The DOI matches its Crossref record; 33 of the 34 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“but it is now clear that ABCB1 is also involved in A peptide transport across the BBB.”
The cited source says what the claim attributes to it.
In the citing paper
“Whereas some studies have reported a role for ABCB1 in A peptide elimination from the brain [37,67]”
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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 201–300 of 662
Modarres, H. P., Janmaleki, M., Novin, M., Saliba, J., Moussa, F. E. H., Charan, M. R., Seyfoori, A., SadAbadi, H., Vandal, M., Nguyen, M. D., et al. (2018) · Journal of Controlled Release · doi:10.1016/j.jconrel.2018.01.024 · Cited by 77
Divecha, Y. A., Rampes, S., Tromp, S., Boyanova, S., Fleckney, A. L., Fidanboylu, M., & Thomas, S. A. (2025) · Pharmacological Reviews · doi:10.1016/j.pharmr.2025.100052 · Cited by 83
Behl, T., Kaur, I., Sehgal, A., Kumar, A., Uddin, M. S., & BUNGAU, S. G. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-02211-x · Cited by 78
Modulation of the Blood–Brain Barrier for Drug Delivery to Brain
Han, L. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13122024 · Cited by 78
Beta‐Amyloid Downregulates MDR1‐P‐Glycoprotein (Abcb1) Expression at the Blood‐Brain Barrier in Mice
Brenn, A., Grube, M., Peters, M., Fischer, A., Jedlitschky, G., Kroemer, H. K., Warzok, R., & Vogelgesang, S. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/690121 · Cited by 80
ElAli, A., Thériault, P., Préfontaine, P., & Rivest, S. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-75 · Cited by 72
Abdullahi, W., Davis, T., & Ronaldson, P. (2017) · AAPS Journal · doi:10.1208/s12248-017-0081-9 · Cited by 67
SARS-CoV-2: is there neuroinvasion?
McQuaid, C., Brady, M., & Deane, R. (2021) · Fluids and Barriers of the CNS · doi:10.1186/s12987-021-00267-y · Cited by 72
Westerhout, J., Danhof, M., & de Lange, E. C. M. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.22604 · Cited by 72
Devraj, K., Poznanovic, S., Spahn, C., Schwall, G., Harter, P. N., Mittelbronn, M., Antoniello, K., Paganetti, P., Muhs, A., Heilemann, M., et al. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x15606463 · Cited by 63
Dutheil, F., Jacob, A., Dauchy, S., Beaune, P. H., Scherrmann, J., Declèves, X., & Loriot, M. (2010) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425255.2010.510832 · Cited by 79
P‐glycoprotein (ABCB1) and Oxidative Stress: Focus on Alzheimer’s Disease
Sita, G., Hrelia, P., Tarozzi, A., & Morroni, F. (2017) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2017/7905486 · Cited by 73
Katt, M. E., Mayo, L. N., Ellis, S., Mahairaki, V., Rothstein, J. D., Cheng, L., & Searson, P. C. (2019) · Fluids and Barriers of the CNS · doi:10.1186/s12987-019-0139-4 · Cited by 69
Tryps and trips: cell trafficking across the 100-year-old blood–brain barrier
Bentivoglio, M., & Kristensson, K. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.03.007 · Cited by 78
Dysregulated Wnt Signalling in the Alzheimer’s Brain
Aghaizu, N. D., Jin, H., & Whiting, P. J. (2020) · Brain Sciences · doi:10.3390/brainsci10120902 · Cited by 70
Regulation of ABC Transporters at the Blood-Brain Barrier: New Targets for CNS Therapy
Hartz, A. M. S., & Bauer, B. (2010) · Molecular Interventions · doi:10.1124/mi.10.5.6 · Cited by 70
Abuznait, A. H., Cain, C. M., Ingram, D., Burk, D. H., & Kaddoumi, A. (2011) · Journal of Pharmacy and Pharmacology · doi:10.1111/j.2042-7158.2011.01309.x · Cited by 69
Targeting regulation of ABC efflux transporters in brain diseases: A novel therapeutic approach
Potschka, H. (2009) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2009.10.004 · Cited by 71
Paris‐Robidas, S., Émond, V., Tremblay, C., Soulet, D., & Calon, F. (2011) · Molecular Pharmacology · doi:10.1124/mol.111.071027 · Cited by 70
Addressing Blood–Brain Barrier Impairment in Alzheimer’s Disease
Sharma, C., Woo, H., & Kim, S. R. (2022) · Biomedicines · doi:10.3390/biomedicines10040742 · Cited by 72
Revisiting the role of brain and peripheral Aβ in the pathogenesis of Alzheimer's disease
Uddin, M. S., Kabir, M. T., Tewari, D., Mamun, A. A., Mathew, B., Aleya, L., Barreto, G. E., Bin-Jumah, M. N., Abdel‐Daim, M. M., & Ashraf, G. M. (2020) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2020.116974 · Cited by 70
Beta amyloid effects on expression of multidrug efflux transporters in brain endothelial cells.
Kania, K., Wijesuriya, H. C., Hladky, S., & Barrand, M. (2011) · Brain Research · doi:10.1016/j.brainres.2011.08.044 · Cited by 63
Pahnke, J., Walker, L. C., Scheffler, K., & Krohn, M. (2009) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2009.05.006 · Cited by 68
Eyal, S., Ke, B., Muzi, M., Link, J. M., Mankoff, D. A., Collier, A. C., & Unadkat, J. D. (2010) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2010.11 · Cited by 67
Su, L., Mruk, D. D., Lui, W., Lee, W. M., & Cheng, C. Y. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111414108 · Cited by 65
P-glycoprotein Trafficking as a Therapeutic Target to Optimize CNS Drug Delivery
Davis, T. P., Sanchez‐Covarrubias, L., & Tome, M. E. (2014) · Advances in pharmacology · doi:10.1016/bs.apha.2014.06.009 · Cited by 66
Ketone Bodies Promote Amyloid-β1–40 Clearance in a Human in Vitro Blood–Brain Barrier Model
Versele, R., Corsi, M., Fuso, A., Sevin, E., Businaro, R., Gosselet, F., Fénart, L., & Candela, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21030934 · Cited by 66
Yuede, C. M., Lee, H. J., Restivo, J. L., Davis, T. A., Hettinger, J. C., Wallace, C. E., Young, K. L., Hayne, M. R., Bu, G., Li, C.-Z., et al. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151428 · Cited by 65
Self-citationQosa, H., Mohamed, L. A., Rihani, S. B. A., Batarseh, Y. S., Duong, Q.-V., Keller, J. N., & Kaddoumi, A. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151179 · Cited by 64
Effect of escitalopram on Aβ levels and plaque load in an Alzheimer mouse model
Cirrito, J. R., Wallace, C. E., Yan, P., Davis, T. A., Gardiner, W. D., Doherty, B. M., King, D., Yuede, C. M., Lee, J., & Sheline, Y. I. (2020) · Neurology · doi:10.1212/wnl.0000000000010733 · Cited by 65
Self-citationLiow, J., Kreisl, W. C., Zoghbi, S. S., Lazarova, N., Seneca, N. M., Gladding, R. L., Taku, A. K., Herscovitch, P., Pike, V. W., & Innis, R. B. (2008) · Journal of Nuclear Medicine · doi:10.2967/jnumed.108.056226 · Cited by 63
Mohamed, L. A., Keller, J. N., & Kaddoumi, A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.01.013 · Cited by 65
Aging alters mRNA expression of amyloid transporter genes at the blood-brain barrier
Osgood, D., Miller, M. C., Messier, A. A., Gonzalez, L., & Silverberg, G. D. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.05.011 · Cited by 63
Contribution of Gut Microbiota to Immunological Changes in Alzheimer’s Disease
van Olst, L., Roks, S. J. M., Kamermans, A., Verhaar, B. J. H., van der Geest, A. M., Muller, M., van der Flier, W. M., & de Vries, H. E. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.683068 · Cited by 68
Poustforoosh, A., Nematollahi, M. H., Hashemipour, H., & Pardakhty, A. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.02.015 · Cited by 62
Chaves, J. C. S., Dando, S. J., White, A. R., & Oikari, L. E. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166967 · Cited by 62
The role of the efflux transporter, P‐glycoprotein, at the blood–brain barrier in drug discovery
Cox, B., Nicolaï, J., & Williamson, B. (2022) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.2331 · Cited by 73
Effects of oxysterols on the blood–brain barrier: Implications for Alzheimer’s disease
Gosselet, F., Saint-Pol, J., & Fenart, L. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.11.059 · Cited by 53
An investigation into the role of P-glycoprotein in Alzheimer's disease lesion pathogenesis
Jeynes, B., & Provias, J. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.10.063 · Cited by 61
Acıoğlu, Ç., & Elkabes, S. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03360-3 · Cited by 67
Qosa, H., LeVine, H., Keller, J. N., & Kaddoumi, A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.06.029 · Cited by 64
Increased amyloid β-peptide (1–40) level in brain of streptozotocin-induced diabetic rats
Liu, Y., Liu, H., Yang, J., Liu, X., Lü, S., Wen, T., Xie, L. Y., & Wang, G. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.03.019 · Cited by 59
Kabir, M. T., Uddin, M. S., Jeandet, P., Emran, T. B., Mitra, S., Albadrani, G. M., Sayed, A. A., Abdel‐Daim, M. M., & Simal‐Gándara, J. (2021) · Marine Drugs · doi:10.3390/md19050251 · Cited by 65
Walker, J. R., Pacoma, R., Watson, J., Ou, W., Alves, J., Mason, D. E., Peters, E. C., Urbina, H. D., Welzel, G., Althage, A., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3407-12.2013 · Cited by 59
Sink Hypothesis and Therapeutic Strategies for Attenuating Aβ Levels
Zhang, Y., & Lee, D. H. S. (2011) · The Neuroscientist · doi:10.1177/1073858410381532 · Cited by 61
The Role of the Blood-Brain Barrier in the Pathogenesis of Senile Plaques in Alzheimer’s Disease
Provias, J., & Jeynes, B. (2014) · International Journal of Alzheimer s Disease · doi:10.1155/2014/191863 · Cited by 60
Mohamed, L. A., Qosa, H., & Kaddoumi, A. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00040 · Cited by 58
Novelli, M., Masiello, P., Beffy, P., & Menegazzi, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218108 · Cited by 63
Expression and Processing of Amyloid Precursor Protein in Vascular Endothelium
d’Uscio, L. V., He, T., & Katušić, Z. S. (2016) · Physiology · doi:10.1152/physiol.00021.2016 · Cited by 57
Storelli, F., Billington, S. F., Kumar, A. R., & Unadkat, J. D. (2020) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.2035 · Cited by 60
Kuntz, M., Candela, P., Saint-Pol, J., Lamartinière, Y., Boucau, M.-C., Sevin, E., Fenart, L., & Gosselet, F. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-150469 · Cited by 55
Lennerz, J. K., Hurov, J., White, L. S., Lewandowski, K. T., Prior, J. L., Planer, G. J., Gereau, R. W., Piwnica-Worms, D., Schmidt, R. E., & Piwnica-Worms, H. M. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01472-09 · Cited by 59
Use of PET Imaging to Evaluate Transporter‐Mediated Drug‐Drug Interactions
Langer, O. (2016) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.722 · Cited by 57
Chen, K.-D., Chang, P.-T., Ping, Y., Lee, H., Yeh, C., & Wang, P. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.05.023 · Cited by 54
Preventing P-gp Ubiquitination Lowers Aβ Brain Levels in an Alzheimer’s Disease Mouse Model
Hartz, A. M. S., Zhong, Y., Shen, A. N., Abner, E. L., & Bauer, B. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00186 · Cited by 54
Drug Permeability: From the Blood–Brain Barrier to the Peripheral Nerve Barriers
Sun, Y., Zabihi, M., Li, Q., Li, X., Kim, B. J., Ubogu, E. E., Raja, S. N., Wesselmann, U., & Zhao, C. (2023) · Advanced Therapeutics · doi:10.1002/adtp.202200150 · Cited by 59
Association between the ABCG2 C421A polymorphism and Alzheimer's disease
Fehér, Á., Juhász, A., László, A., Pákáski, M., Kálmán, J., & Janka, Z. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.06.044 · Cited by 52
A-Subclass ATP-Binding Cassette Proteins in Brain Lipid Homeostasis and Neurodegeneration
Piehler, A. P., Özcürümez, M. K., & Kaminski, W. E. (2012) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2012.00017 · Cited by 61
Pan, W., & Kastin, A. J. (2016) · The Neuroscientist · doi:10.1177/1073858416639005 · Cited by 58
Wiese, M., & Stefan, S. M. (2019) · Medicinal Research Reviews · doi:10.1002/med.21573 · Cited by 53
Disease-Induced Modulation of Drug Transporters at the Blood–Brain Barrier Level
Rihani, S. B. A., Darakjian, L. I., Deodhar, M., Dow, P., Turgeon, J., & Michaud, V. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073742 · Cited by 55
Methodologies to Assess Drug Permeation Through the Blood–Brain Barrier for Pharmaceutical Research
Passeleu, C. L. B., Carrupt, P., Scherrmann, J. M. G., & Martel, S. (2013) · Pharmaceutical Research · doi:10.1007/s11095-013-1119-z · Cited by 55
Llorach-Parés, L., Nonell‐Canals, A., Sánchez-Martínez, M., & Àvila, C. (2017) · Marine Drugs · doi:10.3390/md15120366 · Cited by 52
The case for blood–brain barrier dysfunction in the pathogenesis of Alzheimer's disease
Jeynes, B., & Provias, J. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22527 · Cited by 51
RIFAMPICIN: An antibiotic with brain protective function
Yuluğ, B., Hanoğlu, L., Kılıç, E., & Schabitz, W. R. (2014) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2014.05.007 · Cited by 51
Kannan, P., Brimacombe, K. R., Zoghbi, S. S., Liow, J., Morse, C. L., Taku, A. K., Pike, V. W., Halldin, C., Innis, R. B., Gottesman, M. M., et al. (2010) · Drug Metabolism and Disposition · doi:10.1124/dmd.109.031161 · Cited by 51
Carrano, A., Snkhchyan, H., Kooij, G., van der Pol, S., van Horssen, J., Veerhuis, R., Hoozemans, J., Rozemuller, A., & de Vries, H. E. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.09.015 · Cited by 51
The impact of ATP-binding cassette transporters in the diseased brain: Context matters
Baltira, C., Aronica, E., Elmquist, W. F., Langer, O., Löscher, W., Sarkaria, J. N., Wesseling, P., de Gooijer, M. C., & van Tellingen, O. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101609 · Cited by 54
Gadolinium-staining reveals amyloid plaques in the brain of Alzheimer's transgenic mice
Petiet, A., Santin, M. D., Bertrand, A., Wiggins, C. J., Petit, F., Houitte, D., Hantraye, P., Bénavidès, J., Debeir, T., Rooney, T., et al. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.03.009 · Cited by 54
Bernstein, H., Hölzl, G., Dobrowolny, H., Hildebrandt, J., Trübner, K., Krohn, M., Bogerts, B., & Pahnke, J. (2014) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2014.08.003 · Cited by 50
Radioligands targeting P‐glycoprotein and other drug efflux proteins at the blood–brain barrier
Wanek, T., Mairinger, S., & Langer, O. (2013) · Journal of Labelled Compounds and Radiopharmaceuticals · doi:10.1002/jlcr.2993 · Cited by 50
Aleidi, S. M., Howe, V., Sharpe, L. J., Yang, A., Rao, G., Brown, A. J., & Gelissen, I. C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.675579 · Cited by 49
Lamartinière, Y., Boucau, M.-C., Dehouck, L., Krohn, M., Pahnke, J., Candela, P., Gosselet, F., & Fenart, L. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170883 · Cited by 50
Ogata, S., Ito, S., Masuda, T., & Ohtsuki, S. (2019) · Pharmaceutical Research · doi:10.1007/s11095-019-2674-8 · Cited by 50
Wojtunik‐Kulesza, K. A., Rudkowska, M., Kasprzak‐Drozd, K., Oniszczuk, A., & Borowicz, K. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147366 · Cited by 51
Anastasio, T. J. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00016 · Cited by 49
P-glycoprotein transporter in drug development
Prachayasittikul, V., & Prachayasittikul, V. (2016) · EXCLI journal · doi:10.17179/excli2015-768 · Cited by 49
Miller, B., Whisner, C. M., & Johnston, C. S. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150901 · Cited by 48
Accumulation of murine amyloid-β mimics early Alzheimer’s disease
Krohn, M., Bracke, A., Avchalumov, Y., Schumacher, T., Hofrichter, J., Paarmann, K., Fröhlich, C., Lange, C., Brüning, T., von Bohlen und Halbach, O., et al. (2015) · Brain · doi:10.1093/brain/awv137 · Cited by 47
Badaut, J., & Bix, G. J. (2013) · Translational Stroke Research · doi:10.1007/s12975-013-0304-z · Cited by 48
Pan, Y., Short, J. L., Newman, S. A., Choy, K. H. C., Tiwari, D., Yap, C., Senyschyn, D., Banks, W. A., & Nicolazzo, J. A. (2018) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2018.03.007 · Cited by 50
Matsumoto, K., Chiba, Y., Fujihara, R., Kubo, H., Sakamoto, H., & Ueno, M. (2015) · Histochemistry and Cell Biology · doi:10.1007/s00418-015-1366-7 · Cited by 46
Glycoproteomics Landscape of Asymptomatic and Symptomatic Human Alzheimer’s Disease Brain
Suttapitugsakul, S., Stavenhagen, K., Donskaya, S., Bennett, D. A., Mealer, R. G., Seyfried, N. T., & Cummings, R. D. (2022) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2022.100433 · Cited by 48
Evaluation of hypoxia inducible factor expression in inflammatory and neurodegenerative brain models
de Lemos, M. L., de la Torre, A. V., Petrov, D., Brox, S., Folch, J., Pallàs, M., Lazarowski, A., Beas‐Zárate, C., Auladell, C., & Camins, A. (2013) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2013.04.011 · Cited by 47
Targeting ApoE4/ApoE receptor LRP1 in Alzheimer's disease
Martiskainen, H., Haapasalo, A., Kurkinen, K. M. A., Pihlajamäki, J., Soininen, H. S., & Hiltunen, M. O. (2013) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2013.789862 · Cited by 49
Patel, P., & Shah, J. (2017) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2017.06.007 · Cited by 46
Jia, Y., Wang, N., Zhang, Y., Xue, D., Lou, H., & Liu, X. (2020) · Aging and Disease · doi:10.14336/ad.2019.0519 · Cited by 50
Drug Access to the Central Nervous System in Alzheimer’s Disease: Preclinical and Clinical Insights
Mehta, D. C., Short, J. L., Hilmer, S. N., & Nicolazzo, J. A. (2014) · Pharmaceutical Research · doi:10.1007/s11095-014-1522-0 · Cited by 47
Mechanisms of the Penetration of Blood-Borne Substances into the Brain
Ueno, M. (2009) · Current Neuropharmacology · doi:10.2174/157015909788848901 · Cited by 44
Pahnke, J., Wolkenhauer, O., Krohn, M., & Walker, L. C. (2008) · Current Alzheimer Research · doi:10.2174/156720508785132262 · Cited by 45
Sullivan, S. E., Dillon, G. M., Sullivan, J. M., & Ho, A. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.541003 · Cited by 44
Cataldi, M. (2013) · Current Neuropharmacology · doi:10.2174/1570159x11311030004 · Cited by 45
Ballatore, C., Brunden, K. R., Trojanowski, J. Q., Lee, V. M. Y., Smith, A. B., & Huryn, D. M. (2010) · Current Topics in Medicinal Chemistry · doi:10.2174/156802611794072605 · Cited by 46
Liu, L., Collier, A. C., Link, J. M., Domino, K. B., Mankoff, D. A., Eary, J. F., Spiekerman, C. F., Hsiao, P., Deo, A. K., & Unadkat, J. D. (2015) · Drug Metabolism and Disposition · doi:10.1124/dmd.114.058685 · Cited by 45
Microphysiological systems for recapitulating physiology and function of blood-brain barrier
Seo, S., Kim, H., Sung, J. H., Choi, N., Lee, K., & Kim, H. N. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119732 · Cited by 46
Transport of Alzheimer’s associated amyloid-β catalyzed by P-glycoprotein
McCormick, J. W., McCormick, L. A., (党陈), G. C., Vogel, P. D., & Wise, J. G. (2021) · PLoS ONE · doi:10.1371/journal.pone.0250371 · Cited by 43
Jana, A., Wang, X., Leasure, J. W., Magana, L., Wang, L., Kim, Y.-M., Dodiya, H., Toth, P. T., Sisodia, S. S., & Rehman, J. (2022) · Scientific Reports · doi:10.1038/s41598-022-20889-y · Cited by 43
Cerebrovascular P-glycoprotein expression is decreased in Creutzfeldt–Jakob disease
Vogelgesang, S., Glatzel, M., Walker, L. C., Kroemer, H. K., Aguzzi, A., & Warzok, R. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0042-3 · Cited by 43
Savolainen, H., Windhorst, A. D., Elsinga, P. H., Cantore, M., Colabufo, N. A., Willemsen, A. T. M., & Luurtsema, G. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16654493 · Cited by 43
Linking activity dyshomeostasis and sleep disturbances in Alzheimer disease
Slutsky, I. (2024) · Nature reviews. Neuroscience · doi:10.1038/s41583-024-00797-y · Cited by 43
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
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