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Brain extracellular matrix
Abstract
The extracellular matrix of the adult brain tissue has a unique composition. The striking feature of this matrix is the prominence of lecticans, proteoglycans that contain a lectin domain and a hyaluronic acid-binding domain. Hyaluronic acid and tenascin family adhesive/anti-adhesive proteins are also abundant. Matrix proteins common in other tissues are nearly absent in adult brain. The brain extracellular matrix appears to have trophic effects on neuronal cells and affect neurite outgrowth. The unique composition of this matrix may be responsible for the resistance of brain tissue toward invasion by tumors of non-neuronal origin.
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“The striking feature of the brain ECM is the prominence of proteoglycans and hyaluronan with the exception of basement membrane structures (Ruoslahti, 1996).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Ruoslahti, 1996
In the citing paper
“The current concept of supramolecular organization and assembly of PNN was first proposed by Ruoslahti (1996) and designated as “HLT (hyaluronan, lecticans and TN-R)” model by Yamaguchi (2000) (Fig. 2).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Ruoslahti, 1996
Citations
Cites
Proteoglycans as modulators of growth factor activities
Ruoslahti, E. I., & Yamaguchi, Y. (1991) · Cell · doi:10.1016/0092-8674(91)90308-l · Cited by 1,342
Self-citationWillis, R. A. (1948) · Butterworths eBooks · Cited by 1,254
Selectins: Interpreters of Cell-Specific Carbohydrate Information During Inflammation
Lasky, L. A. (1992) · Science · doi:10.1126/science.1439808 · Cited by 1,236
Varki, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.16.7390 · Cited by 946
Proteoglycans in Cell Regulation
Ruoslahti, E. I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)80001-1 · Cited by 679
Self-citationMultiple domains of the large fibroblast proteoglycan, versican.
Zimmermann, D., & Ruoslahti, E. I. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08447.x · Cited by 652
Self-citationGladson, C. L., & Cheresh, D. A. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115516 · Cited by 415
Chondroitin Sulfate as a Regulator of Neuronal Patterning in the Retina
Brittis, P. A., Canning, D. R., & Silver, J. (1992) · Science · doi:10.1126/science.1738848 · Cited by 415
Isolation of a neural chondroitin sulfate proteoglycan with neurite outgrowth promoting properties.
Faissner, A., Clement, A. M., Lochter, A., Streit, A., Mandl, C., & Schachner, M. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.3.783 · Cited by 354
Schönherr, E., Järveläinen, H., Sandell, L. J., & Wight, T. N. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47419-x · Cited by 335
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Extracellular Matrix Assembly: A Multiscale Deconstruction
Mouw, J. K., Ou, G., & Weaver, V. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3902 · Cited by 1,534
Diffusion in Brain Extracellular Space
Syková, E., & Nicholson, C. (2008) · Physiological Reviews · doi:10.1152/physrev.00027.2007 · Cited by 1,481
Extracellular space structure revealed by diffusion analysis
Nicholson, C., & Syková, E. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01261-2 · Cited by 914
Lecticans: organizers of the brain extracellular matrix
Yamaguchi, Y. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000690 · Cited by 642
Proteoglycans in the Developing Brain: New Conceptual Insights for Old Proteins
Bandtlow, C. E., & Zimmermann, D. R. (2000) · Physiological Reviews · doi:10.1152/physrev.2000.80.4.1267 · Cited by 632
Rasmussen, M. K., Mestre, H., & Nedergaard, M. (2021) · Physiological Reviews · doi:10.1152/physrev.00031.2020 · Cited by 642
Extracellular matrix molecules and synaptic plasticity
Dityatev, A., & Schachner, M. (2003) · Nature Reviews Neuroscience · doi:10.1038/nrn1115 · Cited by 564
Diffusion and related transport mechanisms in brain tissue
Nicholson, C. (2001) · Reports on Progress in Physics · doi:10.1088/0034-4885/64/7/202 · Cited by 498
Extracellular matrix of the central nervous system: from neglect to challenge
Zimmermann, D. R., & Dours-Zimmermann, M. T. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0485-9 · Cited by 465
A stoichiometric complex of neurexins and dystroglycan in brain
Sugita, S., Saito, F., Tang, J., Satz, J., Campbell, K., & Südhof, T. (2001) · Journal of Cell Biology · doi:10.1083/jcb.200105003 · Cited by 453
Fibulins: a versatile family of extracellular matrix proteins
Timpl, R., Sasaki, T., Kostka, G., & Chu, M.-L. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1130 · Cited by 494
Extracellular matrix and perineuronal nets in CNS repair
Kwok, J. C. F., Dick, G., Wang, D., & Fawcett, J. W. (2011) · Developmental Neurobiology · doi:10.1002/dneu.20974 · Cited by 395
The perineuronal net and the control of CNS plasticity
Wang, D., & Fawcett, J. (2012) · Cell and Tissue Research · doi:10.1007/s00441-012-1375-y · Cited by 373
Miroshnikova, Y. A., Mouw, J. K., Barnes, J. M., Pickup, M. W., Lakins, J. N., Kim, Y., Lobo, K. A., Persson, A. I., Reis, G. F., McKnight, T. R., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3429 · Cited by 390
Composition of Perineuronal Net Extracellular Matrix in Rat Brain
Deepa, S. S., Carulli, D., Galtrey, C., Rhodes, K., Fukuda, J., Mikami, T., Sugahara, K., & Fawcett, J. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600544200 · Cited by 367
Härtig, W., Derouiche, A., Welt, K., Brauer, K., Grosche, J., Mäder, M., Reichenbach, A., & Brückner, G. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01784-9 · Cited by 339
Molecular mechanisms of dendritic spine development and remodeling
Ethell, I. M., & Pasquale, E. B. (2005) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2005.02.003 · Cited by 367
Ananthanarayanan, B., Kim, Y., & Kumar, S. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.07.005 · Cited by 337
Tissue mechanics regulate brain development, homeostasis and disease
Barnes, J. M., Przybyla, L., & Weaver, V. M. (2017) · Journal of Cell Science · doi:10.1242/jcs.191742 · Cited by 344
Mechanics in Neuronal Development and Repair
Franze, K., Janmey, P. A., & Guck, J. R. (2013) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-071811-150045 · Cited by 322
Lo, E. H., Wang, X., & Cuzner, M. L. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10270 · Cited by 310
Hydrogels derived from central nervous system extracellular matrix
Medberry, C. J., Crapo, P. M., Siu, B. F., Carruthers, C. A., Wolf, M. T., Nagarkar, S. P., Agrawal, V., Jones, K. E., Kelly, J., Johnson, S. A., et al. (2012) · Biomaterials · doi:10.1016/j.biomaterials.2012.10.062 · Cited by 278
Aspberg, A., Miura, R., Bourdoulous, S., Shimonaka, M., Heinegård, D., Schachner, M., Ruoslahti, E., & Yamaguchi, Y. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.19.10116 · Cited by 275
Self-citationDifferential matrix metalloproteinase expression in cases of multiple sclerosis and stroke
Anthony, D. C., Ferguson, B., Matyzak, M. K., Miller, K., Esiri, M. M., & Perry, V. H. (1997) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1997.tb01315.x · Cited by 268
The Medium of Haptic Perception: A Tensegrity Hypothesis
Turvey, M. T., & Fonseca, S. T. (2014) · Journal of Motor Behavior · doi:10.1080/00222895.2013.798252 · Cited by 239
Decellularized Porcine Brain Matrix for Cell Culture and Tissue Engineering Scaffolds
DeQuach, J. A., Yuan, S. H., Goldstein, L. S. B., & Christman, K. L. (2011) · Tissue Engineering Part A · doi:10.1089/ten.tea.2010.0724 · Cited by 234
Reinhard, S. M., Razak, K., & Ethell, I. M. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00280 · Cited by 219
3D in vitro modeling of the central nervous system
Hopkins, A. M., DeSimone, E. K., Chwalek, K., & Kaplan, D. L. (2014) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2014.11.003 · Cited by 234
CD44-Mediated Adhesion to Hyaluronic Acid Contributes to Mechanosensing and Invasive Motility
Kim, Y., & Kumar, S. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0629 · Cited by 229
Yamada, H., Fredette, B. J., Shitara, K., Hagihara, K., Miura, R., Ranscht, B., Stallcup, W. B., & Yamaguchi, Y. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-20-07784.1997 · Cited by 228
Immune determinants of the pre-metastatic niche
Pătraș, L., Shaashua, L., Matei, I. R., & Lyden, D. C. (2023) · Cancer Cell · doi:10.1016/j.ccell.2023.02.018 · Cited by 229
Isogai, Z., Aspberg, A., Keene, D. R., Ono, R. N., Reinhardt, D. P., & Sakai, L. Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110583200 · Cited by 222
Compression stiffening of brain and its effect on mechanosensing by glioma cells
Pogoda, K., Chin, L., Georges, P. C., Byfield, F. J., Bucki, R., Kim, R., Weaver, M. W., Wells, R. G., Marcinkiewicz, C., & Janmey, P. A. (2014) · New Journal of Physics · doi:10.1088/1367-2630/16/7/075002 · Cited by 216
Fibulin-1 Is a Ligand for the C-type Lectin Domains of Aggrecan and Versican
Aspberg, A., Adam, S., Kostka, G., Timpl, R., & Heinegård, D. K. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20444 · Cited by 207
Defining and designing polymers and hydrogels for neural tissue engineering
Aurand, E. R., Lampe, K. J., & Bjugstad, K. B. (2011) · Neuroscience Research · doi:10.1016/j.neures.2011.12.005 · Cited by 210
Olin, A. I., Mörgelin, M., Sasaki, T., Timpl, R., Heinegård, D. K., & Aspberg, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006783200 · Cited by 204
Brückner, G., Hausen, D., Härtig, W., Drlicek, M., Arendt, T., & Brauer, K. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00071-8 · Cited by 196
Brain derived versican V2 is a potent inhibitor of axonal growth
Schmalfeldt, M., Bandtlow, C. E., Dours-Zimmermann, M. T., Winterhalter, K. H., & Zimmermann, D. R. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.5.807 · Cited by 197
Extracellular matrix components associated with remodeling processes in brain
Rauch, U. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4043-x · Cited by 199
Arendt, T. (2003) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2003.09.007 · Cited by 189
Kitagawa, H., Tsutsumi, K., Tone, Y., & Sugahara, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.50.31377 · Cited by 187
Extracellular matrix abnormalities in schizophrenia
Berretta, S. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.08.010 · Cited by 179
Biology of Fibrocartilage Cells
BENJAMIN, M., & Ralphs, J. R. (2004) · International review of cytology · doi:10.1016/s0074-7696(04)33001-9 · Cited by 189
Mann, A. P., Scodeller, P., Hussain, S., Joo, J., Kwon, E. J., Braun, G. B., Mölder, T., She, Z. G., Kotamraju, V. R., Ranscht, B., et al. (2016) · Nature Communications · doi:10.1038/ncomms11980 · Cited by 187
Self-citationAnthony, D. C., Miller, K., Fearn, S., Townsend, M. J., Opdenakker, G., Wells, G., Clements, J. M., Chandler, S., Gearing, A. J. H., & Perry, V. H. (1998) · Journal of Neuroimmunology · doi:10.1016/s0165-5728(98)00046-0 · Cited by 180
Miyata, S., & Kitagawa, H. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.06.010 · Cited by 171
Brevican Is Degraded by Matrix Metalloproteinases and Aggrecanase-1 (ADAMTS4) at Different Sites
Nakamura, H., Fujii, Y., Inoki, I., Sugimoto, K., Tanzawa, K., Matsuki, H., Miura, R., Yamaguchi, Y., & Okada, Y. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003875200 · Cited by 168
Scaffolds for 3D in vitro culture of neural lineage cells
Murphy, A. R., Laslett, A. L., O’Brien, C., & Cameron, N. R. (2017) · Acta Biomaterialia · doi:10.1016/j.actbio.2017.02.046 · Cited by 160
Koh, I., Cha, J., Park, J., Choi, J., Kang, S., & Kim, P. (2018) · Scientific Reports · doi:10.1038/s41598-018-22681-3 · Cited by 163
Park, M., Kim, M., Park, I., Kang, H., Yoo, H., Park, S. H., Rhee, C. H., Hong, S., & Lee, S. (2002) · European Journal of Cancer · doi:10.1016/s0959-8049(02)80906-6 · Cited by 155
In Vitro Microfluidic Models for Neurodegenerative Disorders
Osaki, T., Shin, Y., Sivathanu, V., Campisi, M., & Kamm, R. D. (2017) · Advanced Healthcare Materials · doi:10.1002/adhm.201700489 · Cited by 155
Collagen–Alginate Composite Hydrogel: Application in Tissue Engineering and Biomedical Sciences
Hu, T., & Lo, A. C. Y. (2021) · Polymers · doi:10.3390/polym13111852 · Cited by 155
The perineuronal net component of the extracellular matrix in plasticity and epilepsy
McRae, P. A., & Porter, B. E. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.08.007 · Cited by 143
Blended alginate/collagen hydrogels promote neurogenesis and neuronal maturation
Moxon, S. R., Corbett, N. J., Fisher, K., Potjewyd, G., Domingos, M. A. N., & Hooper, N. M. (2019) · Materials Science and Engineering C · doi:10.1016/j.msec.2019.109904 · Cited by 148
Novel immunogenic antigen homologous to hyaluronidase in meningioma
Heckel, D., Comtesse, N., Brass, N., Blin, N., Zang, K. D., & Meese, E. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.12.1859 · Cited by 140
Hiraoka, N., Nakagawa, H., Ong, E., Akama, T. O., Fukuda, M. N., & Fukuda, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002443200 · Cited by 139
Mechanobiology of the brain in ageing and Alzheimer's disease
Hall, C. M., Moeendarbary, E., & Sheridan, G. K. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.14766 · Cited by 140
Biology and Models of the Blood–Brain Barrier
Hajal, C., Roi, B. L., Kamm, R. D., & Maoz, B. M. (2021) · Annual Review of Biomedical Engineering · doi:10.1146/annurev-bioeng-082120-042814 · Cited by 143
Oohashi, T., Edamatsu, M., Bekku, Y., & Carulli, D. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.09.010 · Cited by 131
Biofabrication methods for reconstructing extracellular matrix mimetics
Aazmi, A., Zhang, D., Mazzaglia, C., Yu, M., Wang, Z., Yang, H., Huang, Y. Y. S., & Ma, L. (2023) · Bioactive Materials · doi:10.1016/j.bioactmat.2023.08.018 · Cited by 142
The Different Roles of Aggrecan Interaction Domains
Aspberg, A. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412464376 · Cited by 130
Fibulin-3 Is Uniquely Upregulated in Malignant Gliomas and Promotes Tumor Cell Motility and Invasion
Hu, B., Rajamani, K. T., Sim, H., & Viapiano, M. S. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0207 · Cited by 135
Glycosaminoglycans and β-amyloid, prion and tau peptides in neurodegenerative diseases
Díaz‐Nido, J., Wandosell, F. G., & Ávila, J. (2002) · Peptides · doi:10.1016/s0196-9781(02)00068-2 · Cited by 131
The role of integrins in immune-mediated diseases of the nervous system
Archelos, J. J., Previtali, S. C., & Hartung, H.-P. (1999) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01287-9 · Cited by 130
Day, J. M., Olin, A. I., Murdoch, A. D., Canfield, A., Sasaki, T., Timpl, R., Hardingham, T. E., & Aspberg, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400242200 · Cited by 127
A 2020 view of tension-based cortical morphogenesis
Essen, D. C. V. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2016830117 · Cited by 124
Structural Basis for Interactions between Tenascins and Lectican C-Type Lectin Domains
Lundell, A., Olin, A. I., Mörgelin, M., al-Karadaghi, S., Aspberg, A., & Logan, D. T. (2004) · Structure · doi:10.1016/j.str.2004.05.021 · Cited by 127
Oohashi, T., Hirakawa, S., Bekku, Y., Rauch, U., Zimmermann, D. R., Su, W.-D., Ohtsuka, A., Murakami, T., & Ninomiya, Y. (2002) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2001.1061 · Cited by 124
Immunotherapies for malignant glioma
Boussiotis, V. A., & Charest, A. (2017) · Oncogene · doi:10.1038/s41388-017-0024-z · Cited by 126
Processive DNA synthesis by DNA polymerase II mediated by DNA polymerase III accessory proteins.
Bonner, C. A., Stukenberg, P. T., Rajagopalan, M. R., Eritja, R., O’Donnell, M. E., McEntee, K., Echols, H., & Goodman, M. F. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49928-6 · Cited by 125
John, N., Krügel, H., Frischknecht, R., Smalla, K.-H., Schultz, C., Kreutz, M. R., Gundelfinger, E. D., & Seidenbecher, C. I. (2006) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2006.01.011 · Cited by 122
Sood, D., Chwalek, K., Stuntz, E., Pouli, D., Du, C., Tang‐Schomer, M. D., Georgakoudi, I., Black, L. D., & Kaplan, D. L. (2015) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.5b00446 · Cited by 123
Xu, C., Chang, Y., Wu, P., Liu, K., Dong, X., Nie, A., Mu, C., Liu, Z., Dai, H., & Luo, Z. (2021) · Advanced Functional Materials · doi:10.1002/adfm.202104440 · Cited by 124
The Proteoglycan Lectin Domain Binds Sulfated Cell Surface Glycolipids and Promotes Cell Adhesion
Miura, R., Aspberg, A., Ethell, I. M., Hagihara, K., Schnaar, R. L., Ruoslahti, E. I., & Yamaguchi, Y. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.11431 · Cited by 119
Self-citationSpatially Gradated Hydrogel Platform as a 3D Engineered Tumor Microenvironment
Pedrón, S., Becka, E., & Harley, B. A. C. (2014) · Advanced Materials · doi:10.1002/adma.201404896 · Cited by 120
Soria, F. N., Paviolo, C., Doudnikoff, É., Arotçarena, M.-L., Lee, A., Danné, N., Mandal, A. K., Gosset, P., Dehay, B., Groc, L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-17328-9 · Cited by 124
Versican V2 Is a Major Extracellular Matrix Component of the Mature Bovine Brain
Schmalfeldt, M., Dours-Zimmermann, M. T., Winterhalter, K. H., & Zimmermann, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.25.15758 · Cited by 118
Johnson, J. K., Nowicki, M. O., Lee, C., Chiocca, E. A., Viapiano, M. S., Lawler, S. E., & Lannutti, J. J. (2009) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2008.0486 · Cited by 120
Novel enzymatically cross-linked hyaluronan hydrogels support the formation of 3D neuronal networks
Broguière, N., Isenmann, L., & Zenobi‐Wong, M. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.04.036 · Cited by 116
Brain organoid formation on decellularized porcine brain ECM hydrogels
Simsa, R., Rothenbücher, T., Gürbüz, H., Ghosheh, N., Emneus, J., Jenndahl, L., Kaplan, D. L., Bergh, N., Serrano, A. M., & Fogelstrand, P. (2021) · PLOS ONE · doi:10.1371/journal.pone.0245685 · Cited by 114
Impact of the biophysical features of a 3D gelatin microenvironment on glioblastoma malignancy
Pedrón, S., & Harley, B. A. C. (2013) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.34637 · Cited by 113
The extracellular matrix in multiple sclerosis pathology
van Horssen, J., Dijkstra, C. D., & de Vries, H. E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04897.x · Cited by 114
Jin, Y., Lee, J. S., Kim, J., Min, S., Wi, S., Yu, J. H., Chang, G.-E., Cho, A., Choi, Y., Ahn, D.-H., et al. (2018) · Nature Biomedical Engineering · doi:10.1038/s41551-018-0260-8 · Cited by 116
Li, H., Leung, T.-C., Hoffman, S., Balsamo, J., & Lilien, J. E. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.6.1275 · Cited by 111
Acid-degradable lipid nanoparticles enhance the delivery of mRNA
Zhao, S., Gao, K., Han, H., Stenzel, M., Yin, B., Song, H., Lawanprasert, A., Nielsen, J. E., Sharma, R. K., Arogundade, O. H., et al. (2024) · Nature Nanotechnology · doi:10.1038/s41565-024-01765-4 · Cited by 117
Diffusion of molecules in brain extracellular space: theory and experiment
Nicholson, C., Chen, K. C., Hrabětová, S., & Tao, L. (2000) · Progress in brain research · doi:10.1016/s0079-6123(00)25007-3 · Cited by 110
Molecular Cloning and Expression of Chondroitin 4-Sulfotransferase
Yamauchi, S., Mita, S., Matsubara, T., Fukuta, M., Habuchi, H., Kimata, K., & Habuchi, O. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8975 · Cited by 111
Katt, M. E., Linville, R. M., Mayo, L. N., Xu, Z. S., & Searson, P. C. (2018) · Fluids and Barriers of the CNS · doi:10.1186/s12987-018-0092-7 · Cited by 102
Magnetic resonance elastography (MRE) in cancer: Technique, analysis, and applications
Pepin, K. M., Ehman, R. L., & McGee, K. P. (2015) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2015.06.001 · Cited by 111
Indyk, J. A., Chen, Z. L., Tsirka, S. E., & Strickland, S. (2003) · Neuroscience · doi:10.1016/s0306-4522(02)00704-2 · Cited by 107
Mechanosensation in traumatic brain injury
Keating, C. E., & Cullen, D. K. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105210 · Cited by 109
HIF1A signaling selectively supports proliferation of breast cancer in the brain
Ebright, R. Y., Zachariah, M. A., Micalizzi, D. S., Wittner, B. S., Niederhoffer, K., Nieman, L. T., Chirn, B., Wiley, D. F., Wesley, B., Shaw, B. L., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-20144-w · Cited by 104
Rahmani, M., Wong, B. W., Ang, L. S., Cheung, C., Carthy, J. M., Walinski, H., & McManus, B. M. (2006) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y05-154 · Cited by 105
Inatani, M., & Tanihara, H. (2002) · Progress in Retinal and Eye Research · doi:10.1016/s1350-9462(02)00009-5 · Cited by 105
From barriers to bridges: chondroitin sulfate proteoglycans in neuropathology
Viapiano, M. S., & Matthews, R. T. (2006) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.08.007 · Cited by 103
Differential response of patient-derived primary glioblastoma cells to environmental stiffness
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The α5β1 Integrin Mediates Elimination of Amyloid-β Peptide and Protects Against Apoptosis
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Self-citationExtracellular matrix control of dendritic spine and synapse structure and plasticity in adulthood
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Metadata
- Authors
- Ruoslahti, E.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- Corresponding author
- Ruoslahti, Erkki
- ORCID
- Ruoslahti, Erkki
- Venue
- Glycobiology
- Publisher
- Oxford University Press (OUP)
- Published
- 1996
- Volume
- 6
- Issue
- 5
- Pages
- 489-492
- ISSN
- 0959-6658 (ISSN-L)
- 1460-2423
- OpenAlex
- W1988575276
- Cited by
- 467
- References
- 40
- Citations by year
- 2026: 10 · 2025: 7 · 2024: 15 · 2023: 14 · 2022: 22 · 2021: 28 · 2020: 35 · 2019: 23 · 2018: 17 · 2017: 19 · 2016: 18 · 2015: 17 · 2014: 25 · 2013: 16 · 2012: 19
- FWCI
- 6.05
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Glycobiology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Karolinska Institutet
- National Institutes of Health (5p01ca028896-15)
- National Cancer Institute (CA30199, CA 28896, P30CA030199)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- brain extracellular matrix, lecticans, proteoglycans, hyaluronic acid, tenascin, matrix protein, neurite outgrowth
- MeSH terms
- Adult, Brain Chemistry, Extracellular Matrix, Humans, Hyaluronic Acid, Protein Binding, Proteoglycans, Tenascin, Lectins
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