The DOI matches its Crossref record; 76 of the 77 references it cites were found in a registry or an index.
Perineuronal net formation and structure in aggrecan knockout mice
Open accessAbstract
Perineuronal nets (PNNs) are specialized substructures of the neural extracellular matrix (ECM) which envelop the cell soma and proximal neurites of particular sets of neurons with apertures at sites of synaptic contact. Previous studies have shown that PNNs are enriched with chondroitin sulfate proteoglycans (CSPGs) and hyaluronan, however, a complete understanding of their precise molecular composition has been elusive. In addition, identifying which specific PNN components are critical to the formation of this structure has not been demonstrated. Previous work in our laboratory has demonstrated that the CSPG, aggrecan, is a key activity-dependent component of PNNs in vivo. In order to assess the contribution of aggrecan to PNN formation, we utilized cartilage matrix deficiency (cmd) mice, which lack aggrecan. Herein, we utilized an in vitro model, dissociated cortical culture, and an ex vivo model, organotypic slice culture, to specifically investigate the role aggrecan plays in PNN formation. Our work demonstrates that staining with the lectin, Wisteria floribunda agglutinin (WFA), considered a broad PNN marker, is eliminated in the absence of aggrecan, suggesting the loss of PNNs. However, in contrast, we found that the expression patterns of other PNN markers, including hyaluronan and proteoglycan link protein 1 (HAPLN1), tenascin-R, brevican, and hyaluronan are unaffected by the absence of aggrecan. Lastly, we determined that while all PNN components are bound to the surface in a hyaluronan-dependent manner, only HAPLN1 remains attached to the cell surface when neurons are treated with chondroitinase. These results suggest a different model for the molecular association of PNNs to the cell surface. Together our work has served to assess the contribution of aggrecan to PNN formation while providing key evidence concerning the molecular composition of PNNs in addition to determining how these components ultimately form PNNs.
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
“ChABC degrades chondroitin sulfate proteoglycans, which are a major component of the PNNs (32).”
From Perineuronal nets protect fast-spiking interneurons against oxidative stress (2013) · cites this paper as [32]
In the citing paper
“cortical primary neurons derived from aggrecan--deficient mice are abnormal in that they are not stained by the lectin Wisteria floribunda agglutinin (WFA), a broad PNN marker, indicating an essential role of aggrecan in PNN formation (Giamanco et al., 2010).”
From Casting a Wide Net: Role of Perineuronal Nets in Neural Plasticity (2016) · cites this paper as Giamanco et al., 2010
In the citing paper
“heterozygote aggrecan-deficient (ACAN+/−) mice”
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 [36]
In the citing paper
“Aggrecan is a major component of the brain ECM and of at least a subgroup of PNNs, and contains numerous CS chains with a predominant CS-6 representation.45, 46”
From Aggrecan and chondroitin-6-sulfate abnormalities in schizophrenia and bipolar disorder: a postmortem study on the amygdala (2015) · cites this paper as [45]
In the citing paper
“Reports that aggrecan knockout results in loss of WFA-positive PNNs45, 46 support this possibility.”
From Aggrecan and chondroitin-6-sulfate abnormalities in schizophrenia and bipolar disorder: a postmortem study on the amygdala (2015) · cites this paper as [45]
In the citing paper
“Together, these findings indicate that WFA may not detect CS-6 sulfation patterns, at least not those recognized by 3B3 and CS56, and may label only some forms of aggrecan (see below).45”
From Aggrecan and chondroitin-6-sulfate abnormalities in schizophrenia and bipolar disorder: a postmortem study on the amygdala (2015) · cites this paper as [45]
In the citing paper
“Notably, aggrecan is necessary for PNN formation, as shown in the HEK cell model (Kwok et al., 2010) and in organotypic cultures derived from aggrecan knockout mice (Giamanco et al., 2010).”
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 Giamanco et al., 2010
Citations
Cites
Hyaluronan: from extracellular glue to pericellular cue
Toole, B. P. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1391 · Cited by 2,125
Reactivation of Ocular Dominance Plasticity in the Adult Visual Cortex
Pizzorusso, T., Medini, P., Berardi, N., Chierzi, S., Fawcett, J. W., & Maffei, L. (2002) · Science · doi:10.1126/science.1072699 · Cited by 1,679
Camenisch, T. D., Spicer, A. P., Brehm-Gibson, T., Biesterfeldt, J., Augustine, M. L., Calabro, A., Kubalak, S., Klewer, S. E., & McDonald, J. A. (2000) · Journal of Clinical Investigation · doi:10.1172/jci10272 · Cited by 901
Organotypic slice cultures: a technique has come of age
Gähwiler, B. H. (1997) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01122-3 · Cited by 884
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
Numbers and proportions of GABA-immunoreactive neurons in different areas of monkey cerebral cortex
Hendry, S., Schwark, H. D., Jones, E. G., & Yan, J. (1987) · Journal of Neuroscience · doi:10.1523/jneurosci.07-05-01503.1987 · Cited by 601
Perineuronal nets: past and present
Celio, M. R., Spreafico, R., De Biasi, S., & Vitellaro-Zuccarello, L. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01298-3 · Cited by 497
Animals lacking link protein have attenuated perineuronal nets and persistent plasticity
Carulli, D., Pizzorusso, T., Kwok, J. C. F., Putignano, E., Poli, A., Forostyak, S., Andrews, M. R., Deepa, S. S., Glant, T. T., & Fawcett, J. W. (2010) · Brain · doi:10.1093/brain/awq145 · Cited by 495
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
Flagged first, then by citations
1 of the 77 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
The roles of perineuronal nets and the perinodal extracellular matrix in neuronal function
Fawcett, J. W., Oohashi, T., & Pizzorusso, T. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0196-3 · Cited by 589
Perineuronal nets protect fast-spiking interneurons against oxidative stress
Cabungcal, J.-H., Steullet, P., Morishita, H., Kraftsik, R., Cuenod, M., Hensch, T. K., & Do, K. Q. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1300454110 · Cited by 512
Casting a Wide Net: Role of Perineuronal Nets in Neural Plasticity
Sorg, B. A., Berretta, S., Blacktop, J. M., Fawcett, J. W., Kitagawa, H., Kwok, J. C. F., & Miquel, M. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.2351-16.2016 · Cited by 454
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
Crosstalk between glia, extracellular matrix and neurons
Song, I., & Dityatev, A. E. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.03.003 · Cited by 270
Diversity of Interneurons in the Dorsal Striatum Revealed by Single-Cell RNA Sequencing and PatchSeq
Muñoz-Manchado, A. B., Bengtsson Gonzales, C., Zeisel, A., Munguba, H., Bekkouche, B., Skene, N. G., Lönnerberg, P., Ryge, J., Harris, K. D., Linnarsson, S., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.07.053 · Cited by 229
Extracellular matrix regulation of inflammation in the healthy and injured spinal cord
Gaudet, A. D., & Popovich, P. G. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2013.11.020 · Cited by 227
Aggrecan Directs Extracellular Matrix-Mediated Neuronal Plasticity
Rowlands, D., Lensjø, K. K., Dinh, T., Yang, S., Andrews, M. R., Hafting, T., Fyhn, M., Fawcett, J. W., & Dick, G. (2018) · The Journal of Neuroscience · doi:10.1523/jneurosci.1122-18.2018 · Cited by 204
Proteoglycans and their roles in brain cancer
Wade, A., Robinson, A. E., Engler, J. R., Petritsch, C. K., James, C. D., & Phillips, J. J. (2013) · FEBS Journal · doi:10.1111/febs.12109 · Cited by 197
Cognitive-Affective Functions of the Cerebellum
Rudolph, S., Badura, A., Lutzu, S., Pathak, S. S., Thieme, A. G., Verpeut, J. L., Wagner, M. J., Yang, Y., & Fioravante, D. (2023) · Journal of Neuroscience · doi:10.1523/jneurosci.1451-23.2023 · Cited by 215
The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders
Wen, T. H., Binder, D. K., Ethell, I. M., & Razak, K. A. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00270 · Cited by 170
Suttkus, A., Rohn, S., Weigel, S., Glöckner, P., Arendt, T., & Morawski, M. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.25 · Cited by 168
Self-citationMiyata, S., & Kitagawa, H. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.06.010 · Cited by 171
The Brain’s Extracellular Matrix and Its Role in Synaptic Plasticity
Frischknecht, R., & Gundelfinger, E. D. (2012) · Advances in Experimental Medicine and Biology · doi:10.1007/978-3-7091-0932-8_7 · Cited by 156
Morawski, M., Brückner, G., Jäger, C., Seeger, G., Matthews, R. T., & Arendt, T. (2012) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00557.x · Cited by 157
Self-citationPantazopoulos, H., Markota, M., Jaquet, F., Ghosh, D., Wallin, A., Santos, A., Caterson, B., & Berretta, S. (2015) · Translational Psychiatry · doi:10.1038/tp.2014.128 · Cited by 153
Geissler, M., Gottschling, C., Aguado, A., Rauch, U., Wetzel, C. H., Hatt, H., & Faissner, A. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.3275-12.2013 · Cited by 140
Chondroitin sulfates and their binding molecules in the central nervous system
Djerbal, L., Lortat-Jacob, H., & Kwok, J. (2017) · Glycoconjugate Journal · doi:10.1007/s10719-017-9761-z · Cited by 144
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
Giamanco, K. A., & Matthews, R. T. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.05.055 · Cited by 138
Self-citationVo, T., Carulli, D., Ehlert, E., Kwok, J. C. F., Dick, G., Mecollari, V., Moloney, E. B., Neufeld, G., de Winter, F., Fawcett, J. W., et al. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.04.009 · Cited by 150
Chondroitin sulfate: A key molecule in the brain matrix
Kwok, J. C. F., Warren, P. M., & Fawcett, J. W. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.01.004 · Cited by 138
Dzyubenko, E., Gottschling, C., & Faissner, A. (2016) · Neural Plasticity · doi:10.1155/2016/5214961 · Cited by 134
Aggrecan: Beyond cartilage and into the brain
Morawski, M., Brückner, G., Arendt, T., & Matthews, R. T. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.01.010 · Cited by 136
Self-citationExtracellular matrix protein expression is brain region dependent
Dauth, S., Grevesse, T., Pantazopoulos, H., Campbell, P. H., Maoz, B. M., Berretta, S., & Parker, K. K. (2016) · The Journal of Comparative Neurology · doi:10.1002/cne.23965 · Cited by 136
Oohashi, T., Edamatsu, M., Bekku, Y., & Carulli, D. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.09.010 · Cited by 131
In Sickness and in Health: Perineuronal Nets and Synaptic Plasticity in Psychiatric Disorders
Pantazopoulos, H., & Berretta, S. (2015) · Neural Plasticity · doi:10.1155/2016/9847696 · Cited by 128
“GAG-ing with the neuron”: The role of glycosaminoglycan patterning in the central nervous system
Smith, P. D., Coulson‐Thomas, V. J., Foscarin, S., Kwok, J. C. F., & Fawcett, J. W. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.08.004 · Cited by 114
Seizure-like activity in hyaluronidase-treated dissociated hippocampal cultures
Vedunova, M., Sakharnova, T., Mitroshina, E., Perminova, M., Pimashkin, A., Zakharov, Y., Dityatev, A., & Mukhina, I. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00149 · Cited by 107
Morawski, M., Dityatev, A., Hartlage-Rübsamen, M., Blosa, M., Holzer, M., Flach, K., Pavlica, S., Dityateva, G., Grosche, J., Brückner, G., et al. (2014) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2014.0046 · Cited by 100
Self-citationProtective Properties of Neural Extracellular Matrix
Suttkus, A., Morawski, M., & Arendt, T. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8990-4 · Cited by 110
Self-citationTewari, B. P., Chaunsali, L., Prim, C. E., & Sontheimer, H. W. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1022754 · Cited by 115
Andrews, E. M., Richards, R. J., Yin, F. Q., Viapiano, M. S., & Jakeman, L. B. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.09.008 · Cited by 104
Dzyubenko, E., Rozenberg, A., Hermann, D. M., & Faissner, A. (2016) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2016.09.001 · Cited by 98
Yi, J., Katagiri, Y., Susarla, B., Figge, D., Symes, A. J., & Geller, H. M. (2012) · Journal of Comparative Neurology · doi:10.1002/cne.23156 · Cited by 93
Perineuronal nets and schizophrenia: The importance of neuronal coatings
Bitanihirwe, B. K. Y., & Woo, T.-U. W. (2014) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2014.03.018 · Cited by 95
Krishnaswamy, V. R., Benbenishty, A., Blinder, P., & Sagi, I. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03182-6 · Cited by 96
Lendvai, D., Morawski, M., Négyessy, L., Gáti, G., Jäger, C., Baksa, G., Glasz, T., Attems, J., Tanila, H., Arendt, T., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-012-1042-0 · Cited by 93
Self-citationArreola, M. A., Soni, N., Crapser, J. D., Hohsfield, L. A., Elmore, M. R. P., Matheos, D. P., Wood, M. A., Swarup, V., Mortazavi, A., & Green, K. N. (2021) · Science Advances · doi:10.1126/sciadv.abg1601 · Cited by 91
(2012) · Europe PMC (PubMed Central) · Cited by 88
Self-citationPersistent decrease in multiple components of the perineuronal net following status epilepticus
McRae, P. A., Baranov, E., Rogers, S. L., & Porter, B. E. (2012) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2012.08268.x · Cited by 85
Murase, S., Lantz, C. L., & Quinlan, E. M. (2017) · eLife · doi:10.7554/elife.27345 · Cited by 87
Molecular signature of extracellular matrix pathology in schizophrenia
Pantazopoulos, H., Katsel, P., Haroutunian, V. H., Chelini, G., Klengel, T., & Berretta, S. (2020) · European Journal of Neuroscience · doi:10.1111/ejn.15009 · Cited by 83
Madinier, A., Quattromani, M. J., Sjölund, C., Ruscher, K., & Wieloch, T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093121 · Cited by 82
Repeated Binge Drinking Increases Perineuronal Nets in the Insular Cortex
Chen, H., He, D., & Lasek, A. W. (2015) · Alcoholism: Clinical and Experimental Research · doi:10.1111/acer.12847 · Cited by 77
Extracellular matrix and biomimetic engineering microenvironment for neuronal differentiation
Yim, E. K. F., Jain, D., Mattiassi, S., & Goh, E. K. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.266907 · Cited by 76
Morikawa, S., Ikegaya, Y., Narita, M., & Tamura, H. (2017) · Scientific Reports · doi:10.1038/srep46024 · Cited by 74
Chondroitin Sulfate Is Required for Onset and Offset of Critical Period Plasticity in Visual Cortex
Hou, X., Yoshioka, N., Tsukano, H., Sakai, A., Miyata, S., Watanabe, Y., Yanagawa, Y., Sakimura, K., Takeuchi, K., Kitagawa, H., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-04007-x · Cited by 83
Miyata, S., & Kitagawa, H. (2016) · Neural Plasticity · doi:10.1155/2016/1305801 · Cited by 70
Mechanisms for modulation of neural plasticity and axon regeneration by chondroitin sulphate
Miyata, S., & Kitagawa, H. (2014) · The Journal of Biochemistry · doi:10.1093/jb/mvu067 · Cited by 73
Releasing Addiction Memories Trapped in Perineuronal Nets
Lasek, A. W., Chen, H., & Chen, W.-Y. (2018) · Trends in Genetics · doi:10.1016/j.tig.2017.12.004 · Cited by 71
Inflammation modulates expression of laminin in the central nervous system following ischemic injury
Ji, K., & Tsirka, S. E. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-159 · Cited by 71
Miyata, S., Nadanaka, S., Igarashi, M., & Kitagawa, H. (2018) · Frontiers in Integrative Neuroscience · doi:10.3389/fnint.2018.00003 · Cited by 68
Bekku, Y., Saito, M., Moser, M., Fuchigami, M., Maehara, A., Nakayama, M., Kusachi, S., Ninomiya, Y., & Oohashi, T. (2012) · Journal of Comparative Neurology · doi:10.1002/cne.23009 · Cited by 65
Drzewiecki, C. M., Willing, J., & Juraska, J. M. (2020) · Brain Structure and Function · doi:10.1007/s00429-020-02137-z · Cited by 71
The Role of Extracellular Matrix in Human Neurodegenerative Diseases
Pintér, P., & Alpár, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911085 · Cited by 68
Horii‐Hayashi, N., Sasagawa, T., Matsunaga, W., & Nishi, M. (2015) · Neural Plasticity · doi:10.1155/2015/256389 · Cited by 66
Yang, S., Hilton, S., Alves, J. N., Saksida, L. M., Bussey, T., Matthews, R. T., Kitagawa, H., Spillantini, M. G., Kwok, J. C. F., & Fawcett, J. W. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.08.002 · Cited by 61
Self-citationHyaluronic acid and neural stem cells: implications for biomaterial design
Khaing, Z. Z., & Seidlits, S. K. (2015) · Journal of Materials Chemistry B · doi:10.1039/c5tb00974j · Cited by 63
Perineuronal Net Dynamics in the Pathophysiology of Epilepsy
Chaunsali, L., Tewari, B. P., & Sontheimer, H. W. (2021) · Epiliepsy currents/Epilepsy currents · doi:10.1177/15357597211018688 · Cited by 60
Yamada, J., & Jinno, S. (2017) · Journal of Comparative Neurology · doi:10.1002/cne.24132 · Cited by 59
Blosa, M., Sonntag, M., Brückner, G., Jäger, C., Seeger, G., Matthews, R. T., Rübsamen, R., Arendt, T., & Morawski, M. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.10.003 · Cited by 60
Self-citationEffects of Ethanol on Brain Extracellular Matrix: Implications for Alcohol Use Disorder
Lasek, A. W. (2016) · Alcoholism Clinical and Experimental Research · doi:10.1111/acer.13200 · Cited by 58
Rupert, D. D., & Shea, S. D. (2022) · Frontiers in Neural Circuits · doi:10.3389/fncir.2022.886629 · Cited by 58
Diurnal changes in perineuronal nets and parvalbumin neurons in the rat medial prefrontal cortex
Harkness, J. H., Gonzalez, A. E., Bushana, P. N., Jorgensen, E. T., Hegarty, D. M., Nardo, A. A. D., Prochiantz, A., Wisor, J. P., Aicher, S. A., Brown, T. E., et al. (2021) · Brain Structure and Function · doi:10.1007/s00429-021-02229-4 · Cited by 55
Umemori, J., Winkel, F., Ċastrén, E., & Karpova, N. N. (2015) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2015.05.006 · Cited by 56
Perineuronal Nets: Subtle Structures with Large Implications
Carceller, H., Gramuntell, Y., Klimczak, P., & Nácher, J. (2022) · The Neuroscientist · doi:10.1177/10738584221106346 · Cited by 54
Suttkus, A., Holzer, M., Morawski, M., & Arendt, T. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2015.11.040 · Cited by 50
Self-citationCaught in the Net: Perineuronal Nets and Addiction
Slaker, M. L., Blacktop, J. M., & Sorg, B. A. (2016) · Neural Plasticity · doi:10.1155/2016/7538208 · Cited by 52
Hyaluronan-based extracellular matrix under conditions of homeostatic plasticity
Valenzuela, J. C., Heise, C., Franken, G., Singh, J. B., Schweitzer, B., Seidenbecher, C. I., & Frischknecht, R. (2014) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2013.0606 · Cited by 48
Irvine, S., & Kwok, J. C. F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041172 · Cited by 55
Review of Design Considerations for Brain-on-a-Chip Models
Cameron, T., Bennet, T. J., Rowe, E. M., Anwer, M., Wellington, C. L., & Cheung, K. C. (2021) · Micromachines · doi:10.3390/mi12040441 · Cited by 49
Perineuronal nets in the auditory system
Sonntag, M., Blosa, M., Schmidt, S., Rübsamen, R., & Morawski, M. (2015) · Hearing Research · doi:10.1016/j.heares.2014.12.012 · Cited by 50
Self-citationPerineuronal and perisynaptic extracellular matrix in the human spinal cord
Jäger, C., Lendvai, D., Seeger, G., Brückner, G., Matthews, R. T., Arendt, T., Alpár, A., & Morawski, M. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.02.014 · Cited by 48
Self-citationExpression of aggrecan components in perineuronal nets in the mouse cerebral cortex
Ueno, H., Fujii, K., Suemitsu, S., Murakami, S., Kitamura, N., Wani, K., Aoki, S., Okamoto, M., Ishihara, T., & Takao, K. (2018) · IBRO Reports · doi:10.1016/j.ibror.2018.01.002 · Cited by 49
Karetko-Sysa, M., Skangiel-Kramska, J., & Nowicka, D. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.05.022 · Cited by 45
Ueno, H., Suemitsu, S., Okamoto, M., Matsumoto, Y., & Ishihara, T. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.04.041 · Cited by 49
Xiao, M., Li, X., Song, Q., Zhang, Q., Lazzarino, M., Cheng, G., Severino, F. P. U., & Torre, V. (2018) · Advanced Materials · doi:10.1002/adma.201806132 · Cited by 46
Nadanaka, S., Miyata, S., Yaqiang, B., Tamura, J.-I., Habuchi, O., & Kitagawa, H. (2020) · Biomolecules · doi:10.3390/biom10111499 · Cited by 43
Extracellular matrixes and neuroinflammation
Jang, D. G., Sim, H. J., Song, E. K., Kwon, T., & Park, T. J. (2020) · BMB Reports · doi:10.5483/bmbrep.2020.53.10.156 · Cited by 45
New Insights into ADAMTS Metalloproteases in the Central Nervous System
Mohamedi, Y., Fontanil, T., Cobo, T., Cal, S., & Obaya, Á. J. (2020) · Biomolecules · doi:10.3390/biom10030403 · Cited by 39
Matrix Metalloproteinases, Neural Extracellular Matrix, and Central Nervous System Pathology
Luca, C. D., & Papa, M. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.04.002 · Cited by 39
Cortical diurnal rhythms remain intact with microglial depletion
Barahona, R. A., Morabito, S., Swarup, V., & Green, K. N. (2022) · Scientific Reports · doi:10.1038/s41598-021-04079-w · Cited by 39
Bitanihirwe, B. K. Y., Mauney, S. A., & Woo, T.-U. W. (2016) · Biological Psychiatry · doi:10.1016/j.biopsych.2016.03.1047 · Cited by 40
Neural ECM in regeneration and rehabilitation
Yang, S., Kwok, J. C. F., & Fawcett, J. W. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00008-6 · Cited by 37
Sonntag, M., Blosa, M., Schmidt, S., Reimann, K., Blum, K., Eckrich, T., Seeger, G., Hecker, D., Schick, B., Arendt, T., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0566-8 · Cited by 40
Self-citationNeurocan Contributes to Perineuronal Net Development
Schmidt, S., Arendt, T., Morawski, M., & Sonntag, M. (2020) · Neuroscience · doi:10.1016/j.neuroscience.2020.06.040 · Cited by 36
Self-citationEnzymatic Degradation of Cortical Perineuronal Nets Reverses GABAergic Interneuron Maturation
Willis, A., Pratt, J. A., & MORRIS, B. J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02772-z · Cited by 38
Bartolini, B., Thelin, M. A., Rauch, U., Feinstein, R. E., Oldberg, Å., Malmström, A., & Maccarana, M. (2012) · Glycobiology · doi:10.1093/glycob/cws065 · Cited by 37
Mueller-Buehl, C., Reinhard, J., Roll, L., Bader, V., Winklhofer, K. F., & Faissner, A. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.886527 · Cited by 37
From molecules to behavior: Implications for perineuronal net remodeling in learning and memory
Sanchez, B., Kraszewski, P., Lee, S., & Cope, E. C. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.16036 · Cited by 41
Dwyer, C. A., Katoh, T., Tiemeyer, M., & Matthews, R. T. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.614099 · Cited by 35
Self-citationWegrzyn, D., Freund, N., Faissner, A., & Juckel, G. (2021) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2021.637549 · Cited by 36
Myers, A. K., Ray, J., & Kulesza, R. J. (2012) · Brain Research · doi:10.1016/j.brainres.2012.05.024 · Cited by 34
The protein tyrosine phosphatase RPTPζ/phosphacan is critical for perineuronal net structure
Eill, G. J., Sinha, A., Morawski, M., Viapiano, M. S., & Matthews, R. T. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.010830 · Cited by 32
Self-citationThe protein tyrosine phosphatase RPTPζ/phosphacan is critical for perineuronal net structure
Eill, G. J., Sinha, A., Morawski, M., Viapiano, M. S., & Matthews, R. T. (2020) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)49907-8 · Cited by 32
Self-citationDistinct roles for hyaluronan in neural stem cell niches and perineuronal nets
Su, W., Matsumoto, S. G., Sorg, B. A., & Sherman, L. S. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.022 · Cited by 33
The Role of Perineuronal Nets in Physiology and Disease: Insights from Recent Studies
Auer, S., Schicht, M., Hoffmann, L., Budday, S., Frischknecht, R., Blümcke, I., & Paulsen, F. P. (2025) · Cells · doi:10.3390/cells14050321 · Cited by 32
Warford, J. R., Lamport, A.-C., Clements, D. R., Malone, A., Kennedy, B. E., Kim, Y., Gujar, S. A., Hoskin, D. W., & Easton, A. S. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0506-9 · Cited by 30
Metadata
- Authors
- Giamanco, K. A., Morawski, M., & Matthews, R. T.
- Affiliations
- SUNY Upstate Medical University (US)
- Leipzig University (DE)
- Venue
- Neuroscience
- Publisher
- Elsevier BV
- Published
- 2010-11
- Volume
- 170
- Issue
- 4
- Pages
- 1314-1327
- ISSN
- 0306-4522 (ISSN-L)
- OpenAlex
- W2033004840
- Cited by
- 207
- References
- 77
- Citations by year
- 2026: 3 · 2025: 15 · 2024: 13 · 2023: 15 · 2022: 15 · 2021: 14 · 2020: 15 · 2019: 9 · 2018: 17 · 2017: 16 · 2016: 15 · 2015: 14 · 2014: 12 · 2013: 11 · 2012: 17
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- green
- zenodo.org
- Licence
- Locations
- Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, other-oa)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- perineuronal nets, aggrecan, chondroitin sulfate proteoglycans, hyaluronic acid, HAPLN1, tenascin-R, brevican, Wisteria floribunda agglutinin, chondroitinase, organotypic slice cultures
- MeSH terms
- Proteoglycan Link Protein, Animals, Cells, Cultured, Chondroitin Sulfates, Extracellular Matrix, gamma-Aminobutyric Acid, Hyaluronic Acid, Interneurons, Neurons, Parvalbumins, Proteoglycans, Extracellular Matrix Proteins, Mice, Knockout, Tenascin, Mice, Aggrecans, In Vitro Techniques
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
