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 401–500 of 662
Drugs and drug delivery systems targeting amyloid-β in Alzheimer's disease
Robinson, M. J., Lee, B. Y., & Leonenko, Z. (2015) · AIMS molecular science · doi:10.3934/molsci.2015.3.332 · Cited by 24
Piwnica-Worms, D. R., Kesarwala, A. H., Pichler, A., Prior, J. L., & Sharma, V. (2006) · Neuroimaging Clinics of North America · doi:10.1016/j.nic.2006.06.007 · Cited by 21
McInerney, M. P., Short, J. L., & Nicolazzo, J. A. (2017) · The AAPS Journal · doi:10.1208/s12248-017-0077-5 · Cited by 20
Rhythms in barriers and fluids: Circadian clock regulation in the aging neurovascular unit
Skapetze, L., Owino, S., Lo, E. H., Arai, K., Merrow, M. W., & Harrington, M. E. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106120 · Cited by 20
Xing, C., Zhang, X., Wang, D., Chen, H., Gao, X., Sun, C., Guo, W., Roshan, S., Li, Y., Hang, Z., et al. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.08.047 · Cited by 20
Minh, T. N., Bedussi, B., Chasseigneaux, S., Dodacki, A., Yapo, C., Chacun, H., Scherrmann, J., Farinotti, R., & Bourasset, F. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-121891 · Cited by 22
Glutathione depletion upregulates P-glycoprotein expression at the blood-brain barrier in rats
Wu, J., Hong, H., Ji, H., Wang, Y. Y., Wang, Y., Li, Y. Q., Li, W. G., Long, Y., & Xia, Y. Z. (2009) · Journal of Pharmacy and Pharmacology · doi:10.1211/jpp.61.06.0016 · Cited by 20
ABCB1 C3435T Polymorphism Influences the Risk for Alzheimer’s Disease
Fehér, Á., Juhász, A., Pákáski, M., Kálmán, J., & Janka, Z. (2014) · Journal of Molecular Neuroscience · doi:10.1007/s12031-014-0427-z · Cited by 20
Ma, C., Gan, L., Wang, H., Ren, L., Lin, Y., Zhao, Y., Zhang, S., Gong, P., & Lin, X. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.834683 · Cited by 17
Implication of ABC transporters in non-proliferative diseases
Grigoreva, T. A., Sagaidak, A. V., Novikova, D., & Tribulovich, V. G. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.175327 · Cited by 18
Römermann, K., Bankstahl, J. P., Löscher, W., & Bankstahl, M. (2015) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.114.221952 · Cited by 20
Tachikawa, M., Uchida, Y., Ohtsuki, S., & Terasaki, T. (2013) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-1-4614-9105-7_2 · Cited by 19
Paik, S., Somvanshi, R. K., & Kumar, U. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1045-5 · Cited by 20
Synthesis and P-glycoprotein induction activity of colupulone analogs
Bharate, J. B., Batarseh, Y. S., Wani, A., Sharma, S., Vishwakarma, R. A., Kaddoumi, A., Kumar, A., & Bharate, S. B. (2015) · Organic & Biomolecular Chemistry · doi:10.1039/c5ob00554j · Cited by 20
Ohtsuki, S., Ito, S., & Terasaki, T. (2010) · Clinical Pharmacology & Therapeutics · doi:10.1038/clpt.2010.160 · Cited by 19
Alzheimer therapeutics—what after the cholinesterase inhibitors?
Walker, L. C., & Rosen, R. F. (2006) · Age and Ageing · doi:10.1093/ageing/afl009 · Cited by 19
Paclitaxel C-10 carbamates: Potential candidates for the treatment of neurodegenerative tauopathies
Ballatore, C., Hyde, E. G., Deiches, R. F., Lee, V. M. ‐., Trojanowski, J. Q., Huryn, D. M., & Smith, A. B. (2007) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2007.04.058 · Cited by 19
Ni, R. (2021) · Pharmaceuticals · doi:10.3390/ph14111179 · Cited by 18
Li, K., Ran, B., Wang, Y., Liu, L., & Li, W. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.999061 · Cited by 18
Quantification of P-glycoprotein function at the human blood-brain barrier using [18F]MC225 and PET
Mossel, P., Arif, W. M., de Souza, G. S., García-Varela, L., van der Weijden, C. W. J., Boersma, H. H., Willemsen, A. T. M., Boellaard, R., Elsinga, P. H., Borra, R., et al. (2023) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-023-06363-5 · Cited by 21
Park, J., Kim, H., Alabdalla, L., Mishra, S., & Mchaourab, H. S. (2023) · Human Genomics · doi:10.1186/s40246-023-00530-3 · Cited by 18
Drug Transporters At Brain Barriers
Ashraf, T., Kis, O., Banerjee, N., & Bendayan, R. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-1-4614-4711-5_2 · Cited by 18
Pérez‐Grijalba, V., Pesini, P., Allué, J. A., Sarasa, L., Montañés, M., Lacosta, A.-M., Casabona, D., José, I. S., Boada, M., Tárraga, L., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140156 · Cited by 20
Mouse models of neurological disorders: A view from the blood–brain barrier
Banks, W. A. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.10.011 · Cited by 22
Vendelbo, J. H., Olesen, R. H., Lauridsen, J. K., Rungby, J., Kleinman, J. E., Hyde, T. M., & Larsen, A. (2016) · The Pharmacogenomics Journal · doi:10.1038/tpj.2016.74 · Cited by 18
McInerney, M. P., Volitakis, I., Bush, A. I., Banks, W. A., Short, J. L., & Nicolazzo, J. A. (2018) · Pharmaceutical Research · doi:10.1007/s11095-018-2377-6 · Cited by 18
Effect of mouse strain as a background for Alzheimer’s disease models on the clearance of amyloid-β
Qosa, H., & Kaddoumi, A. (2016) · Journal of Systems and Integrative Neuroscience · doi:10.15761/jsin.1000123 · Cited by 20
Mapping the Brain’s Glymphatic System
Voumvourakis, K. I., Thomaidis, N. S., & Tsiodras, S. (2026) · Biomedicines · doi:10.3390/biomedicines14020409 · Cited by 17
Camenzind, R. S., Chip, S., Gutmann, H., Kapfhammer, J. P., Nitsch, C., & Bendfeldt, K. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.06.073 · Cited by 17
Transport of Drugs Across the blood–brain Barrier in Alzheimer‘s Disease
Nicolazzo, J. A., & Mehta, D. C. (2010) · Therapeutic Delivery · doi:10.4155/tde.10.41 · Cited by 19
Mechanism of anti-AD action of OAB-14 by enhancing the function of glymphatic system
Zhang, X., Cao, R., Zhu, C., Yang, L., Zheng, N., Ji, W., Liu, P., Chi, T., Ji, X., Zheng, Z., et al. (2023) · Neurochemistry International · doi:10.1016/j.neuint.2023.105633 · Cited by 15
Pyun, J., Koay, H., Runwal, P., Mawal, C., Bush, A. I., Pan, Y., Donnelly, P. S., Short, J. L., & Nicolazzo, J. A. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15082084 · Cited by 16
ABCB1 transporter and Toll-like receptor 4 in trabecular meshwork cells.
Grybauskas, A., Koga, T., Kuprys, P. V., Nolan, M. J., McCarty, R. D., Walker, L., Green, K. A., Norkett, W. M., Yue, B. Y. J. T., & Knepper, P. A. (2015) · Europe PMC (PubMed Central) · Cited by 16
Bello, I., & Salerno, M. (2015) · Cell Stress and Chaperones · doi:10.1007/s12192-014-0566-8 · Cited by 18
P-Glycoprotein Altered Expression in Alzheimer's Disease: Regional Anatomic Variability
Jeynes, B., & Provias, J. (2013) · Journal of Neurodegenerative Diseases · doi:10.1155/2013/257953 · Cited by 17
Ueno, M., Wu, B., Nakagawa, T., Nagai, Y., Onodera, M., Huang, C., Kusaka, T., Kanenishi, K., & Sakamoto, H. (2010) · Histochemistry and Cell Biology · doi:10.1007/s00418-010-0705-y · Cited by 17
Ueno, M. (2017) · Rinsho Shinkeigaku · doi:10.5692/clinicalneurol.cn-001004 · Cited by 15
Couyoupetrou, M., Gantner, M. E., Ianni, M. E. D., Palestro, P. H., Enrique, A., Gavernet, L., Ruiz, M. E., Pesce, G. O., Bruno‐Blanch, L. E., & Talevi, A. (2016) · Mini-Reviews in Medicinal Chemistry · doi:10.2174/1389557516666161013103408 · Cited by 16
Syndapin-2 mediated transcytosis of amyloid-β across the blood–brain barrier
Leite, D. M., Seifi, M., Ruiz‐Pérez, L., Nguemo, F., Plomann, M., Swinny, J. D., & Battaglia, G. (2022) · Brain Communications · doi:10.1093/braincomms/fcac039 · Cited by 16
Theoretical and applied concepts of nanocarriers for the treatment of Parkinson's diseases
Bhosale, A., Paul, G., Mazahir, F., & Yadav, A. K. (2022) · OpenNano · doi:10.1016/j.onano.2022.100111 · Cited by 15
Extracellular matrix proteins in construction and function of in vitro blood-brain barrier models
Du, F., Shusta, E. V., & Palecek, S. P. (2023) · Frontiers in Chemical Engineering · doi:10.3389/fceng.2023.1130127 · Cited by 17
Imaging transporters: Transforming diagnostic and therapeutic development
Mann, A., Han, H., & Eyal, S. (2016) · Clinical Pharmacology & Therapeutics · doi:10.1002/cpt.416 · Cited by 15
Regulation of P-glycoprotein by miR-27a-3p at the Brain Endothelial Barrier
Hammad, S., Mabondzo, A. M., Hamoudi, R., & Harati, R. (2021) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2021.10.021 · Cited by 15
Nanotherapeutic Strategies for the Treatment of Alzheimer's Disease
Gu, X. Q., Chen, H., & Gao, X. (2015) · Therapeutic Delivery · doi:10.4155/tde.14.97 · Cited by 15
ABCB1 Genotype and CSF β-Amyloid in Alzheimer Disease
Kohen, R., Shofer, J. B., Korvatska, O., Petrie, E. C., Wang, L. Y., Schellenberg, G. D., Peskind, E. R., & Wilkinson, C. W. (2011) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988711402325 · Cited by 16
Frankfort, S. V., Doodeman, V. D., Bakker, R., Tulner, L. R., van Campen, J. P., Smits, P. H. M., & Beijnen, J. H. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-13 · Cited by 15
Shubbar, M. H., & Penny, J. I. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173009 · Cited by 14
Yang, Q., Xing, Z., Du, L., Fang, X., Liang, H., Zhang, S., Shi, L., Kuang, C., & Han, T.-X. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.358607 · Cited by 15
New findings concerning vertebrate porin II — On the relevance of glycine motifs of type-1 VDAC
THINNES, F. P. (2013) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2013.01.008 · Cited by 14
Rihani, S. B. A., Lan, R. S.-L., & Kaddoumi, A. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190849 · Cited by 14
Role of A β Transport and Clearance in the Pathogenesis and Treatment of Alzheimer’s Disease
Holtzman, D. M., & Zloković, B. V. (2007) · Springer eBooks · doi:10.1007/978-0-387-35135-3_11 · Cited by 15
A Chronological Review of Potential Disease-Modifying Therapeutic Strategies for Alzheimer’s Disease
Ettcheto, M., Busquets, O., Espinosa-Jiménez, T., Verdaguer, E., Auladell, C., & Camins, A. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200211121416 · Cited by 13
Wang, H., Qiao, Y., Lu, H., Bo, X., Chen, F., Pu, N., Zhou, Y., & Cheng, Q. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.107224 · Cited by 13
mohamed, I. E., Osman, E. E., Saeed, A. M., Ming, L. C., Goh, K. W., Razi, P., Abdullah, A. D. I., & Dahab, M. M. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e35943 · Cited by 16
Paganetti, P., Antoniello, K., Devraj, K., Toni, N., Kieran, D., Madani, R., Pihlgren, M., Adolfsson, O., Froestl, W., Schrattenholz, A. S., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-131091 · Cited by 13
Self-citationSchoenfelder, Y., Hiemke, C., & Schmitt, U. (2012) · Journal of Neuroendocrinology · doi:10.1111/j.1365-2826.2012.02278.x · Cited by 14
Contino, M., Cantore, M., Capparelli, E., Perrone, M. G., Niso, M., Inglese, C., Berardi, F., Leopoldo, M., Perrone, R., & Colabufo, N. A. (2011) · ChemMedChem · doi:10.1002/cmdc.201100469 · Cited by 13
Ashraf, T., Ronaldson, P. T., & Bendayan, R. (2014) · doi:10.1002/9781118705308.ch14 · Cited by 13
Shao, X., Shou, Q., Felix, K., Ojogho, B., Jiang, X., Gold, B. T., Herting, M. M., Goldwaser, E. L., Kochunov, P. V., Hong, E. L., et al. (2024) · eLife · doi:10.7554/elife.96155 · Cited by 13
Erickson, M. A., Johnson, R. S., Damodarasamy, M., MacCoss, M. J., Keene, C. D., Banks, W. A., & Reed, M. J. (2024) · Fluids and Barriers of the CNS · doi:10.1186/s12987-024-00581-1 · Cited by 12
Rhodehouse, B. C., Erickson, M. A., Banks, W. A., & Bearden, S. E. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-122347 · Cited by 12
Heikkinen, R., Malm, T., Heikkilä, J., Muona, A., Tanila, H., Koistinaho, M., & Koıstınaho, J. (2014) · Aging and Disease · doi:10.14336/ad.2014.050076 · Cited by 12
Newman, S. A., Pan, Y., Short, J. L., & Nicolazzo, J. A. (2021) · Pharmaceutical Research · doi:10.1007/s11095-021-03006-y · Cited by 13
Mamma Mia, P‐glycoprotein binds again
Callaghan, R., Gelissen, I. C., George, A. M., & Hartz, A. M. S. (2020) · FEBS Letters · doi:10.1002/1873-3468.13951 · Cited by 12
The Function and Expression of ATP-Binding Cassette Transporters Proteins in the Alzheimer's Disease
Aykaç, A., & Sehirli, A. Ö. (2021) · Global Medical Genetics · doi:10.1055/s-0041-1735541 · Cited by 12
Yadav, S., & Tapadia, M. G. (2013) · Genetics · doi:10.1534/genetics.113.155077 · Cited by 12
In Vivo Imaging of Human MDR1 Transcription in the Brain and Spine of MDR1-Luciferase Reporter Mice
Yasuda, K., Cline, C., Lin, Y. S., Scheib, R., Ganguly, S., Thirumaran, R. K., Chaudhry, A. S., Kim, R. B., & Schuetz, E. G. (2015) · Drug Metabolism and Disposition · doi:10.1124/dmd.115.065078 · Cited by 12
Nicolazzo, J. A., & Banks, W. A. (2011) · Therapeutic Delivery · doi:10.4155/tde.11.65 · Cited by 11
Why cancer survivors have a lower risk of Alzheimer disease
THINNES, F. P. (2012) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2012.06.016 · Cited by 11
Common and Rare Genetic Variants Associated With Alzheimer's Disease
Marei, H. E. S., Thani, A. A. A., Suhonen, J., Zowalaty, M. E. E., Al-Banna, M. A., Cenciarelli, C., Wang, T., & Caceci, T. (2015) · Journal of Cellular Physiology · doi:10.1002/jcp.25225 · Cited by 11
Shinde, P., Vidyasagar, N., Dhulap, S., Dhulap, A., & Hirwani, R. R. (2015) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/1871524915666150826092152 · Cited by 11
Role of ABC transporters in the pathology of Alzheimer’s disease
Zhao, Y., Hou, D., Feng, X., Lin, F., & Luo, J. (2016) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0060 · Cited by 11
Multidrug Resistance P-Glycoprotein (P-gp), Glucocorticoids, and the Stress Response
Bloise, E., & Matthews, S. G. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813146-6.00019-9 · Cited by 11
In situ blood–brain barrier permeability of a C-10 paclitaxel carbamate
Ballatore, C., Zhang, B., Trojanowski, J. Q., Lee, V. M. ‐., & Smith, A. B. (2008) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2008.10.024 · Cited by 11
Frankfort, S. V., van Campen, J., Tulner, L. R., & Beijnen, J. H. (2008) · Current Clinical Pharmacology · doi:10.2174/157488408785747665 · Cited by 11
Newman, S. A., Pan, Y., Short, J. L., & Nicolazzo, J. A. (2017) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2017.01.013 · Cited by 11
Tuma, R. F. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374530-9.00013-9 · Cited by 11
Bartels, A. L., Kortekaas, R., & Leenders, K. L. (2008) · NeuroImage · doi:10.1016/j.neuroimage.2008.04.140 · Cited by 11
The endocrine pancreas of old obesehyperglycemic mice.
Westman, S. (1968) · PubMed · Cited by 11
P-glycoprotein and Alzheimer’s Disease: Threats and Opportunities
Asante, J., & Barger, S. W. (2025) · ASN NEURO · doi:10.1080/17590914.2025.2495632 · Cited by 11
Takeuchi, L. E., Kalia, L. V., & Simmons, C. A. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2025.106864 · Cited by 11
Brain Distribution of Dual ABCB1/ABCG2 Substrates Is Unaltered in a Beta-Amyloidosis Mouse Model
Wanek, T., Zoufal, V., Brackhan, M., Krohn, M., Mairinger, S., Filip, T., Sauberer, M., Stanek, J., Pekar, T., Pahnke, J., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218245 · Cited by 9
Tuma, R. F. (2008) · Comprehensive physiology · doi:10.1002/cphy.cp020411 · Cited by 9
Fiscalin Derivatives as Potential Neuroprotective Agents
Barreiro, S., Silva, B., Long, S., Pinto, M. M. M., Remião, F., Sousa, E., & Silva, R. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14071456 · Cited by 9
Chaves, J. C. S., Wasielewska, J. M., Cuní‐López, C., Rantanen, L. M., Lee, S., Koıstınaho, J., White, A. R., & Oikari, L. E. (2023) · Neurotherapeutics · doi:10.1016/j.neurot.2023.10.009 · Cited by 10
Bonada, M., Pittarello, M., Fazio, E. D., Gans, A., Alimonti, P., Slika, H., Legnani, F. G., Meco, F. D., & Tyler, B. (2024) · Genes · doi:10.3390/genes15081038 · Cited by 10
Tai, L. M., Jacobsen, H., Ozmen, L., Flohr, A., Jakob‐Roetne, R., Caruso, A., & Grimm, H. P. (2012) · Journal of Pharmacokinetics and Pharmacodynamics · doi:10.1007/s10928-012-9246-4 · Cited by 9
11C‐ and 18F‐Labeled Radioligands for P‐Glycoprotein Imaging by Positron Emission Tomography
Cantore, M., Benadiba, M., Elsinga, P. H., Kwizera, C., Dierckx, R., Colabufo, N. A., & Luurtsema, G. (2015) · ChemMedChem · doi:10.1002/cmdc.201500420 · Cited by 9
Glucocorticoids modify effects of TGF-β1 on multidrug resistance in the fetal blood-brain barrier
Baello, S., Iqbal, M., Kearney, S., Kuthiala, S., Bloise, E., Gibb, W., & Matthews, S. G. (2016) · Growth Factors · doi:10.3109/08977194.2016.1162163 · Cited by 9
Liang, R., Ou, S., Han, Y., Xu, J., & Zhou, S. (2019) · Experimental Gerontology · doi:10.1016/j.exger.2019.110737 · Cited by 9
Sivapackiam, J., Gammon, S. T., Harpstrite, S. E., & Sharma, V. (2009) · Methods in molecular biology · doi:10.1007/978-1-60761-416-6_8 · Cited by 9
Elfakhri, K. H., Duong, Q.-V., Langley, C., Depaula, A., Mousa, Y. M., Lebeouf, T., Cain, C. M., & Kaddoumi, A. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.03.028 · Cited by 9
Manrique‐Castano, D., Sardari, M., de Carvalho, T. S., Doeppner, T. R., Popa‐Wagner, A., Kleinschnitz, C., Chan, A., & Hermann, D. M. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00412 · Cited by 9
Haferkamp, U., Hartmann, C., Abid, C. L., Brachner, A., Höchner, A., Gerhartl, A., Harwardt, B., Leckzik, S., Leu, J., Metzger, M., et al. (2023) · Fluids and Barriers of the CNS · doi:10.1186/s12987-023-00471-y · Cited by 12
Biali, M. E., Breuil, L., Jackwerth, M., Mairinger, S., Weber, M., Wölfl‐Duchek, M., Bamminger, K., Rausch, I., Nics, L., Hacker, M., et al. (2024) · Fluids and Barriers of the CNS · doi:10.1186/s12987-024-00588-8 · Cited by 8
Peng, H., Bukuroshi, P., Durk, M. R., Grootendorst, P. V., Yan, X., Pan, S. R., de Lannoy, I. A. M., & Pang, K. S. (2021) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.2297 · Cited by 8
Endres, K., Reinhardt, S., Geladaris, A., Knies, J., Grimm, M. O. W., Hartmann, T., & Schmitt, U. (2016) · BMC Neuroscience · doi:10.1186/s12868-016-0280-9 · Cited by 9
Yap, C., Short, J. L., & Nicolazzo, J. A. (2020) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2020.04.010 · Cited by 8
Therapeutic Approaches for the Treatment of Alzheimer's Disease: An Overview
Lau, L., & Brodney, M. A. (2007) · Springer eBooks · doi:10.1007/7355_2007_017 · Cited by 8
Management of Epilepsy - Research, Results and Treatment
Günel, M. K. (2011) · InTech eBooks · doi:10.5772/1139 · Cited by 8
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