The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.
Mice Deficient for Tenascin-R Display Alterations of the Extracellular Matrix and Decreased Axonal Conduction Velocities in the CNS
Open accessAbstract
Tenascin-R (TN-R), an extracellular matrix glycoprotein of the CNS, localizes to nodes of Ranvier and perineuronal nets and interacts in vitro with other extracellular matrix components and recognition molecules of the immunoglobulin superfamily. To characterize the functional roles of TN-R in vivo, we have generated mice deficient for TN-R by homologous recombination using embryonic stem cells. TN-R-deficient mice are viable and fertile. The anatomy of all major brain areas and the formation and structure of myelin appear normal. However, immunostaining for the chondroitin sulfate proteoglycan phosphacan, a high-affinity ligand for TN-R, is weak and diffuse in the mutant when compared with wild-type mice. Compound action potential recordings from optic nerves of mutant mice show a significant decrease in conduction velocity as compared with controls. However, at nodes of Ranvier there is no apparent change in expression and distribution of Na+channels, which are thought to bind to TN-R via their β2 subunit. The distribution of carbohydrate epitopes of perineuronal nets recognized by the lectin Wisteria floribunda or antibodies to the HNK-1 carbohydrate on somata and dendrites of cortical and hippocampal interneurons is abnormal. These observations indicate an essential role for TN-R in the formation of perineuronal nets and in normal conduction velocity of optic nerve.
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?
In the citing paper
“TN-R knockout mice (TN-R−/−)”
From Aggrecan, link protein and tenascin-R are essential components of the perineuronal net to protect neurons against iron-induced oxidative stress (2014) · cites this paper as [33]
In the citing paper
“As mentioned above, TN-R knockout mice show abnormal PNN staining, with irregular distribution of WFA around soma and dendrites (Brückner et al., 2000;Morawski et al., 2014;Weber et al., 1999).”
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 Weber et al., 1999
In the citing paper
“Tnr-deficient mice were phenotypically normal, although they exhibited a significant decrease in conduction velocity as compared with wild-type mice.”
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 Weber et al., 1999
In the citing paper
“Immunostaining of phosphacan, a high-affinity ligand for TN-R, showed it to be weak and diffuse at the nodes in the knockouts when compared to wild-type mice.”
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 Weber et al., 1999
In the citing paper
“Thereafter, several extracellular molecules of proteoglycans (e.g.phosphacan) and glycoproteins (e.g.TN-R) were found to localize at the nodes of Ranvier (Weber et al., 1999;Ratcliffe et al., 2000).”
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 Weber et al., 1999
In the citing paper
“Actually, disruption of any single nodal ECM gene does not affect the clustering of nodal Na + channels (Bekku et al., 2010;Dours-Zimmermann et al., 2009;Weber et al., 1999).”
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 Weber et al., 1999
In the citing paper
“While the clustering of nodal sodium channels and paranodal structures appear unaffected in both Vcan V0/V2-and Tnr-deficient mice, effect on the conduction velocity is different in the three types of mutants (V0/V2-, Tnr-andHapln2/Bral1-deficient mice), probably due to the differences of degree of disturbed ECM assembly (Bekku et al., 2010;Dours-Zimmermann et al., 2009;Weber et al., 1999).”
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 Weber et al., 1999
In the citing paper
“While the clustering of nodal sodium channels and paranodal structures appear unaffected in both Vcan V0/V2-and Tnr-deficient mice, effect on the conduction velocity is different in the three types of mutants (V0/V2-, Tnr-andHapln2/Bral1-deficient mice), probably due to the differences of degree of disturbed ECM assembly (Bekku et al., 2010;Dours-Zimmermann et al., 2009;Weber et al., 1999).”
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 Weber et al., 1999
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
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Towbin, H., Staehelin, T., & Gordon, J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4350 · Cited by 53,218
Raza, H., John, A., & Nemmar, A. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350087 · Cited by 47,311
A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity
Feinberg, A. P., & Vogelstein, B. (1983) · Analytical Biochemistry · doi:10.1016/0003-2697(83)90418-9 · Cited by 24,512
Yanisch-Perron, C., Vieira, J., & Messing, J. W. (1985) · Gene · doi:10.1016/0378-1119(85)90120-9 · Cited by 14,909
The Mouse Brain in Stereotaxic Coordinates
Paxinos, G. (2001) · Cited by 12,859
The structure of the nervous system of the nematode Caenorhabditis elegans
White, J. G., Southgate, E., Thomson, J. N., & Brenner, S. (1986) · Philosophical Transactions of the Royal Society of London. B, Biological Sciences · doi:10.1098/rstb.1986.0056 · Cited by 5,589
Manipulating the mouse embryo: A laboratory manual
Hogan, B. L. M., Costantini, F. D., & Lacy, E. (1986) · Cited by 4,460
Targeted disruption of the c-src proto-oncogene leads to osteopetrosis in mice
Soriano, P. M., Montgomery, C. A., Geske, R. S., & Bradley, A. (1991) · Cell · doi:10.1016/0092-8674(91)90499-o · Cited by 1,997
Mansour, S. L., Thomas, K. R., & Capecchi, M. R. (1988) · Nature · doi:10.1038/336348a0 · Cited by 1,683
Research works printed but not linked: 4
- Erickson, 1994, Evolution of the tenascin family: implications for the function of the C-terminal fibrinogen-like domain., Perspect Dev Neurobiol, 2, 9
- Peters A Palay SL Webster HD (1991) The fine structure of the nervous system, p 235. (Oxford, New York).
- Rasband, 1998, Clustering of Na+ and K+ channels during development of myelinated central nervous system axons., Soc Neurosci Abstr, 24, 830
- Srinivasan, 1997, Interaction between neuronal voltage gated sodium channels and the extracellular matrix protein tenascin., Soc Neurosci Abstr, 23, 909
Cited by
Sorted by citations
Items 201–247 of 247
Kaur, S., & Roberts, D. D. (2021) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-020-00598-9 · Cited by 4
Wang, B., Wang, Z., Lv, L., Wang, X., Lu, J., Zhao, Y., Jiang, R., Li, Q., Kong, Y., Yang, X., et al. (2025) · Alzheimer s & Dementia · doi:10.1002/alz.70633 · Cited by 3
Neural extracellular matrix regulates visual sensory motor integration
Reinhard, J., Mueller-Buehl, C., Wiemann, S., Roll, L., Luft, V., Shabani, H., Rathbun, D. L., Gan, L., Kuo, C., Franzen, J., et al. (2024) · iScience · doi:10.1016/j.isci.2024.108846 · Cited by 3
Expression of tenascin R and J1 mRNA in motoneurons after a traumatic lesion in the spinal cord
Lindholm, T., Cullheim, S., Carlstedt, T. P., & Risling, M. (2001) · Neuroreport · doi:10.1097/00001756-200111160-00028 · Cited by 3
Axon Initial Segment: Structure, Biological Functions, Diseases, and Therapeutic Targets
Song, D., Yuan, L., Yang, W., Li, W., & Li, J. (2026) · MedComm · doi:10.1002/mco2.70689 · Cited by 2
Quantitative Morphological Analyses of the Striatum and Cerebellum of Tenascin-R deficient mice
Steen, A.-B. (2006) · Cited by 2
Nouveautés sur les mécanismes de formation des nœuds de Ranvier
Devaux, J. J. (2014) · Revue Neurologique · doi:10.1016/j.neurol.2014.03.017 · Cited by 2
Structure and Function of Myelinated Axons
Buffington, S. A., & Rasband, M. N. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-397265-1.00078-2 · Cited by 2
Self-citationNeural extracellular matrix regulates visual sensory motor integrationPreprint
Reinhard, J., Mueller-Buehl, C., Wiemann, S., Roll, L., Luft, V., Shabani, H., Rathbun, D. L., Gan, L., Kuo, C., Franzen, J., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.17.537074 · Cited by 2
Nakayama, K., Mubuchi, A., & Miyata, S. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.05.29.656756 · Cited by 2
Yue, L., Craig, M. T., & Morris, B. J. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05369-4 · Cited by 2
3 – Molecular Specializations at the Glia-Axon Interface
Peles, E. (2005) · Elsevier eBooks · doi:10.1016/b978-012738761-1/50004-3 · Cited by 1
Involvement of the cerebellum in cocaine-induced memory
Carbo‐Gas, M. (2017) · Tesis Doctorals en Xarxa (Consorci de Serveis Universitaris de Catalunya) · doi:10.6035/14023.2017.208925 · Cited by 1
Recycling as a mechanism for extracellular matrix remodeling at the synapse
Dankovich, T. M. (2021) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8998 · Cited by 1
Chiquet‐Ehrismann, R. (2002) · Wiley Encyclopedia of Molecular Medicine · doi:10.1002/0471203076.emm0606 · Cited by 1
Dialogues: Communication Between Axons and Myelinating Glia
Gould, R. M., & Brady, S. T. (2005) · Elsevier eBooks · doi:10.1016/b978-012738761-1/50003-1 · Cited by 1
Herberholz, M. (2005) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.4893
Study of the role of type V collagen in heritable connective tissue diseases
Symoens, S. (2012) · Ghent University Academic Bibliography (Ghent University)
Structure and Functions of Voltage-Dependent Na+ Channels
Imoto, K. (2000) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-57083-4_1
Chondroitin Sulfate Proteoglycans Regulate Experience-Dependent Neuronal Plasticity
Miyata, S., & Kitagawa, H. (2011) · Trends in Glycoscience and Glycotechnology · doi:10.4052/tigg.23.239
Perinodal ECM - its role in diffusion barrier formation and conduction velocity in the CNS
Bekku, Y., Ninomiya, Y., & Oohashi, T. (2012) · Okayama Igakkai Zasshi (Journal of Okayama Medical Association) · doi:10.4044/joma.124.1
Review Neurocan: a brain chondroitin sulfate proteoglycan
Rauch, U., & Feng, K. (2001)
Liu, S. C. (2017) · Illinois Digital Environment for Access to Learning and Scholarship (University of Illinois at Urbana-Champaign)
The molecular organization and function of paranodal septate junctions
Garcia‐Fresco, G. P. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/zpc6-bt79
Nguyen, T. H. (2019) · DSpace@MIT (Massachusetts Institute of Technology)
Structural and Functional Remodeling of the Extracellular Matrix during Brain Development and Aging
Miyata, S. (2021) · Trends in Glycoscience and Glycotechnology · doi:10.4052/tigg.2003.1e
Structural and Functional Remodeling of the Extracellular Matrix during Brain Development and Aging
Miyata, S. (2021) · Trends in Glycoscience and Glycotechnology · doi:10.4052/tigg.2003.1j
(2006) · Elsevier eBooks · doi:10.1016/b978-0-443-07271-0.50022-7
Nakamura, T., & BORNSTEIN, P. K. (2020) · Elsevier eBooks · doi:10.1016/b978-0-08-102723-3.00009-3 · Cited by 2
Structure and function of myelinated axons
Buffington, S. A., & Rasband, M. N. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-814405-3.00040-0
Self-citationActivity-dependent turnover of the Perineural Extracellular Matrix
Petersen, G. C. (2024) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-10429
Zhang, H., Cicvaric, A., Bassett, T. E., Wood, E. M., Petrovic, Z., & Radulović, J. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-15754-7.00066-3
Linde, J., Yildiz, C. B., Vöhringer, K., Nabbefeld, G., Graff, S., Pensold, D., Reichard, J., Hermanns, M., Weber-Hamacher, C., Spehr, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.11.18.689032
KIAA 0510, Ténascine R, et astrocytomes pilocytiques
Ayachi, I. E. (2010) · theses.fr (ABES) · doi:10.70675/0e9b78fcz07aaz49baz9438z0925e5029be4
Mechanisms of central nervous system nodes of Ranvier assembly
Freeman, S. A. (2015) · theses.fr (ABES) · doi:10.70675/8a8a095cze5faz4cd3z8fcez185fe0291fb2
Devienne, G. F. (2019) · theses.fr (ABES) · doi:10.70675/453418efzc908z49e0zba6fz71fefaa50691
Thétiot, M. (2018) · theses.fr (ABES) · doi:10.70675/4fd006d4z6c0ez4fe8zbcd0z0df8b8ef8d85
The Aging Brain Matrix: Cross-Species Evidence Linking FREM3 to Brain and Cognitive AgingPreprint
Clifford, K. P., Prévot, T. D., Sumitomo, A., Das, S., Bansal, Y., Marcotte, M. D., Zhou, R., Yeung, J. H. M., Ding, M., Felsky, D., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-11381729/v1
Postnatal development of perineuronal nets in wild-type mice and in a mutant deficient in tenascin-R
Br�ckner, G., Grosche, J., Schmidt, S., H�rtig, W., Margolis, R. U., Delpech, B., Seidenbecher, C. I., Czaniera, R., & Schachner, M. (2000) · The Journal of Comparative Neurology · doi:10.1002/1096-9861(20001225)428:4
Self-citationZujovic (2000) · doi:10.1002/(sici)1098-1136(20000215)29:4
Self-citation
Metadata
- Authors
- Weber, P., Bartsch, U., Rasband, M. N., Czaniera, R., Lang, Y., Bluethmann, H., Margolis, R. U., Levinson, S. R., Shrager, P., Montag, D., & Schachner, M.
- Affiliations
- ETH Zurich (CH)
- Universität Hamburg (DE)
- University of Rochester Medicine (US)
- F. Hoffmann-La Roche AG (CH)
- NYU Langone Health (US)
- University of Colorado Denver (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 1999-06-01
- Volume
- 19
- Issue
- 11
- Pages
- 4245-4262
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6782606
- OpenAlex
- W2124266106
- Cited by
- 247
- References
- 93
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 3 · 2023: 1 · 2022: 4 · 2021: 11 · 2020: 9 · 2019: 7 · 2018: 5 · 2017: 14 · 2016: 6 · 2015: 9 · 2014: 9 · 2013: 6 · 2012: 9
- FWCI
- 5.67
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Rutgers University Community Repository (Rutgers University) (submittedVersion)
- Funders
- Multiple Sclerosis Society
- Deutsche Forschungsgemeinschaft
- Schweizerische Multiple Sklerose Gesellschaft
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- tenascin-R, extracellular matrix, perineuronal nets, nodes of Ranvier, axonal conduction velocity, optic nerve, phosphacan, chondroitin sulfate proteoglycans, interneurons
- MeSH terms
- Animals, Axons, Cells, Cultured, Central Nervous System, Microscopy, Electron, Nerve Net, Nerve Tissue Proteins, Neural Conduction, Optic Nerve, Ranvier's Nodes, Stem Cells, Extracellular Matrix Proteins, Mice, Knockout, Myelin-Associated Glycoprotein, Tenascin, 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
