Association between protease-specific proteolytic cleavage of brevican and synaptic loss in the dentate gyrus of kainate-treated rats

Metalloproteinases in biology and pathology of the nervous system

Yong, W. V., Power, C., Forsyth, P., & Edwards, D. (2001) · Nature Reviews Neuroscience · doi:10.1038/35081571 · Cited by 1,094 · see citing works

Kainic acid seizures in the rat

Sperk, G. (1994) · Progress in Neurobiology · doi:10.1016/0301-0082(94)90019-1 · Cited by 688 · see citing works

Purification and Cloning of Aggrecanase-1: A Member of the ADAMTS Family of Proteins

Tortorella, M. D., Burn, T. C., Pratta, M. A., Abbaszade, I., Hollis, J. M., Liu, R., Rosenfeld, S. A., Copeland, R. A., Decicco, C. P., Wynn, R., et al. (1999) · Science · doi:10.1126/science.284.5420.1664 · Cited by 686 · see citing works

Lecticans: organizers of the brain extracellular matrix

Yamaguchi, Y. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000690 · Cited by 642 · see citing works

Matrix metalloproteinases and diseases of the CNS

Yong, V. W., Forsyth, P. A., Bell, R. B., Krekoski, C. A., & Edwards, D. R. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01169-7 · Cited by 635 · see citing works

Neuronal Death in the Hippocampus Is Promoted by Plasmin-Catalyzed Degradation of Laminin

Chen, Z.-L., & Strickland, S. (1997) · Cell · doi:10.1016/s0092-8674(00)80483-3 · Cited by 632 · see citing works

Molecular Cloning of a Gene Encoding a New Type of Metalloproteinase-disintegrin Family Protein with Thrombospondin Motifs as an Inflammation Associated Gene

Kuno, K., Kanada, N., Nakashima, E., Fujiki, F., Ichimura, F., & Matsushima, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.556 · Cited by 505 · see citing works

The Chondroitin Sulfate Proteoglycans Neurocan and Phosphacan Are Expressed by Reactive Astrocytes in the Chronic CNS Glial Scar

McKeon, R. J., Jurynec, M. J., & Buck, C. R. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-24-10778.1999 · Cited by 480 · see citing works

Perineuronal nets — a specialized form of extracellular matrix in the adult nervous system

Celio, M. R., & Blümcke, I. (1994) · Brain Research Reviews · doi:10.1016/0165-0173(94)90006-x · Cited by 386 · see citing works

Expression of Human Apolipoprotein E3 or E4 in the Brains ofApoe−/−Mice: Isoform-Specific Effects on Neurodegeneration

Buttini, M., Orth, M., Bellosta, S., Akeefe, H., Pitas, R. E., Wyss‐Coray, T., Mucke, L., & Mahley, R. W. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-12-04867.1999 · Cited by 355 · see citing works

Mechanisms involved in cartilage proteoglycan catabolism

Caterson, B., Flannery, C. R., Hughes, C., & Little, C. B. (2000) · Matrix Biology · doi:10.1016/s0945-053x(00)00078-0 · Cited by 285 · see citing works

ADAMTS‐1 cleaves a cartilage proteoglycan, aggrecan

Kuno, K., Okada, Y., Kawashima, H., Nakamura, H., Miyasaka, M., Ohno, H., & Matsushima, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01854-8 · Cited by 273 · see citing works

Expression of neural proteoglycans correlates with the acquisition of mature neuronal properties in the mammalian brain

Hockfield, S., Kalb, R. G., Zaremba, S., & Fryer, H. (1990) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1990.055.01.049 · Cited by 271 · see citing works

Differential regulation of expression of hyaluronan-binding proteoglycans in developing brain: aggrecan, versican, neurocan, and brevican.

Milev, P., Maurel, P., Chiba, A., Mevissen, M., Popp, S., Yamaguchi, Y., Margolis, R. K., & Margolis, R. U. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.8759 · Cited by 219 · see citing works

Regulation of Matrix Metalloproteinase Expression in Astrocytes, Microglia and Neurons

Gottschall, P. E., & Deb, S. (1996) · NeuroImmunoModulation · doi:10.1159/000097229 · Cited by 217 · see citing works

Brain-enriched Hyaluronan Binding (BEHAB)/Brevican Cleavage in a Glioma Cell Line Is Mediated by a Disintegrin and Metalloproteinase with Thrombospondin Motifs (ADAMTS) Family Member

Matthews, R. T., Gary, S. C., Zerillo, C. A., Pratta, M. A., Solomon, K. A., Arner, E. C., & Hockfield, S. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m909764199 · Cited by 197 · see citing works

Analysis of aggrecan in human knee cartilage and synovial fluid indicates that aggrecanase (ADAMTS) activity is responsible for the catabolic turnover and loss of whole aggrecan whereas other protease activity is required for C-terminal processing in vivo

Sandy, J. D., & Verscharen, C. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3580615 · Cited by 185 · see citing works

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 · see citing works

Expression of a Cleaved Brain-Specific Extracellular Matrix Protein Mediates Glioma Cell InvasionIn Vivo

Zhang, H., Kelly, G., Zerillo, C. A., Jaworski, D. M., & Hockfield, S. J. (1998) · Journal of Neuroscience · doi:10.1523/jneurosci.18-07-02370.1998 · Cited by 120 · see citing works

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 · see citing works

Regional and differential expression of gelatinases in rat brain after systemic kainic acid or bicuculline administration

Zhang, J. W., Deb, S., & Gottschall, P. E. (1998) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1998.00347.x · Cited by 109 · see citing works

The chondroitin sulphate proteoglycan brevican is upregulated by astrocytes after entorhinal cortex lesions in adult rats

Thon, N., Haas, C. A., Rauch, U., Merten, T., Fässler, R., Frotscher, M., & Deller, T. (2000) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2000.00109.x · Cited by 104 · see citing works

BEHAB, a new member of the proteoglycan tandem repeat family of hyaluronan-binding proteins that is restricted to the brain.

Jaworski, D. M., Kelly, G. M., & Hockfield, S. J. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.125.2.495 · Cited by 98 · see citing works

Intact Aggrecan and Fragments Generated by Both Aggrecanse and Metalloproteinase-Like Activities Are Present in the Developing and Adult Rat Spinal Cord and Their Relative Abundance Is Altered by Injury

Lemons, M. L., Sandy, J. D., Anderson, D. K., & Howland, D. R. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-13-04772.2001 · Cited by 89 · see citing works

Intracranial Injury Acutely Induces the Expression of the Secreted Isoform of the CNS-Specific Hyaluronan-Binding Protein BEHAB/Brevican

Jaworski, D. M., Kelly, G. M., & Hockfield, S. J. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7062 · Cited by 87 · see citing works

Occurrence of a N-terminal proteolytic fragment of neurocan, not a C-terminal half, in a perineuronal net in the adult rat cerebrum

Matsui, F., Nishizuka, M., Yasuda, Y., Aono, S., Watanabe, E., & Oohira, A. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00009-2 · Cited by 78 · see citing works

Transcripts for secreted and GPI‐anchored brevican are differentially distributed in rat brain

Seidenbecher, C. I., Gundelfinger, E. D., Böckers, T. M., Trotter, J., & Kreutz, M. R. (1998) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1998.00166.x · Cited by 77 · see citing works

Glial hyaluronate-binding protein: a product of metalloproteinase digestion of versican?

Perides, G., Asher, R. A., Lark, M. W., Lane, W. S., Robinson, R. A., & Bignami, A. (1995) · Biochemical Journal · doi:10.1042/bj3120377 · Cited by 74 · see citing works

Design and Synthesis of a Series of (2R)-N4-Hydroxy-2-(3-hydroxybenzyl)-N- [(1S,2R)-2-hydroxy-2,3-dihydro-1H-inden- 1-yl]butanediamide Derivatives as Potent, Selective, and Orally Bioavailable Aggrecanase Inhibitors

Yao, W., Wasserman, Z. R., Chao, M., Reddy, G. S., Shi, E., Liu, R., Covington, M. B., Arner, E. C., Pratta, M. A., Tortorella, M. D., et al. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm015533c · Cited by 64 · see citing works

Brevican in the developing hippocampal fimbria: Differential expression in myelinating oligodendrocytes and adult astrocytes suggests a dual role for brevican in central nervous system fiber tract development

Ogawa, T., Hagihara, K., Suzuki, M., & Yamaguchi, Y. (2001) · The Journal of Comparative Neurology · doi:10.1002/cne.1103 · Cited by 61 · see citing works

Potential role of synaptopodin in spine motility by coupling actin to the spine apparatus

Deller, T., Mundel, P. H., & Frotscher, M. (2000) · Hippocampus · doi:10.1002/1098-1063(2000)10:5 · Cited by 61 · see citing works

Pathways of aggrecan processing in joint tissues Implications for disease mechanism and monitoring

Sandy, J. D., Plaas, A., & Koob, T. J. (1995) · Acta Orthopaedica Scandinavica · doi:10.3109/17453679509157643 · Cited by 57 · see citing works

Topographical distribution of synaptic-associated proteins in the neuritic plaques of Alzheimer's disease hippocampus

Masliah, E., Honer, W. G., Mallory, M. E., Voigt, M., Kushner, P. D., Hansen, L. A., & Terry, R. D. (1994) · Acta Neuropathologica · doi:10.1007/bf00296182 · Cited by 56 · see citing works

ADAMTS-4 (a disintegrin and metalloproteinase with thrombospondin motifs) is transcriptionally induced in beta-amyloid treated rat astrocytes

Satoh, K., Suzuki, N., & Yokota, H. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01285-4 · Cited by 51 · see citing works

Regional and age-related expression of gelatinases in the brains of young and old rats after treatment with kainic acid

Zhang, J. W., Deb, S., & Gottschall, P. E. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01582-2 · Cited by 42 · see citing works

Carbohydrate–protein interactions between HNK‐1‐reactive sulfoglucuronyl glycolipids and the proteoglycan lectin domain mediate neuronal cell adhesion and neurite outgrowth

Miura, R., Ethell, I. M., & Yamaguchi, Y. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00042.x · Cited by 39 · see citing works

A disintegrin and metalloprotease with thrombospondin type1 motifs (ADAMTS-1) and IL-1 receptor type 1 mRNAs are simultaneously induced in nerve injured motor neurons

Sasaki, M., Kiryu‐Seo, S., Kato, R., Shin-ichi, K. I. T. A., & Kiyama, H. (2001) · Molecular Brain Research · doi:10.1016/s0169-328x(01)00046-8 · Cited by 34 · see citing works

Proteoglycan Core Proteins and Catabolic Fragments Present in Tissues and Fluids

Sandy, J. D. (2003) · Humana Press eBooks · doi:10.1385/1-59259-209-0:335 · Cited by 22 · see citing works

Untitled work

Hagihara (1999) · doi:10.1002/(sici)1096-9861(19990726)410:2

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 · see citing works

The role of chondroitin sulfate proteoglycans in regeneration and plasticity in the central nervous system

Galtrey, C. M., & Fawcett, J. W. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2006.09.006 · Cited by 575 · see citing works

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 · see citing works

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 · see citing works

Brain Extracellular Matrix in Neurodegeneration

Bonneh‐Barkay, D., & Wiley, C. A. (2008) · Brain Pathology · doi:10.1111/j.1750-3639.2008.00195.x · Cited by 303 · see citing works

Processing and Localization of ADAMTS-1 and Proteolytic Cleavage of Versican during Cumulus Matrix Expansion and Ovulation

Russell, D. L., Doyle, K. M. H., Ochsner, S. A., Sandy, J. D., & Richards, J. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300519200 · Cited by 272 · see citing works

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 263 · see citing works

Targeting the neural extracellular matrix in neurological disorders

Soleman, S., Filippov, M. A., Dityatev, A., & Fawcett, J. W. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.08.050 · Cited by 244 · see citing works

Metzincin Proteases and Their Inhibitors: Foes or Friends in Nervous System Physiology?

Rivera, S., Khrestchatisky, M., Kaczmarek, L., Rosenberg, G. A., & Jaworski, D. M. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.3467-10.2010 · Cited by 237 · see citing works

Adamts-1 Is Essential for the Development and Function of the Urogenital System1

Mittaz, L., Russell, D. L., Wilson, T., Brasted, M., Tkalcevic, J., Salamonsen, L. A., Hertzog, P. J., & Pritchard, M. A. (2004) · Biology of Reproduction · doi:10.1095/biolreprod.103.023911 · Cited by 200 · see citing works

ADAMTS4 (Aggrecanase-1) Activation on the Cell Surface Involves C-terminal Cleavage by Glycosylphosphatidyl Inositol-anchored Membrane Type 4-Matrix Metalloproteinase and Binding of the Activated Proteinase to Chondroitin Sulfate and Heparan Sulfate on Syndecan-1

Gao, G., Plaas, A., Thompson, V. P., Jin, S., Zuo, F., & Sandy, J. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312100200 · Cited by 194 · see citing works

Extracellular matrix components associated with remodeling processes in brain

Rauch, U. (2004) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s00018-004-4043-x · Cited by 205 · see citing works

Shaping Synapses by the Neural Extracellular Matrix

Ferrer-Ferrer, M., & Dityatev, A. (2018) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2018.00040 · Cited by 169 · see citing works

Vitamin D in Synaptic Plasticity, Cognitive Function, and Neuropsychiatric Illness

Mayne, P., & Burne, T. H. J. (2019) · Trends in Neurosciences · doi:10.1016/j.tins.2019.01.003 · Cited by 162 · see citing works

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 · see citing works

Coordinate Transcription of the ADAMTS-1 Gene by Luteinizing Hormone and Progesterone Receptor

Doyle, K. M. H., Russell, D. L., Sriraman, V., & Richards, J. S. (2004) · Molecular Endocrinology · doi:10.1210/me.2003-0380 · Cited by 127 · see citing works

An Extracellular Perspective on CNS Maturation: Perineuronal Nets and the Control of Plasticity

Carulli, D., & Verhaagen, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052434 · Cited by 123 · see citing works

Role of Matrix Metalloproteinases in the Pathogenesis of Traumatic Brain Injury

Muneer, P. M. A., Pfister, B. J., Haorah, J., & Chandra, N. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9520-8 · Cited by 126 · see citing works

Extracellular matrix in plasticity and epileptogenesis

Dityatev, A. E., & Fellin, T. (2008) · Neuron Glia Biology · doi:10.1017/s1740925x09000118 · Cited by 116 · see citing works

Loss of perineuronal net N-acetylgalactosamine in Alzheimer’s disease

Baig, S., Wilcock, G. K., & Love, S. (2005) · Acta Neuropathologica · doi:10.1007/s00401-005-1060-2 · Cited by 112 · see citing works

Initial loss but later excess of GABAergic synapses with dentate granule cells in a rat model of temporal lobe epilepsy

Thind, K. K., Yamawaki, R. M., Phanwar, I., Zhang, G., Wen, X., & Buckmaster, P. S. (2009) · The Journal of Comparative Neurology · doi:10.1002/cne.22235 · Cited by 111 · see citing works

Brevican: A key proteoglycan in the perisynaptic extracellular matrix of the brain

Frischknecht, R., & Seidenbecher, C. I. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.03.022 · Cited by 112 · see citing works

Matrix Metalloproteinase Inhibition Alters Functional and Structural Correlates of Deafferentation-Induced Sprouting in the Dentate Gyrus

Reeves, T. M., Prins, M. L., Zhu, J., Povlishock, J. T., & Phillips, L. L. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-32-10182.2003 · Cited by 105 · see citing works

ADAMTS4 (aggrecanase-1) cleaves human brain versican V2 at Glu405-Gln406 to generate glial hyaluronate binding protein

Westling, J., Gottschall, P. E., Thompson, V. P., Cockburn, A., Perides, G., Zimmermann, D. R., & Sandy, J. D. (2004) · Biochemical Journal · doi:10.1042/bj20030896 · Cited by 104 · see citing works

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 101 · see citing works

ADAMTS expression and function in central nervous system injury and disorders

Gottschall, P. E., & Howell, M. D. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.014 · Cited by 100 · see citing works

ADAMTS proteoglycanases in the physiological and pathological central nervous system.

Lemarchant, S., Pruvost, M., Montaner, J., Emery, E., Vivien, D., Kanninen, K., & Koistinaho, J. (2013) · Journal of Neuroinflammation · doi:10.1186/1742-2094-10-133 · Cited by 96 · see citing works

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 · see citing works

Demystifying the extracellular matrix and its proteolytic remodeling in the brain: structural and functional insights

Krishnaswamy, V. R., Benbenishty, A., Blinder, P., & Sagi, I. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03182-6 · Cited by 92 · see citing works

The endogenous proteoglycan-degrading enzyme ADAMTS-4 promotes functional recovery after spinal cord injury

Tauchi, R., Imagama, S., Natori, T., Ohgomori, T., Muramoto, A., Shinjo, R., Matsuyama, Y., Ishiguro, N., & Kadomatsu, K. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-53 · Cited by 91 · see citing works

Proteolytic Remodeling of Perineuronal Nets: Effects on Synaptic Plasticity and Neuronal Population Dynamics

Bozzelli, P. L., Alaiyed, S., Kim, E., Villapol, S., & Conant, K. E. (2018) · Neural Plasticity · doi:10.1155/2018/5735789 · Cited by 90 · see citing works

Regulated Proteolytic Processing of Reelin through Interplay of Tissue Plasminogen Activator (tPA), ADAMTS-4, ADAMTS-5, and Their Modulators

Krstic, D., Rodríguez, M. E., & Knuesel, I. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047793 · Cited by 92 · see citing works

Persistent 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 · see citing works

MMPs and ADAMTSs: functional studies

Carl, R. F. (2006) · Frontiers in bioscience · doi:10.2741/1818 · Cited by 85 · see citing works

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 79 · see citing works

Matrix metalloproteinase‐3 expression profile differentiates adaptive and maladaptive synaptic plasticity induced by traumatic brain injury

Falo, M. C., Fillmore, H. L., Reeves, T. M., & Phillips, L. L. (2006) · Journal of Neuroscience Research · doi:10.1002/jnr.20986 · Cited by 83 · see citing works

T he extracellular matrix: F ocus on oligodendrocyte biology and targeting CSPG s for remyelination therapies

Pu, A., Stephenson, E. L., & Yong, V. W. (2018) · Glia · doi:10.1002/glia.23333 · Cited by 77 · see citing works

Neural ECM proteases in learning and synaptic plasticity

Tsilibary, E. C., Tzinia, A. K., Radenović, L., Stamenković, V., Lebitko, T., Mucha, M. W., Pawlak, R., Frischknecht, R., & Kaczmarek, L. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00006-2 · Cited by 74 · see citing works

ADAMTS1 Proteinase Is Up-regulated in Wounded Skin and Regulates Migration of Fibroblasts and Endothelial Cells

Krampert, M., Kuenzle, S., Thai, S. N.-M., Lee, N., Iruela‐Arispe, M. L., & Werner, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412212200 · Cited by 76 · see citing works

Metalloproteinase inhibition prevents inhibitory synapse reorganization and seizure genesis

Pollock, E., Everest, M., Brown, A., & Poulter, M. O. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.06.003 · Cited by 75 · see citing works

Lectican proteoglycans, their cleaving metalloproteinases, and plasticity in the central nervous system extracellular microenvironment

Howell, M. D., & Gottschall, P. E. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.05.034 · Cited by 66 · see citing works

Matrix metalloproteinases and proteoglycans in axonal regeneration

Pizzi, M. A., & Crowe, M. J. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.12.012 · Cited by 68 · see citing works

Matrix metalloproteinases and ADAMs in stroke

Montaner, J., Ramiro, L., Simats, A., Hernández‐Guillamón, M., Delgado, P., Bustamante, A., & Rosell, A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03175-5 · Cited by 66 · see citing works

Increased metalloproteinase activity in the hippocampus following status epilepticus

Dubey, D., McRae, P. A., Rankin-Gee, E. K., Baranov, E., Wandrey, L., Rogers, S., & Porter, B. E. (2017) · Epilepsy Research · doi:10.1016/j.eplepsyres.2017.02.021 · Cited by 65 · see citing works

MT5-MMP, ADAM-10, and N-Cadherin Act in Concert To Facilitate Synapse Reorganization after Traumatic Brain Injury

Harrell, K. M., Reeves, T. M., & Phillips, L. L. (2012) · Journal of Neurotrauma · doi:10.1089/neu.2012.2383 · Cited by 65 · see citing works

Metalloproteinase ADAMTS-1 but not ADAMTS-5 is manifold overexpressed in neurodegenerative disorders as Down syndrome, Alzheimer's and Pick's disease

Miguel, R. F., Pollak, A., & Lubec, G. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.09.008 · Cited by 64 · see citing works

Multimodal signaling by the ADAMTSs (a disintegrin and metalloproteinase with thrombospondin motifs) promotes neurite extension

Hamel, M. G., Ajmo, J. M., Leonardo, C. C., Zuo, F., Sandy, J. D., & Gottschall, P. E. (2007) · Experimental Neurology · doi:10.1016/j.expneurol.2007.11.014 · Cited by 60 · see citing works

Evidence for proteolytic cleavage of brevican by the ADAMTSs in the dentate gyrus after excitotoxic lesion of the mouse entorhinal cortex

Mayer, J., Hamel, M. G., & Gottschall, P. E. (2005) · BMC Neuroscience · doi:10.1186/1471-2202-6-52 · Cited by 57 · see citing works

Perineuronal net degradation rescues CA2 plasticity in a mouse model of Rett syndrome

Carstens, K. E., Lustberg, D. J., Shaughnessy, E. K., McCann, K. E., Alexander, G. M., & Dudek, S. M. (2021) · Journal of Clinical Investigation · doi:10.1172/jci137221 · Cited by 57 · see citing works

A disintegrin and metalloproteinase with thrombospondin motifs 4 (ADAMTS‐4) cleaves Reelin in an isoform‐dependent manner

Hisanaga, A., Morishita, S., Suzuki, K. M., Sasaki, K., Koie, M., Kohno, T., & Hattori, M. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.07.017 · Cited by 56 · see citing works

Altered production and proteolytic processing of brevican by transforming growth factor β in cultured astrocytes

Hamel, M. G., Mayer, J., & Gottschall, P. E. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03144.x · Cited by 55 · see citing works

Neural ECM molecules in axonal and synaptic homeostatic plasticity

Frischknecht, R., Chang, K.-J., Rasband, M. N., & Seidenbecher, C. I. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00004-9 · Cited by 53 · see citing works

Discordant localization of WFA reactivity and brevican/ADAMTS-derived fragment in rodent brain

Ajmo, J. M., Eakin, A. K., Hamel, M. G., & Gottschall, P. E. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-14 · Cited by 53 · see citing works

Proteolysis: a key post-translational modification regulating proteoglycans

Mead, T. J., Bhutada, S., Martin, D. R., & Apte, S. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00215.2022 · Cited by 49 · see citing works

ADAMTSL3 as a candidate gene for schizophrenia: gene sequencing and ultra-high density association analysis by imputation

Dow, D. J., Huxley-Jones, J., Hall, J. M., Francks, C., Maycox, P. R., Kew, J. N. C., Gloger, I. S., Mehta, N. A. L., Kelly, F. M., Muglia, P., et al. (2011) · Schizophrenia Research · doi:10.1016/j.schres.2010.12.009 · Cited by 48 · see citing works

A potential role for glia‐derived extracellular matrix remodeling in postinjury epilepsy

Kim, S. Y., Porter, B. E., Friedman, A., & Kaufer, D. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23758 · Cited by 47 · see citing works

Dopamine Receptor Activation Modulates the Integrity of the Perisynaptic Extracellular Matrix at Excitatory Synapses

Mitlöhner, J., Kaushik, R., Niekisch, H., Blondiaux, A., Gee, C. E., Happel, M. F. K., Gundelfinger, E., Dityatev, A., Frischknecht, R., & Seidenbecher, C. (2020) · Cells · doi:10.3390/cells9020260 · Cited by 47 · see citing works

CD44 adhesion molecule and neuro-glial proteoglycan NG2 as invasive markers of glioma

Wiranowska, M., Ladd, S., Smith, S., & Gottschall, P. E. (2007) · Journal of Neurocytology · doi:10.1007/s11068-007-9009-0 · Cited by 47 · see citing works

Expression of ADAMTS-1, -4, -5 and TIMP-3 in normal and multiple sclerosis CNS white matter

Haddock, G., Cross, A. K., Plumb, J., Surr, J., Buttle, D. J., Bunning, R. A. D., & Woodroofe, M. N. (2006) · Multiple Sclerosis Journal · doi:10.1191/135248506ms1300oa · Cited by 45 · see citing works

Anti‐inflammatory effects of ADAMTS‐4 in a mouse model of ischemic stroke

Lemarchant, S., Dhungana, H., Pomeshchik, Y., Leinonen, H., Kołosowska, N., Korhonen, P., Kanninen, K. M., García‐Berrocoso, T., Montaner, J., Malm, T., et al. (2016) · Glia · doi:10.1002/glia.23017 · Cited by 45 · see citing works

Nitric Oxide and Synaptic Dynamics in the Adult Brain: Physiopathological Aspects

Moreno‐López, B., & Gonzáylez-Forero, D. (2006) · Reviews in the Neurosciences · doi:10.1515/revneuro.2006.17.3.309 · Cited by 45 · see citing works

Glycosaminoglycans and Glycomimetics in the Central Nervous System

Rowlands, D., Sugahara, K., & Kwok, J. C. F. (2015) · Molecules · doi:10.3390/molecules20033527 · Cited by 43 · see citing works

Abnormal post‐translational and extracellular processing of brevican in plaque‐bearing mice over‐expressing APPsw

Ajmo, J. M., Bailey, L. A., Howell, M. D., Cortez, L. K., Pennypacker, K. R., Mehta, H. N., Morgan, D., Gordon, M. N., & Gottschall, P. E. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06647.x · Cited by 41 · see citing works

Astrocyte-selective AAV-ADAMTS4 gene therapy combined with hindlimb rehabilitation promotes functional recovery after spinal cord injury

Griffin, J. M., Fackelmeier, B., Clemett, C. A., Fong, D. M., Mouravlev, A., Young, D., & O’Carroll, S. J. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113232 · Cited by 40 · see citing works

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 · see citing works

ADAMTS4 and ADAMTS5 Knockout Mice Are Protected from Versican but Not Aggrecan or Brevican Proteolysis during Spinal Cord Injury

Demircan, K., Topçu, V., Takigawa, T., Akyol, S., Yonezawa, T., Öztürk, G., Uğurcu, V., Hasgül, R., Yiǧitoǧlu, M. R., Akyol, Ö., et al. (2014) · BioMed Research International · doi:10.1155/2014/693746 · Cited by 39 · see citing works

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 · see citing works

Cell‐specific and developmental expression of lectican‐cleaving proteases in mouse hippocampus and neocortex

Levy, C., Brooks, J. M., Chen, J., Su, J., & Fox, M. A. (2014) · The Journal of Comparative Neurology · doi:10.1002/cne.23701 · Cited by 38 · see citing works

Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer’s disease

Gurses, M. S., Ural, M. N., Gulec, M. A., Akyol, O., & Akyol, S. (2016) · Aging and disease · doi:10.14336/ad.2016.0111 · Cited by 35 · see citing works

Loss of Perineuronal Net in ME7 Prion Disease

Franklin, S. L., Love, S., Greene, J. R. T., & Betmouni, S. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e3181654386 · Cited by 33 · see citing works

Differential expression of ADAMTS-1, -4, -5 and TIMP-3 in rat spinal cord at different stages of acute experimental autoimmune encephalomyelitis

Cross, A. K., Haddock, G., Surr, J., Plumb, J., Bunning, R. A. D., Buttle, D. J., & Woodroofe, M. N. (2005) · Journal of Autoimmunity · doi:10.1016/j.jaut.2005.09.026 · Cited by 31 · see citing works

Destruction of extracellular matrix proteoglycans is pervasive in simian retroviral neuroinfection

Medina‐Flores, R., Wang, G., Bissel, S. J., Murphey‐Corb, M., & Wiley, C. A. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.04.011 · Cited by 31 · see citing works

The effect of hypoxic–ischemic brain injury in perinatal rats on the abundance and proteolysis of brevican and NG2

Aya-ay, J., Mayer, J., Eakin, A. K., Muffly, B. G., Anello, M., Sandy, J. D., & Gottschall, P. E. (2005) · Experimental Neurology · doi:10.1016/j.expneurol.2004.11.021 · Cited by 29 · see citing works

ADAMTS18 Deficiency Affects Neuronal Morphogenesis and Reduces the Levels of Depression-like Behaviors in Mice

Zhu, R., Pan, Y.-H., Sun, L., Zhang, T., Wang, C., Ye, S., Yang, N., Lu, T., Wısnıewskı, T., Dang, S., et al. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.12.025 · Cited by 28 · see citing works

The quantification of ADAMTS expression in an animal model of cerebral ischemia using real‐time PCR

Tian, Y. F., Zhang, P. B., Xiao, X., Zhang, J., Zhao, J., Kang, Q., Chen, X. L., Qiu, F., & Liu, Y. (2006) · Acta Anaesthesiologica Scandinavica · doi:10.1111/j.1399-6576.2006.01161.x · Cited by 28 · see citing works

Sugar glues for broken neurons

Swarup, V. P., Mencio, C. P., Hlady, V., & Kuberan, B. (2013) · BioMolecular Concepts · doi:10.1515/bmc-2012-0042 · Cited by 26 · see citing works

Linking epileptic phenotypes and neural extracellular matrix remodeling signatures in mouse models of epilepsy

Blondiaux, A., Jia, S., Annamneedi, A., Çalışkan, G., Nebel, J., Montenegro‐Venegas, C., Wykes, R. C., Fejtová, A., Walker, M. C., Stork, O., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106324 · Cited by 26 · see citing works

Reorganization of Synaptic Connections and Perineuronal Nets in the Deep Cerebellar Nuclei of Purkinje Cell Degeneration Mutant Mice

Blosa, M., Bursch, C., Weigel, S., Holzer, M., Jäger, C., Janke, C., Matthews, R. T., Arendt, T., & Morawski, M. (2015) · Neural Plasticity · doi:10.1155/2016/2828536 · Cited by 25 · see citing works

ADAMTS‐4 in oligodendrocytes contributes to myelination with an impact on motor function

Pruvost, M., Lépine, M., Leonetti, C., Etard, O., Naveau, M., Agin, V., Docagne, F., Maubert, E., Ali, C., Emery, É., et al. (2017) · Glia · doi:10.1002/glia.23207 · Cited by 22 · see citing works

Selective Decline of Synaptic Protein Levels in the Frontal Cortex of Female Mice Deficient in the Extracellular Metalloproteinase ADAMTS1

Howell, M. D., Torres‐Collado, A. X., Iruela‐Arispe, M. L., & Gottschall, P. E. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047226 · Cited by 21 · see citing works

Multifaceted Roles of Metzincins in CNS Physiology and Pathology: From Synaptic Plasticity and Cognition to Neurodegenerative Disorders

Brzdąk, P., Nowak, D., Wiera, G., & Mozrzymas, J. W. (2017) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2017.00178 · Cited by 21 · see citing works

The CNS-specific proteoglycan, brevican, and its ADAMTS4-cleaved fragment show differential serological levels in Alzheimer’s disease, other types of dementia and non-demented controls: A cross-sectional study

Jonesco, D. S., Karsdal, M. A., & Henriksen, K. (2020) · PLoS ONE · doi:10.1371/journal.pone.0234632 · Cited by 18 · see citing works

ADAMTS‐4 in central nervous system pathologies

Lemarchant, S., Wojciechowski, S., Vivien, D., & Koıstınaho, J. (2017) · Journal of Neuroscience Research · doi:10.1002/jnr.24021 · Cited by 16 · see citing works

Brevican and phosphacan expression and localization following transient middle cerebral artery occlusion in the rat

Haddock, G., Cross, A. K., Allan, S. M., Sharrack, B., Callaghan, J., Bunning, R. A. D., Buttle, D. J., & Woodroofe, M. N. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350692 · Cited by 16 · see citing works

Interactions between astrocytes and extracellular matrix structures contribute to neuroinflammation-associated epilepsy pathology

Woo, A. M., & Sontheimer, H. W. (2023) · Frontiers in Molecular Medicine · doi:10.3389/fmmed.2023.1198021 · Cited by 15 · see citing works

Molecular analyses and identification of promising candidate genes for loci on mouse chromosome 1 affecting alcohol physical dependence and associated withdrawal

Denmark, D. L., & Buck, K. J. (2008) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2008.00396.x · Cited by 15 · see citing works

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 14 · see citing works

Sleep and Memory Consolidation Dysfunction in Psychiatric Disorders: Evidence for the Involvement of Extracellular Matrix Molecules

Gisabella, B., Babu, J., Valeri, J., Rexrode, L., & Pantazopoulos, H. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.646678 · Cited by 13 · see citing works

Polymorphisms in the ASMT and ADAMTS1 gene may increase litter size in goats

Hu, W., Tang, J., Zhang, Z., Tang, Q., Yan, Y., Wang, P., Wang, X., Liu, Q., Guo, X., Jin, M., et al. (2020) · Veterinary Medicine and Science · doi:10.1002/vms3.301 · Cited by 12 · see citing works

Altered Synaptic Marker Abundance in the Hippocampal Stratum Oriens of Ts65Dn Mice is Associated with Exuberant Expression of Versican

Howell, M. D., & Gottschall, P. E. (2012) · ASN NEURO · doi:10.1042/an20110037 · Cited by 11 · see citing works

Modulation of stress-, pain-, and alcohol-related behaviors by perineuronal nets

Aguilar, J. S., & Lasek, A. W. (2024) · Neurobiology of Stress · doi:10.1016/j.ynstr.2024.100692 · Cited by 10 · see citing works

Diverse Functions of a Disintegrin and Metalloproteinase with Thrombospondin Motif-1

Hirohata, S., Inagaki, J., & Ohtsuki, T. (2017) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.16-00236-4 · Cited by 10 · see citing works

Molecular mechanisms mediating involvement of glial cells in brain plastic remodeling in epilepsy

Хаспеков, Л. Г., & Frumkina, L. E. (2017) · Biochemistry (Moscow) · doi:10.1134/s0006297917030178 · Cited by 10 · see citing works

Matrix Metalloproteinases, Synaptic Injury, and Multiple Sclerosis

Szklarczyk, A., & Conant, K. E. (2010) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2010.00130 · Cited by 9 · see citing works

Methods in studying ECM degradation

Everts, V. E., & Buttle, D. J. (2008) · Methods · doi:10.1016/j.ymeth.2008.01.009 · Cited by 8 · see citing works

Perineuronal Nets: From Structure to Neurological Disorders

Li, X., Li, N., Zhao, P., Ren, D., Luo, B., & Zhou, T. G. (2023) · Current Medicinal Chemistry · doi:10.2174/0109298673258290231009111633 · Cited by 6 · see citing works

Meprin β Modulates Brevican Proteolysis Impairing Neural Plasticity and Memory Formation

Keller, M., Gallagher, C., Kreiselmaier, S., Bickenbach, K., Schmitt, U., Marengo, L., Taghikhah, D., Abukhalaf, M., Tholey, A., Becker‐Pauly, C., et al. (2025) · The FASEB Journal · doi:10.1096/fj.202500017r · Cited by 2 · see citing works

Dopamine modulates the integrity of the perisynaptic extracellular matrix at excitatory synapsesPreprint

Mitlöhner, J., Kaushik, R., Niekisch, H., Blondiaux, A., Gee, C. E., Happel, M. F. K., Gundelfinger, E. D., Dityatev, A. E., Frischknecht, R., & Seidenbecher, C. I. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/722454 · Cited by 2 · see citing works

Neural Extracellular Matrix Remodeling Signatures in Genetic and Acquired Mouse Models of EpilepsyPreprint

Blondiaux, A., Jia, S., Annamneedi, A., Çalışkan, G., Schulze, J., Montenegro‐Venegas, C., Wykes, R. C., Fejtová, A., Walker, M. C., Stork, O., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.04.19.537468 · Cited by 2 · see citing works

MMPs and Other Matrix-Degrading Metalloproteinases in Neurological Disease

Gottschall, P. E., & Conant, K. E. (2007) · Springer eBooks · doi:10.1007/978-0-387-30379-6_19 · Cited by 1 · see citing works

Evidence for proteolytic cleavage of brevican by the ADAMTSs in the dentate gyrus after excitotoxic lesion of the mouse entorhinal cortex

Mayer, J., Hamel, M. G., & Gottschall, P. E. (2005) · BMC Neuroscience · doi:10.1186/1471-2202-6-52 · Cited by 57 · see citing works

BMC Neuroscience BioMed Central

Mayer, J., Hamel, M. G., & Gottschall, P. E. (2005)

Elevated Cathepsin D Expression in Kainate-Evoked Rat Brain Neurodegeneration

Hetman, M., Filipkowski, R. K., Domagała, W., & Kaczmarek, L. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1083 · Cited by 45 · see citing works

ADAM9, ADAM10, and ADAM15 mRNA levels in the rat brain after kainic acid-induced status epilepticus

Ortiz, R. M., Kärkkäinen, I., Huovila, A. J., & Honkaniemi, J. (2005) · Molecular Brain Research · doi:10.1016/j.molbrainres.2005.03.008 · Cited by 18 · see citing works

Cell‐specific and developmental expression of lectican‐cleaving proteases in mouse hippocampus and neocortex

Levy, C., Brooks, J. M., Chen, J., Su, J., & Fox, M. A. (2014) · The Journal of Comparative Neurology · doi:10.1002/cne.23701 · Cited by 38 · see citing works