The DOI matches its Crossref record; 40 of the 40 references it cites were found in a registry or an index.
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.
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
“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
Cited by
Sorted by citations
Items 301–400 of 468
Heck, N., Garwood, J., Dobbertin, A., Calco, V., Sirko, S., Mittmann, T., Eysel, U. T., & Faissner, A. (2007) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.06.002 · Cited by 17
Hurdles in treating Hurler disease: potential routes to achieve a “real” cure
van den Broek, B. T. A., van Doorn, J., Hegeman, C. V., Nierkens, S., Lindemans, C. A., Verhoeven‐Duif, N. M., Boelens, J. J., & van Hasselt, P. M. (2020) · Blood Advances · doi:10.1182/bloodadvances.2020001708 · Cited by 17
Giamanco, K. A., & Matthews, R. T. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-48457-6_7 · Cited by 17
Nandigam, R. K., & Kroll, D. M. (2007) · Biophysical Journal · doi:10.1529/biophysj.106.095547 · Cited by 17
Abi‐Ghanem, C., Jonnalagadda, D., Chun, J. J. M., Kihara, Y., & Ranscht, B. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.908401 · Cited by 16
Boiczyk, G. M., Pearson, N., Kote, V. B., Sundaramurthy, A., Subramaniam, D. R., Rubio, J. E., Unnikrishnan, G. U., Jaques Reifman, A., & Monson, K. L. (2022) · Journal of Biomechanical Engineering · doi:10.1115/1.4056480 · Cited by 16
Aspberg, A. (2016) · Springer eBooks · doi:10.1007/978-3-319-29568-8_1 · Cited by 16
New insights into the altered fibronectin matrix and extrasynaptic transmission in the aging brain
Wang, J., Yin, L., & Chen, Z. (2011) · Journal of Clinical Gerontology and Geriatrics · doi:10.1016/j.jcgg.2010.12.002 · Cited by 16
Yamada, J., Ohgomori, T., & Jinno, S. (2017) · The Journal of Comparative Neurology · doi:10.1002/cne.24198 · Cited by 17
Perspective: The role of mechanobiology in the etiology of brain metastasis
Tanner, K. (2018) · APL Bioengineering · doi:10.1063/1.5024394 · Cited by 18
Tumor Dormancy and Reactivation: The Role of Heat Shock Proteins
Amissah, H. A., Combs, S. E., & Shevtsov, M. A. (2024) · Cells · doi:10.3390/cells13131087 · Cited by 15
Defining standard enzymatic dissociation methods for individual brains and spinal cords in EAE
Hussain, R. Z., Miller-Little, W. A., Doelger, R., Cutter, G., Loof, N., Cravens, P. D., & Stüve, O. (2018) · Neurology Neuroimmunology & Neuroinflammation · doi:10.1212/nxi.0000000000000437 · Cited by 15
Day, J. M., Murdoch, A. D., & Hardingham, T. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38107 · Cited by 15
Seiler, A., Sood, A. K., Jenewein, J., & Fagundes, C. P. (2019) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2019.12.013 · Cited by 14
Altered Extracellular Matrix as an Alternative Risk Factor for Epileptogenicity in Brain Tumors
de Jong, J. M., Broekaart, D. W. M., Bongaarts, A., Mühlebner, A., Mills, J. D., van Vliet, E. A., & Aronica, E. (2022) · Biomedicines · doi:10.3390/biomedicines10102475 · Cited by 15
Patlay, A. A., Belousov, A. S., Silant’ev, V. E., Shatilov, R. A., Shmelev, M. E., Ковалев, В. В., Perminova, I. V., Baklanov, I., & Kumeiko, V. V. (2023) · Polymers · doi:10.3390/polym15153280 · Cited by 14
Bieler, L., Vogl, M., Kirchinger, M., Urmann, C., Riepl, H., Bandtlow, C. E., Klimaschewski, L. P., Aigner, L., & Couillard‐Després, S. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00332 · Cited by 14
Cost-Effective Cosmetic-Grade Hyaluronan Hydrogels for ReNcell VM Human Neural Stem Cell Culture
Ma, W., & Suh, W. H. (2019) · Biomolecules · doi:10.3390/biom9100515 · Cited by 14
Mechanical properties of human glioma
Tsitlakidis, A., Aifantis, E. C., Κritis, A., Tsingotjidou, A., Cheva, A., Selviaridis, P., & Foroglou, N. (2020) · Neurological Research · doi:10.1080/01616412.2020.1796381 · Cited by 15
Altered migration and adhesion potential of pro-neurally converted human bone marrow stromal cells
Habisch, H., Fiedler, J., Ludolph, A. C., Storch, A., & Brenner, R. E. (2008) · Cytotherapy · doi:10.1080/14653240802474331 · Cited by 14
Kuehn, M. H., Stone, E. M., & Hageman, G. S. (2001) · PubMed · Cited by 14
I-type lectins in the nervous system
Probstmeier, R., & Pesheva, P. (1999) · Progress in Neurobiology · doi:10.1016/s0301-0082(98)00079-3 · Cited by 14
Kapellos, G. E., & Alexiou, T. S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-415824-5.00001-1 · Cited by 13
Architecture of cartilage tissue and its adaptation to pathological conditions
Şenol, M. S., & Özer, H. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-812162-7.00007-2 · Cited by 13
Pigino, G. F., Morfini, G. A., & Brady, S. T. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-374947-5.00007-9 · Cited by 14
Vincent, M., Gaudin, M., Lucas‐Torres, C., Wong, A., Escartin, C., & Valette, J. (2021) · NMR in Biomedicine · doi:10.1002/nbm.4478 · Cited by 13
MURAKAMI, T., Murakami, T., Sato, H., MUBARAK, W. A. E.-D., Ohtsuka, A., & Abe, K. (1999) · Archivum histologicum japonicum · doi:10.1679/aohc.62.71 · Cited by 13
Bahia, C. P., Houzel, J., Diniz, C. W. P., & Pereira, A. (2008) · The Journal of Comparative Neurology · doi:10.1002/cne.21781 · Cited by 13
Extracellular Matrix Recycling as a Novel Plasticity Mechanism With a Potential Role in Disease
Dankovich, T. M., & Rizzoli, S. O. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.854897 · Cited by 12
Sorhun, D. T., Kuşoğlu, A., & Öztürk, E. (2023) · ACS Omega · doi:10.1021/acsomega.3c04064 · Cited by 12
Heterogeneity of brain extracellular matrix and astrocyte activation
Huber, R. E., Babbitt, C. C., & Peyton, S. R. (2024) · Journal of Neuroscience Research · doi:10.1002/jnr.25356 · Cited by 15
Morita, T., Fujikawa, K., Baba, O., & Shibata, S. (2016) · Gene Expression Patterns · doi:10.1016/j.gep.2016.06.002 · Cited by 12
Pertussis Toxin Is a Robust and Selective Inhibitor of High Grade Glioma Cell Migration and Invasion
Gilder, A. S., Wang, L., Natali, L., Karimi-Mostowfi, N., Brifault, C., & Gonias, S. L. (2016) · PLoS ONE · doi:10.1371/journal.pone.0168418 · Cited by 12
Filali, H., Vidal, E., Bolea, R., Márquez, M., Marco-Salazar, P., Vargas, A., Pumarola, M. B., Martín‐Burriel, I., & Badiola, J. J. (2013) · Veterinary Research · doi:10.1186/1297-9716-44-14 · Cited by 14
Zimmermann, D. R. (2000) · CRC Press eBooks · doi:10.1201/9780203909720.ch13 · Cited by 12
Tenascin-R as a regulator of CNS glial cell function
Pesheva, P., Gloor, S. M., & Probstmeier, R. (2001) · Progress in brain research · doi:10.1016/s0079-6123(01)32069-1 · Cited by 12
MURAKAMI, T., Murakami, T., Luo Jia, H. O. N. G., Wei Dong, S. U., Da Xun, P. I. A. O., Mahmut, N., & Ohtsuka, A. (1997) · Archivum histologicum japonicum · doi:10.1679/aohc.60.347 · Cited by 12
Zhang, G., Jin, L., Rodemer, W., Hu, J., Root, Z. D., Medeiros, D. M., & Selzer, M. E. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.918871 · Cited by 12
Live Mapping of the Brain Extracellular Matrix and Remodeling in Neurological Disorders
Ge, X., Xu, X., Cai, Q., Xiong, H., Xie, C., Hong, Y., Gao, X., Yao, Y., Bachoo, R. M., & Qin, Z. (2023) · Small Methods · doi:10.1002/smtd.202301117 · Cited by 13
Singh, T., Kothapalli, C. R., Varma, D. M., Nicoll, S. B., & Vázquez, M. (2014) · Journal of Biomaterials Applications · doi:10.1177/0885328214532969 · Cited by 11
Intermolecular cross-talk in tumor metastasis
Skouteris, G. G., & Nicolson, G. L. (1999) · IOS Press eBooks · Cited by 11
Central Nervous System Tissue Engineering: Current Considerations and Strategies
Wilkinson, A. E., McCormick, A. M., & Leipzig, N. D. (2011) · Synthesis lectures on tissue engineering · doi:10.2200/s00390ed1v01y201111tis008 · Cited by 10
Najjary, S., de Koning, W., Kros, J. M., & Mustafa, D. A. M. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1305644 · Cited by 10
The Extracellular Matrix in Neural Development, Plasticity, and Regeneration
Garwood, J., Heck, N., Rigato, F., & Faissner, A. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-108-4_5 · Cited by 11
Stroke: A double-edged sword for cleaving clots?
Anthony, D. C., & Perry, V. H. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70171-x · Cited by 10
Wang, L., Chen, H., Wang, Z., Ning, D., Zhao, W. G., Rat, V., Lamb, D. C., Pang, D., & Liu, S. (2024) · Advanced Materials · doi:10.1002/adma.202311457 · Cited by 9
Sullivan, D. J., Wu, X., Gallo, N. R., Naughton, N. M., Georgiadis, J. G., & Pelegri, A. A. (2020) · Physics in Medicine and Biology · doi:10.1088/1361-6560/aba0cc · Cited by 9
Ion Transport and Radioresistance
Roth, B., & Huber, S. M. (2020) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2020_33 · Cited by 9
Tsitlakidis, A., Tsingotjidou, A., Κritis, A., Cheva, A., Selviaridis, P., Aifantis, E. C., & Foroglou, N. (2021) · Cancers · doi:10.3390/cancers13184539 · Cited by 9
Sulfation Pattern Dependent Iron(III) Mediated Interleukin‐8 Glycan Binding
Brunori, F., Padhi, D. K., Alshanski, I., Freyse, J., Dürig, J., Penk, A., Vaccaro, L., Hurevich, M., Rademann, J., & Yitzchaik, S. (2021) · ChemBioChem · doi:10.1002/cbic.202100552 · Cited by 9
Mukhina, I. V., Александровна, К. С., & Dityatev, A. E. (2012) · Neurochemical Journal · doi:10.1134/s1819712412020055 · Cited by 8
Yoneda, M., Nakamura, T., Murai, M., & Wada, H. (2010) · Journal of Molecular Evolution · doi:10.1007/s00239-010-9363-x · Cited by 8
Metzger, M., Bartsch, S., Bartsch, U., Bock, J., Schachner, M., & Braun, K. A. (2006) · Neuroscience · doi:10.1016/j.neuroscience.2006.05.025 · Cited by 9
Histochemical study of perineuronal nets in the retrosplenial cortex of adult rats
Sayed, R., Mubarak, W., Ohtsuka, A., TAGUCHI, T., & MURAKAMI, T. (2002) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/s0940-9602(02)80048-6 · Cited by 9
Prestressed Composite Polymer Gels as a Model of the Extracellular-Matrix of Cartilage
Chremos, A., Douglas, J. F., Basser, P. J., & Horkay, F. (2022) · Gels · doi:10.3390/gels8110707 · Cited by 8
Thomas, I., William, P., & Sarah, K. (2011) · InTech eBooks · doi:10.5772/19775 · Cited by 7
Longitudinal biometal accumulation and Ca isotope composition of the Göttingen minipig brain
Mahan, B., Antonelli, M. A., Bürckel, P., Turner, S., Chung, R. S., Habekost, M., Jørgensen, A. L., & Moynier, F. (2020) · Metallomics · doi:10.1039/d0mt00134a · Cited by 8
Distinct Glycosylation Responses to Spinal Cord Injury in Regenerative and Nonregenerative Models
Ronan, R., Kshirsagar, A., Rebelo, A. L., Sunny, A., Kilcoyne, M., O’Flaherty, R., Rudd, P. M., Schlosser, G., Saldova, R., Pandit, A. S., et al. (2022) · Journal of Proteome Research · doi:10.1021/acs.jproteome.2c00043 · Cited by 8
Uskoković, V., Huynh, E., & Wu, V. (2020) · Journal of Nanoparticle Research · doi:10.1007/s11051-020-04892-w · Cited by 8
Modulating Microenvironments for Treating Glioblastoma
Roberts, L. M., & Munson, J. M. (2020) · Current Tissue Microenvironment Reports · doi:10.1007/s43152-020-00010-z · Cited by 10
Han, S., Kim, J., Kim, S. H., Youn, W., Kim, J., Ji, G. Y., Yang, S., Park, J., Lee, G. M., Kim, Y., et al. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.09.046 · Cited by 7
Blanco, I., Deasy, S., Amontree, M., Gabriel, M., Caccavano, A., Vicini, S., Glasgow, E. F., & Conant, K. E. (2025) · Molecular Psychiatry · doi:10.1038/s41380-025-03007-y · Cited by 7
Structure, Biosynthesis, and Function of Glycosaminoglycans
Jones, C. L., Liu, J., & Xu, D. (2010) · Elsevier eBooks · doi:10.1016/b978-008045382-8.00132-5 · Cited by 7
Sadeghi, S. M., Negah, S. S., Khaksar, Z., Kazemi, H., & Aligholi, H. (2014) · The Neuroscience Journal of Shefaye Khatam · doi:10.18869/acadpub.shefa.2.1.69 · Cited by 7
Sandeep, M., & Nandini, C. (2017) · Metabolic Brain Disease · doi:10.1007/s11011-017-0019-z · Cited by 7
Compressive tumours cause neuronal damage
Janmey, P. A., & Pogoda, K. (2019) · Nature Biomedical Engineering · doi:10.1038/s41551-019-0370-y · Cited by 7
Ježek, K., Schulz, D., Silva, M. A. D. S., Müller, H.-W., Huston, J. P., & Hasenöhrl, R. U. (2003) · Behavioural Brain Research · doi:10.1016/s0166-4328(03)00138-4 · Cited by 7
Xie, M., Wang, T., Feng, J., Ma, D., Feng, L., & Hao, Y. (2025) · Current Neuropharmacology · doi:10.2174/1570159x23666250225091729 · Cited by 7
The extracellular matrix as a dynamic regulator of brain function and plasticity
Ge, C., & Tajerian, M. (2026) · Neurobiology of Disease · doi:10.1016/j.nbd.2026.107374 · Cited by 8
Alcaide, D., Cacheux, J., Bancaud, A., Muramatsu, R., & Matsunaga, Y. T. (2023) · Biomaterials Science · doi:10.1039/d3bm00027c · Cited by 7
Perineuronal Net Microscopy: From Brain Pathology to Artificial Intelligence
Paveliev, M., Egorchev, A. A., Musin, F., Lipachev, N., Melnikova, A., Gimadutdinov, R. M., Kashipov, A., Molotkov, D., Chickrin, D. E., & Aganov, A. V. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25084227 · Cited by 8
Harmonic viscoelastic response of 3D histology-informed white matter model
Wu, X., Georgiadis, J. G., & Pelegri, A. A. (2022) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2022.103782 · Cited by 6
Jakovljević, A., Stamenković, V., Poleksić, J., Hamad, M. I. K., Reiss, G., Jakovčevski, I., & Anđjus, P. R. (2024) · Biomolecules · doi:10.3390/biom14040508 · Cited by 7
Chrissa, A., & Russell, T. (2011) · InTech eBooks · doi:10.5772/21709 · Cited by 7
Chondroitin Sulfate Proteoglycans in the Brain
Aono, S., & Oohira, A. (2006) · Advances in pharmacology · doi:10.1016/s1054-3589(05)53015-1 · Cited by 6
Multiple Species and Functions of Proteoglycans in the Central Nervous System
Oohira, A. (2007) · Elsevier eBooks · doi:10.1016/b978-044451967-2/00095-7 · Cited by 6
Systematic Review of Peptide CAQK: Properties, Applications, and Outcomes
Castillo, J. A., Le, M. N., Ratcliff, A., Soufi, K. H., Huang, K., Vatoofy, S., Ghaffari‐Rafi, A., Emerson, S., Reynolds, E., Pivetti, C. D., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252010990 · Cited by 6
Subdiffusion in an array of solid obstacles
Postnikov, E. B., & Sokolov, I. M. (2024) · Journal of Physics A Mathematical and Theoretical · doi:10.1088/1751-8121/ad1d90 · Cited by 5
Gonsalves, N., Sun, M. K., Chopra, P., Latchoumane, C.-F. V., Bajwa, S., Tang, R., Patel, B., Boons, G., & Karumbaiah, L. (2024) · Journal of Neural Engineering · doi:10.1088/1741-2552/ad5108 · Cited by 5
Wang, J., Wang, X., Rong, W., Lv, J., Wei, F., & Liu, Z. (2014) · Neurochemical Research · doi:10.1007/s11064-014-1442-8 · Cited by 5
Koessinger, D., Novo, D., Koessinger, A. L., Campos, A. V., Peters, J., Dutton, L. R., Paschke, P., Zerbst, D., Moore, M. H., Mitchell, L. E., et al. (2023) · Neuro-Oncology Advances · doi:10.1093/noajnl/vdad067 · Cited by 5
Jeong, Y., Kim, Y. S., Jin, S., Pei, J., Wen, M., Kim, I., Moon, K., Jung, T., Ryu, H., & Jung, S. (2013) · International Journal of Nanomedicine · doi:10.2147/ijn.s52577 · Cited by 5
Amyloid Fibrils in Neurodegenerative Diseases: Villains or Heroes?
Fernàndez‐Busquets, X. (2013) · Future Medicinal Chemistry · doi:10.4155/fmc.13.138 · Cited by 5
Proteoglycans (Glycosaminoglycans/Mucopolysaccharides)
Nakano, T., Dixon, W. T., & Ozimek, L. (2002) · Biopolymers Online · doi:10.1002/3527600035.bpol6016 · Cited by 5
Using REMBRANDT to Paint in the Details of Glioma Biology: Applications for Future Immunotherapy
An, Q., Neil, T., Ge, L., Arismendi, G. R., Paleo, B. J., Esteban, J., Shon, D. J., Hong, E., Ahmed, M., & Martin, R. (2013) · InTech eBooks · doi:10.5772/52363 · Cited by 4
Three-dimensional culture systems in central nervous system research
Onuwaje, I., & Phillips, J. B. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818084-6.00016-7 · Cited by 4
Mécanismes cellulaires et moléculaires de la croissance axonale
Gaillard, S., Nasarre, C., Gonthier, B., & Bagnard, D. (2005) · Revue Neurologique · doi:10.1016/s0035-3787(05)85019-2 · Cited by 4
Stem Cells for Targeting CNS Malignancy
Yip, S. S. F., Sidman, R. L., & Snyder, E. Y. (2005) · KARGER eBooks · doi:10.1159/000084482 · Cited by 4
Logun, M. T., Begley, S. L., Hicks, K., Park, J., Zhang, L., Binder, Z. A., & O’Rourke, D. M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.11.637648 · Cited by 4
High-fidelity predictions of diffusion in the brain microenvironment
Schimek, N., Wood, T. R., Beck, D. A. C., McKenna, M., Toghani, A., & Nance, E. A. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.10.005 · Cited by 5
Gáti, G., & Lendvai, D. (2013) · Orvosi Hetilap · doi:10.1556/oh.2013.29646 · Cited by 3
Clotting Promotes Glioma Growth and Infiltration Through Activation of Focal Adhesion Kinase
Knowles, L. M., Wolter, C., Linsler, S., Müller, S. J., Urbschat, S., Ketter, R., Müller, A., Zhou, X., Qu, B., Senger, S., et al. (2024) · Cancer Research Communications · doi:10.1158/2767-9764.crc-24-0164 · Cited by 4
Junghans, U., Franken, S., Pommer, A., Müller, H. W., Viebahn, C., & Kappler, J. (2002) · Histochemistry and Cell Biology · doi:10.1007/s00418-002-0394-2 · Cited by 3
Salehi, Z. (2009) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2008.06.010 · Cited by 3
Integrated Vascular Engineering: Vascularization of Reconstructed Tissue
Sudo, R., Chung, S. H., Shin, Y., & Tanishita, K. (2016) · Springer eBooks · doi:10.1007/978-4-431-54801-0_16 · Cited by 3
Histochemistry and Cytochemistry of Endogenous Animal Lectins
Akimoto, Y., Hirano, H., Imai, Y., Hirabayashi, J., & Kasai, K. (1998) · Progress in Histochemistry and Cytochemistry · doi:10.1016/s0079-6336(98)80002-8 · Cited by 3
A neuroprotective tetrapeptide for treatment of acute traumatic brain injury
Mann, A. P., Hussain, S., Scodeller, P., Moore, H. N. B., Sherazee, E. A., Russo, R. M., & Ruoslahti, E. (2025) · EMBO Molecular Medicine · doi:10.1038/s44321-025-00312-5 · Cited by 2
Self-citationGómez, A., Tran, U. T., Grozdanov, P. N., & Cornwall, G. A. (2026) · Journal of Neuroscience Research · doi:10.1002/jnr.70113 · Cited by 2
Emerging Therapeutic Role of Chondroitinase (ChABC) in Neurological Disorders and Cancer
Kolathur, K. K., Kumar, A., Biswas, A., Bojja, S. L., & Subrahmanyam, V. M. (2022) · Current Drug Therapy · doi:10.2174/1574885517666220331151619 · Cited by 3
Lin, S., Zhang, X., Chen, S., Lin, C., & Chiu, Y. (2021) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2021/9163279 · Cited by 2
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
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