwal, P., Mawal, C., Fuller, O. K., Egan, C. L., Febbraio, M. A., Donnelly, P. S., Short, J. L., Bush, A. I., et al. (2026) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6c00252 · Cited by 1
Yao, M., Liu, A., Xing, L., Song, J., Yang, Y., Yue, X., & Li, H. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103260 · Cited by 1
Is amyloid beta peptide a driver of inflammaging?
Kechko, O. I., Moskalev, A. A., Franceschi, C., Mitkevich, V. A., & Makarov, A. А. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103280 · Cited by 1
Multiple Sclerosis, Alzheimer’s Disease, and Inflammation: A Hypothetical View
Bynoe, M. S., & Viret, C. (2012) · Molecular and integrative toxicology · doi:10.1007/978-1-61779-812-2_9 · Cited by 1
Risk Factors for Alzheimer’s Disease
Cai, D., & Gaamouch, F. E. (2016) · InTech eBooks · doi:10.5772/64270 · Cited by 1
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Funke, D., Contreras, E. G., & Klämbt, C. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-95424-2.00010-8 · Cited by 2
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Kondo, N., Katsuno, M., Riku, Y., & Sobue, G. (2016) · Springer eBooks · doi:10.1007/978-4-431-55852-1_11 · Cited by 1
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Hashimoto, S., Nilsson, P., & Saido, T. C. (2015) · Springer eBooks · doi:10.1007/978-4-431-55763-0_19 · Cited by 2
Role of Impaired ABC Transporters in Alzheimer’s Disease
Haque, M., Rather, G. A., Siddiqui, E. M., Jahan, S., Khan, A., Makeen, H. A., Alexiou, A. T., & Ashraf, G. M. (2021) · Springer eBooks · doi:10.1007/978-981-16-4558-7_13 · Cited by 1
Ikezu, T. (2016) · Springer eBooks · doi:10.1007/978-3-319-44022-4_30 · Cited by 1
PET Imaging of ABC Transporters at the Blood–Brain Barrier
Langer, O. (2017) · Methods and principles in medicinal chemistry · doi:10.1002/9783527679430.ch8 · Cited by 1
Zhou, W., Wang, Z., Wang, W., Yang, J., Qi, W., Xu, H., & Xue, J. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6076076 · Cited by 1
Functional Imaging of P-glycoprotein in the Blood–Brain Barrier with PET: State of the Art
Hendrikse, N. H., Luurtsema, G., van Berckel, B. N. M., Franssen, E. J. F., & Lammertsma, A. A. (2007) · Springer eBooks · doi:10.1007/978-0-387-30380-2_5 · Cited by 1
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Davies, J. (2014) · Brunel University Research Archive (BURA) (Brunel University London)
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Akkaya, B. G. (2014)
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Lee, C., Varnäs, K., & Farde, L. (2013) · doi:10.1002/9781118356845.ch20
In vivo PET assay of functional P-gp in the blood-brain barrier
Luurtsema, G. (2006) · Digital Academic REpository of VU University Amsterdam (Vrije Universiteit Amsterdam)
Mechanisms of dopaminergic neurotoxin-induced blood-brain barrier disruption
Larsen, N. J. (2007) · D-Scholarship@Pitt (University of Pittsburgh)
Transporters in the Blood-Brain Barrier
Ueno, M., Nakagawa, T., & Sakamoto, H. (2011) · InTech eBooks · doi:10.5772/21162
Hembury, A. (2008) · OpenGrey (Institut de l'Information Scientifique et Technique)
Merlin, J. L. P. (2013) · Journal of the Chosun Natural Science · doi:10.13160/ricns.2013.6.3.125
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Metadata
- Authors
- Cirrito, J. R.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Cirrito, J. R.
- ORCID
- Cirrito, J. R.
- Venue
- Journal of Clinical Investigation
- Published
- 2005-11-01
- Volume
- 115
- Issue
- 11
- Pages
- 3285-3290
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC1257538
- OpenAlex
- W2163209521
- Cited by
- 660
- References
- 34
- Citations by year
- 2026: 21 · 2025: 24 · 2024: 29 · 2023: 36 · 2022: 31 · 2021: 30 · 2020: 37 · 2019: 31 · 2018: 30 · 2017: 35 · 2016: 43 · 2015: 40 · 2014: 41 · 2013: 44 · 2012: 26
- FWCI
- 12.44
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
- Funders
- U.S. Department of Energy
- National Institutes of Health (CA94056, AG13956)
- National Institute on Aging (AG023316, R03AG023316, R01AG023084, AG23084, R01AG013956, R37AG023084, R37AG013956)
- National Cancer Institute (P50 CA94056, P50CA094056)
- National Institute of Allergy and Infectious Diseases (AI-13956)
- National Institute of Neurological Disorders and Stroke (NS034467, R37NS034467, R01NS034467)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Keywords
- P-glycoprotein, blood-brain barrier, amyloid-beta, Alzheimer's disease, APP transgenic mice, P-glycoprotein inhibitors, brain interstitial fluid, amyloid-beta clearance, brain microvascular endothelial cells, amyloid-beta deposition
- MeSH terms
- Alzheimer Disease, Animals, Blood-Brain Barrier, Disease Models, Animal, Mice, Inbred C57BL, Mice, Transgenic, Polymorphism, Genetic, Up-Regulation, Amyloid beta-Peptides, Mice, Knockout, ATP Binding Cassette Transporter, Subfamily B, Member 1, Mice
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