The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.
Severe alterations of endothelial and glial cells in the blood‐brain barrier of dystrophic mdx mice
Open accessAbstract
In this study, we investigated the involvement of the blood‐brain barrier (BBB) in the brain of the dystrophin‐deficient mdx mouse, an experimental model of Duchenne muscular dystrophy (DMD). To this purpose, we used two tight junction markers, the Zonula occludens (ZO‐1) and claudin‐1 proteins, and a glial marker, the aquaporin‐4 (AQP4) protein, whose expression is correlated with BBB differentiation and integrity. Results showed that most of the brain microvessels in mdx mice were lined by altered endothelial cells that showed open tight junctions and were surrounded by swollen glial processes. Moreover, 18% of the perivascular glial endfeet contained electron‐dense cellular debris and were enveloped by degenerating microvessels. Western blot showed a 60% reduction in the ZO‐1 protein content in mdx mice and a similar reduction in AQP4 content compared with the control brain. ZO‐1 immunocytochemistry and claudin‐1 immunofluorescence in mdx mice revealed a diffuse staining of microvessels as compared with the control ones, which displayed a banded staining pattern. ZO‐1 immunogold electron microscopy showed unlabeled tight junctions and the presence of gold particles scattered in the endothelial cytoplasm in the mdx mice, whereas ZO‐1 gold particles were exclusively located at the endothelial tight junctions in the controls. Dual immunofluorescence staining of α‐actin and ZO‐1 revealed colocalization of these proteins. As in ZO‐1 staining, the pattern of immunolabeling with anti–α‐actin antibody was diffuse in the mdx vessels and pointed or banded in the controls. α‐actin immunogold electron microscopy showed gold particles in the cytoplasms of endothelial cells and pericytes in the mdx mice, whereas α‐actin gold particles were revealed on the endothelial tight junctions and the cytoskeletal microfilaments of pericytes in the controls. Perivascular glial processes of the mdx mice appeared faintly stained by anti‐AQP4 antibody, while in the controls a strong AQP4 labeling of glial processes was detected at light and electron microscope level. The vascular permeability of the mdx brain microvessels was investigated by means of the horseradish peroxidase (HRP). After HRP injection, extensive perivascular areas of marker escape were observed in mdx mice, whereas HRP was exclusively intravascularly localized in the controls. Inflammatory cells, CD4‐, CD8‐, CD20‐, and CD68‐positive cells, were not revealed in the perivascular stroma of the mdx brain. These findings indicate that dystrophin deficiency in the mdx brain leads to severe injury of the endothelial and glial cells with disturbance in α‐actin cytoskeleton, ZO‐1, claudin‐1, and AQP4 assembly, as well as BBB breakdown. The BBB alterations suggest that changes in vascular permeability are involved in the pathogenesis of the neurological dysfunction associated with DMD. GLIA 42:235–251, 2003. © 2003 Wiley‐Liss, Inc.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“Dystrophin knockout mice exhibit a notable brain microvascular phenotype with disrupted endothelial TJs, swollen perivascular glial endfeet, and degenerating microvessels (433).”
From Blood-Brain Barrier: From Physiology to Disease and Back (2019) · cites this paper as [433]
Citations
Cites
Occludin: a novel integral membrane protein localizing at tight junctions.
Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S. (1993) · The Journal of cell biology · doi:10.1083/jcb.123.6.1777 · Cited by 2,580
Furuse, M., Fujita, K., Hiiragi, T., Fujimoto, K., & Tsukita, S. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.7.1539 · Cited by 2,100
X chromosome-linked muscular dystrophy (mdx) in the mouse
Bulfield, G., Siller, W. G., Wight, P. A., & Moore, K. J. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.4.1189 · Cited by 1,765
Stevenson, B. R., Siliciano, J. D., Mooseker, M. S., & Goodenough, D. A. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.3.755 · Cited by 1,640
Astrocytes induce blood–brain barrier properties in endothelial cells
Janzer, R. C., & RAFF, M. C. (1987) · Nature · doi:10.1038/325253a0 · Cited by 1,613
Aquaporin-4 deletion in mice reduces brain edema after acute water intoxication and ischemic stroke
Manley, G. T., Fujimura, M., Ma, T., Noshita, N., Filiz, F., Bollen, A. W., Chan, P. H., & Verkman, A. S. (2000) · Nature Medicine · doi:10.1038/72256 · Cited by 1,501
Nielsen, S. M., Nagelhus, E. A., Amiry-Moghaddam, M. R., Bourque, C. W., Agre, P. C., & Ottersen, O. P. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-01-00171.1997 · Cited by 1,440
Fanning, A. S., Jameson, B. J., Jesaitis, L. A., & Anderson, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29745 · Cited by 1,432
Martín-Padura, I., Lostaglio, S., Schneemann, M., Williams, L., Romano, M., Fruscella, P., Panzeri, C., Stoppacciaro, A., Ruco, L., Villa, A., et al. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.1.117 · Cited by 1,387
Lack of Pericytes Leads to Endothelial Hyperplasia and Abnormal Vascular Morphogenesis
Hellström, M., Gerhardt, H., Kalén, M., Li, X., Eriksson, U., Wolburg, H., & Betsholtz, C. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.3.543 · Cited by 1,132
Flagged first, then by citations
Research works printed but not linked: 1
- Wittchen ES, 1998, Novel binding interactions among tight junction proteins, Mol Biol Cell, 9, 82A
Cited by
Sorted by citations
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
Blood-Brain Barrier: From Physiology to Disease and Back
Sweeney, M. D., Zhao, Z., Montagne, A., Nelson, A. R., & Zlokovic, B. V. (2019) · Physiological Reviews · doi:10.1152/physrev.00050.2017 · Cited by 2,312
Aquaporin water channels in the nervous system
Papadopoulos, M. C., & Verkman, A. S. (2013) · Nature reviews. Neuroscience · doi:10.1038/nrn3468 · Cited by 748
Development of the blood-brain barrier
Engelhardt, B. (2003) · Cell and Tissue Research · doi:10.1007/s00441-003-0751-z · Cited by 386
Astrocytic laminin regulates pericyte differentiation and maintains blood brain barrier integrity
Yao, Y., Chen, Z.-L., Norris, E. H., & Strickland, S. (2014) · Nature Communications · doi:10.1038/ncomms4413 · Cited by 357
A review of progress in understanding the pathophysiology and treatment of brain edema
Marmarou, A. (2007) · Neurosurgical FOCUS · doi:10.3171/foc.2007.22.5.2 · Cited by 333
Three distinct roles of aquaporin-4 in brain function revealed by knockout mice.
Verkman, A., Binder, D., Bloch, O., Auguste, K., & Papadopoulos, M. (2006) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamem.2006.02.018 · Cited by 319
Aquaporin-4 square array assembly: Opposing actions of M1 and M23 isoforms
Furman, C. S., Gorelick-Feldman, D. A., Davidson, K. G. V., Yasumura, T., Neely, J. D., Agre, P. C., & Rash, J. E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2235843100 · Cited by 315
Manley, G. T., Binder, D. K., Papadopoulos, M. C., & Verkman, A. S. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.06.088 · Cited by 312
Amiry-Moghaddam, M. R., Frydenlund, D. S., & Ottersen, O. P. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.08.049 · Cited by 277
The blood–brain barrier in neurodegenerative disease: a rhetorical perspective
Carvey, P. M., Hendey, B., & Monahan, A. J. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06319.x · Cited by 260
Horie, N., Pereira, M. P., Niizuma, K., Sun, G., Keren-Gill, H., Encarnacion, A., Shamloo, M., Hamilton, S. A., Jiang, K., Huhn, S., et al. (2011) · Stem Cells · doi:10.1002/stem.584 · Cited by 240
Current concepts of blood-brain barrier development
Liebner, S., Czupalla, C. J., & Wolburg, H. (2011) · The International Journal of Developmental Biology · doi:10.1387/ijdb.103224sl · Cited by 244
Satellite Cells in Muscular Dystrophy – Lost in Polarity
Chang, N. C., Chevalier, F. P., & Rudnicki, M. A. (2016) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2016.04.002 · Cited by 218
Kr�ger, S., Wolburg, H., & Warth, A. (2004) · Acta Neuropathologica · doi:10.1007/s00401-003-0812-0 · Cited by 202
Nicchia, G. P., Nico, B., Camassa, L. M. A., Mola, M. G., Loh, N., Dermietzel, R., Spray, D. C., Svelto, M., & Frigeri, A. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.07.055 · Cited by 216
Self-citationHaenggi, T., & Fritschy, J. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-005-5461-0 · Cited by 180
Migliati, E., Meurice, N., DuBois, P., Fang, J. S., Somasekharan, S., Beckett, E. A. H., Flynn, G. A., & Yool, A. J. (2009) · Molecular Pharmacology · doi:10.1124/mol.108.053744 · Cited by 166
Brain Water Mobility Decreases after Astrocytic Aquaporin-4 Inhibition Using RNA Interference
Badaut, J., Ashwal, S., Adami, A., Tone, B., Recker, R., Spagnoli, D., Ternon, B., & Obenaus, A. (2010) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2010.163 · Cited by 166
Review: Molecular pathogenesis of blood–brain barrier breakdown in acute brain injury
Nag, S., Kapadia, A. N., & Stewart, D. J. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01138.x · Cited by 163
Neuroimmunological Implications of AQP4 in Astrocytes
Ikeshima‐Kataoka, H. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17081306 · Cited by 151
Altered blood–brain barrier integrity in adult aquaporin-4 knockout mice
Zhou, J., Kong, H., Hua, X., Xiao, M., Ding, J., & Hu, G. (2008) · Neuroreport · doi:10.1097/wnr.0b013e3282f2b4eb · Cited by 144
The role of pericytic laminin in blood brain barrier integrity maintenance
Gautam, J., Zhang, X., & Yao, Y. (2016) · Scientific Reports · doi:10.1038/srep36450 · Cited by 144
Leech, S., Kirk, J., Plumb, J., & McQuaid, S. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00781.x · Cited by 137
Hamm, S., Dehouck, B., Kraus, J., Wolburg‐Buchholz, K., Wolburg, H., Risau, W., Cecchelli, R., Engelhardt, B., & Dehouck, M. (2004) · Cell and Tissue Research · doi:10.1007/s00441-003-0825-y · Cited by 134
Cornford, E. M., & Hyman, S. (2004) · NeuroRx · doi:10.1602/neurorx.2.1.27 · Cited by 132
The role of actin-binding proteins in the control of endothelial barrier integrity
García‐Ponce, A., Citalán‐Madrid, A. F., Velázquez-Avila, M., Vargas‐Robles, H., & Schnoor, M. (2014) · Thrombosis and Haemostasis · doi:10.1160/th14-04-0298 · Cited by 128
Slow CCL2-dependent translocation of biopersistent particles from muscle to brain
Khan, Z., Combadière, C., Authier, F., Itier, V., Lux, F., Exley, C., Mahrouf‐Yorgov, M., Decrouy, X., Moretto, P., Tillement, O., et al. (2013) · BMC Medicine · doi:10.1186/1741-7015-11-99 · Cited by 127
Protection after stroke: cellular effectors of neurovascular unit integrity
Posada‐Duque, R., Barreto, G. E., & Cardona‐Gómez, G. P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00231 · Cited by 122
Guadagno, É., & Moukhles, H. (2004) · Glia · doi:10.1002/glia.20039 · Cited by 123
Dystrophin Dp71: The Smallest but Multifunctional Product of the Duchenne Muscular Dystrophy Gene
Tadayoni, R., Rendón, Á., Soria-Jasso, L. E., & Cisneros, B. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8218-9 · Cited by 120
Oudega, M. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1440-6 · Cited by 121
Dolman, D. E. M., Drndarski, S., Abbott, N. J., & Rattray, M. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03111.x · Cited by 114
Perronnet, C., & Vaillend, C. (2010) · BioMed Research International · doi:10.1155/2010/849426 · Cited by 103
Altered blood–brain barrier development in dystrophic MDX mice
Nico, B., Nicchia, G. P., Frigeri, A., Corsi, P., Mangieri, D., Ribatti, D., Svelto, M., & Roncali, L. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.02.008 · Cited by 102
Self-citationProgranulin Deficiency Promotes Post-Ischemic Blood–Brain Barrier Disruption
Jackman, K. A., Kahles, T., Lane, D., García‐Bonilla, L., Abe, T., Capone, C., Hochrainer, K., Voss, H. U., Zhou, P., Ding, A. H., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.4318-13.2013 · Cited by 99
Benfenati, V., & Ferroni, S. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.12.017 · Cited by 103
Novel roles of aquaporins revealed by phenotype analysis of knockout mice
Verkman, A. S. (2006) · Reviews of Physiology, Biochemistry, and Pharmacology · doi:10.1007/3-540-28217-3_2 · Cited by 97
Sinclair, C., Kirk, J., Herron, B. M., FitzGerald, U., & McQuaid, S. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0169-2 · Cited by 88
Kim, J., Yeo, S., Ryu, H. J., Kim, M., Kim, D., Jo, S., & Kang, T. (2010) · The Journal of Comparative Neurology · doi:10.1002/cne.22482 · Cited by 84
Effects of Aquaporin-4 on edema formation following intracerebral hemorrhage
Tang, Y., Wu, P., Su, J., Xiang, J. Y., Cai, D., & Dong, Q. (2010) · Experimental Neurology · doi:10.1016/j.expneurol.2010.01.015 · Cited by 83
Aquaporin-4 maintains ependymal integrity in adult mice
Li, X., Kong, H., Wu, W., Xiao, M., Sun, X., & Hu, G. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.04.044 · Cited by 81
Fluid dynamics in developmental biology: Moving fluids that shape ontogeny
Cartwright, J. H. E., Piro, O., & Tuval, I. (2008) · HFSP journal · doi:10.2976/1.3043738 · Cited by 74
The Blood–Brain Barrier: Composition, Properties, and Roles in Brain HealthPreprint
Lacoste, B., Prat, A., Andrade, M. F., & Gu, C. (2024) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a041422 · Cited by 83
Lien, C.-F., Mohanta, S., Frontczak-Baniewicz, M., Swinny, J., Zabłocka, B., & Górecki, D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.400044 · Cited by 83
Bragg, A., Amiry-Moghaddam, M., Ottersen, O., Adams, M., & Froehner, S. (2006) · Glia · doi:10.1002/glia.20347 · Cited by 74
Knockdown of MLC1 in primary astrocytes causes cell vacuolation: A MLC disease cell model
Duarri, A., de Heredia, M. L., Capdevila‐Nortes, X., Ridder, M. C., Montolio, M., López-Hernández, T., Boor, I., Lien, C., Hagemann, T. L., Messing, A., et al. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.03.015 · Cited by 71
Aquaporins in development – a review
Liu, H., & Wintour, E. M. (2005) · Reproductive Biology and Endocrinology · doi:10.1186/1477-7827-3-18 · Cited by 69
Bendfeldt, K., Radojevic, V., Kapfhammer, J. P., & Nitsch, C. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4033-06.2007 · Cited by 67
A possible role of dystrophin in neuronal excitability: A review of the current literature
Hendriksen, R. G. F., Hoogland, G., Schipper, S., Hendriksen, J. G. M., Vles, J. S. H., & Aalbers, M. W. (2015) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2015.01.023 · Cited by 63
Vitellaro‐Zuccarello, L., Mazzetti, S., Bosisio, P., Monti, C., & Biasi, S. D. (2005) · Glia · doi:10.1002/glia.20196 · Cited by 64
Qi, X., Inagaki, K., Sobel, R. A., & Mochly‐Rosen, D. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32636 · Cited by 61
Pericytic Laminin Maintains Blood-Brain Barrier Integrity in an Age-Dependent Manner
Gautam, J., Cao, Y., & Yao, Y. (2019) · Translational Stroke Research · doi:10.1007/s12975-019-00709-8 · Cited by 60
Kim, J., Ryu, H. J., & Kang, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0074458 · Cited by 63
Vitellaro‐Zuccarello, L., Mazzetti, S., Madaschi, L., Bosisio, P., Fontana, E., Gorio, A., & Biasi, S. D. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.11.004 · Cited by 60
Targeting angiogenesis in Duchenne muscular dystrophy
Podkalicka, P., Mucha, O., Dulak, J., & Łoboda, A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03006-7 · Cited by 59
Watts, L. T., Sprague, S., Zheng, W., Garling, R. J., Jimenez, D., Digicaylioglu, M., & Lechleiter, J. D. (2013) · Journal of Neurotrauma · doi:10.1089/neu.2012.2488 · Cited by 58
Zabłocka, B., Górecki, D. C., & Zabłocki, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222011040 · Cited by 54
Cherkaoui, M. B., Vacca, O., Izabelle, C., Boulay, A., Boulogne, C., Gillet, C., Barnier, J., Rendón, Á., Cohen‐Salmon, M., & Vaillend, C. (2020) · Glia · doi:10.1002/glia.23941 · Cited by 52
Eilert‐Olsen, M., Haj‐Yasein, N. N., Vindedal, G. F., Enger, R., Gundersen, G. A., Hoddevik, E. H., Petersen, P. H., Haug, F. Š., Skare, Ø., Adams, M. E., et al. (2011) · Glia · doi:10.1002/glia.22277 · Cited by 54
Nico, B., Mangieri, D., Tamma, R., Longo, V., Annese, T., Enrico Crivellato, B., Pollo, B., Maderna, E., Ribatti, D., & Salmaggi, A. (2009) · European Journal of Cancer · doi:10.1016/j.ejca.2009.09.023 · Cited by 52
Self-citationAquaporin-4 and Alzheimer’s Disease
Yang, C., Huang, X., Huang, X., Mai, H., Li, J., Jiang, T., Wang, X., & Lü, T. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150949 · Cited by 53
Zhao, F. L., Deng, J., Xu, X., Cao, F., Lu, K., Li, D., Cheng, X., Wang, X., & Zhao, Y. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1203-8 · Cited by 52
Ohlendieck, K., & Swandulla, D. (2021) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-021-02623-1 · Cited by 48
Morphology and Properties of Brain Endothelial Cells
Nag, S. (2010) · Methods in molecular biology · doi:10.1007/978-1-60761-938-3_1 · Cited by 54
Tham, D. K. L., Joshi, B., & Moukhles, H. (2016) · PLoS ONE · doi:10.1371/journal.pone.0165439 · Cited by 46
Noël, G. P. J. C., Tham, D. K. L., & Moukhles, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.010090 · Cited by 43
Yang, J., Cao, C., Liu, J., Liu, Y., Lü, J., Yu, H., Li, X., Wu, J., Yu, Z., Li, H., et al. (2024) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106586 · Cited by 45
Bake, S., Okoreeh, A. K., Khosravian, H., & Sohrabji, F. (2018) · Experimental Neurology · doi:10.1016/j.expneurol.2018.09.016 · Cited by 42
Hämmerling, B., Gründ, C., Boda‐Heggemann, J., Moll, R., & Franke, W. W. (2005) · Cell and Tissue Research · doi:10.1007/s00441-005-0090-3 · Cited by 41
MLC1 protein: a likely link between leukodystrophies and brain channelopathies
Brignone, M. S., Lanciotti, A., Camerini, S., Nuccio, C. D., Petrucci, T. C., Visentin, S., & Ambrosini, E. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00106 · Cited by 39
Glial dystrophin-associated proteins, laminin and agrin, are downregulated in the brain of mdx mouse
Nico, B., Tamma, R., Annese, T., Mangieri, D., Luca, A. D., Corsi, P., Benagiano, V., Longo, V., Enrico Crivellato, B., Salmaggi, A., et al. (2010) · Laboratory Investigation · doi:10.1038/labinvest.2010.149 · Cited by 39
Self-citationAqp 9 and Brain Tumour Stem Cells
Fossdal, G., Vik-Mo, E. O., Sandberg, C. J., Varghese, M., Kaarbø, M., Telmo, E., Langmoen, I. A., & Murrell, W. G. (2012) · The Scientific World JOURNAL · doi:10.1100/2012/915176 · Cited by 38
Emotional behavior and brain anatomy of the mdx52 mouse model of Duchenne muscular dystrophy
Saoudi, A., Zarrouki, F., Sebrié, C., Izabelle, C., Goyenvalle, A., & Vaillend, C. (2021) · Disease Models & Mechanisms · doi:10.1242/dmm.049028 · Cited by 38
Nico, B., Mangieri, D., Enrico Crivellato, B., Longo, V., Giorgis, M. D., Capobianco, C., Corsi, P., Benagiano, V., Roncali, L., & Ribatti, D. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00090.x · Cited by 37
Self-citationSheen, S. H., Kim, J., Ryu, H. J., Yang, Y., Choi, K., & Kang, T. (2010) · Brain Research · doi:10.1016/j.brainres.2010.10.080 · Cited by 35
Inhibition of angiogenesis by β-galactosylceramidase deficiency in globoid cell leukodystrophy
Belleri, M., Ronca, R., Coltrini, D., Nico, B., Ribatti, D., Poliani, P. L., Giacomini, A., Alessi, P., Marchesini, S., Santos, M. B., et al. (2013) · Brain · doi:10.1093/brain/awt215 · Cited by 35
Self-citationAltered astrocyte morphology and vascular development in dystrophin‐ D p71‐null mice
Giocanti‐Auregan, A., Vacca, O., Bénard, R., Cao, S., Siqueiros‐Márquez, L., Montáñez, C., Pâques, M., Sahel, J., Sennlaub, F., Guillonneau, X., et al. (2015) · Glia · doi:10.1002/glia.22956 · Cited by 34
Breathing in Duchenne muscular dystrophy: translation to therapy
Mhandire, D. Z., Burns, D. P., Roger, A. L., O’Halloran, K. D., & ElMallah, M. K. (2022) · The Journal of Physiology · doi:10.1113/jp281671 · Cited by 37
Amtul, Z., & Hepburn, J. D. (2014) · Reviews in the Neurosciences · doi:10.1515/revneuro-2013-0041 · Cited by 30
Simon, M. J., Murchison, C., & Iliff, J. J. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24082 · Cited by 32
Goren, O., Adorjan, I., & Kálmán, M. (2006) · Anatomy and Embryology · doi:10.1007/s00429-005-0067-8 · Cited by 35
Lack of dystrophin results in abnormal cerebral diffusion and perfusion in vivo
Goodnough, C. L., Gao, Y., Li, X., Qutaish, M. Q., Goodnough, L. H., Molter, J. P., Wilson, D. L., Flask, C. A., & Yu, X. (2014) · NeuroImage · doi:10.1016/j.neuroimage.2014.08.053 · Cited by 31
Rurak, J., Noël, G. P. J. C., Lui, L., Joshi, B., & Moukhles, H. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04886.x · Cited by 31
Murphy, S., Zweyer, M., Henry, M. A., Meleady, P., Mundegar, R. R., Swandulla, D., & Ohlendieck, K. (2015) · Clinical Proteomics · doi:10.1186/s12014-015-9099-0 · Cited by 31
Ron, N. P., Kazianis, J. A., Padbury, J. F., Brown, C. M., McGonnigal, B., Sysyn, G. D., Sadowska, G. B., & Stonestreet, B. S. (2005) · Reproduction Fertility and Development · doi:10.1071/rd03044 · Cited by 29
Tight Junctions in the Blood–Brain Barrier
Wolburg, H., Lippoldt, A., & Ebnet, K. (2002) · Springer eBooks · doi:10.1007/978-0-387-30380-2_1 · Cited by 30
Park, H., Choi, S.-H., Kong, M.-J., & Kang, T. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00236 · Cited by 28
Tamma, R., Annese, T., Capogrosso, R. F., Cozzoli, A., Benagiano, V., Sblendorio, V. T., Ruggieri, S., Enrico Crivellato, B., Specchia, G., Ribatti, D., et al. (2013) · Laboratory Investigation · doi:10.1038/labinvest.2013.46 · Cited by 28
Self-citationAstrocytes in rare neurological conditions: Morphological and functional considerations
Ravi, K., Paidas, M. J., Saad, A. G., & Jayakumar, A. R. (2021) · The Journal of Comparative Neurology · doi:10.1002/cne.25118 · Cited by 28
Qiu, G., Xu, J., Zhuo, F., Sun, S., Liu, H., Yang, M., Huang, J., Lu, W., & Huang, S. (2014) · Neuroscience Letters · doi:10.1016/j.neulet.2014.12.053 · Cited by 27
Jung, H. K., Ryu, H. J., Kim, M.-J., Kim, W. I., Choi, H. K., Choi, H., Song, H., Jo, S., & Kang, T. (2012) · Brain Research · doi:10.1016/j.brainres.2012.01.057 · Cited by 27
Boda‐Heggemann, J., Régnier‐Vigouroux, A., & Franke, W. W. (2008) · Cell and Tissue Research · doi:10.1007/s00441-008-0718-1 · Cited by 27
Nico, B., Corsi, P., Ria, R., Enrico Crivellato, B., Vacca, A., Roccaro, A. M., Mangieri, D., Ribatti, D., & Roncali, L. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.02.077 · Cited by 26
Self-citationPreethish‐Kumar, V., Shah, A., Kumar, M., Ingalhalikar, M., Polavarapu, K., Afsar, M., Rajeswaran, J., Vengalil, S., Nashi, S., Thomas, P. T., et al. (2020) · American Journal of Neuroradiology · doi:10.3174/ajnr.a6604 · Cited by 25
Xu, S., Shi, D., Pratt, S. J. P., Zhu, W., Marshall, A. D., & Lovering, R. M. (2015) · Neuromuscular Disorders · doi:10.1016/j.nmd.2015.07.003 · Cited by 25
Jo, S., Ryu, H. J., Kim, J., Yeo, S., Kim, M.-J., Choi, H., Song, H., & Kang, T. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.06.032 · Cited by 24
Characterization of a Dmd EGFP reporter mouse as a tool to investigate dystrophin expression
Petkova, M. V., Morales-Gonzalez, S., Relizani, K., Gill, E., Seifert, F., Radke, J., Stenzel, W., Garcı́a, L., Amthor, H., & Schuelke, M. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0095-5 · Cited by 24
Ramiro, L., Simats, A., Penalba, A., García-Tornel, Á., Rovira, À., Mancha, F., Bustamante, A., & Montaner, J. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2019.134580 · Cited by 20
Baby, S. M., Bogdanovich, S., Willmann, G., Basu, U., Lozynska, O., & Khurana, T. S. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00275.x · Cited by 22
Metadata
- Authors
- Nico, B., Frigeri, A., Nicchia, G. P., Corsi, P., Ribatti, D., Quondamatteo, F., Herken, R., Girolamo, F., Marzullo, A., Svelto, M., & Roncali, L.
- Affiliations
- University of Bari Aldo Moro (IT)
- University of Göttingen (DE)
- Corresponding author
- Nico, Beatrice
- ORCID
- Venue
- Glia
- Publisher
- Wiley
- Published
- 2003-03-18
- Volume
- 42
- Issue
- 3
- Pages
- 235-251
- ISSN
- 0894-1491 (ISSN-L)
- 1098-1136
- OpenAlex
- W2001178402
- Cited by
- 172
- References
- 93
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 5 · 2023: 4 · 2022: 4 · 2021: 6 · 2020: 4 · 2019: 12 · 2018: 5 · 2017: 1 · 2016: 10 · 2015: 7 · 2014: 9 · 2013: 8 · 2012: 8
- FWCI
- 7.07
- Type
- journal article
- Language
- en
- Open access
- Locations
- Glia (publishedVersion)
- PubMed (publishedVersion)
- GRO (submittedVersion, cc-by)
- CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- blood-brain barrier, Duchenne muscular dystrophy, mdx mice, dystrophin deficiency, endothelial cells, astrocytes, tight junctions, ZO-1, claudin-1, aquaporin-4, alpha-actin, pericytes
- MeSH terms
- Actins, Animals, Antigens, Surface, Astrocytes, Blood-Brain Barrier, Brain, Disease Models, Animal, Endothelium, Vascular, Female, Horseradish Peroxidase, Immunohistochemistry, Membrane Proteins, Microscopy, Electron, Phosphoproteins, Biomarkers, Down-Regulation, Mice, Inbred mdx, Tight Junctions, Aquaporins, Muscular Dystrophy, Duchenne, Mice, Aquaporin 4, Claudin-1, Zonula Occludens-1 Protein
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
