The DOI matches its Crossref record; 144 of the 145 references it cites were found in a registry or an index.
A delicate balance: role of MMP-9 in brain development and pathophysiology of neurodevelopmental disorders.
Open accessAbstract
The extracellular matrix (ECM) is a critical regulator of neural network development and plasticity. As neuronal circuits develop, the ECM stabilizes synaptic contacts, while its cleavage has both permissive and active roles in the regulation of plasticity. Matrix metalloproteinase 9 (MMP-9) is a member of a large family of zinc-dependent endopeptidases that can cleave ECM and several cell surface receptors allowing for synaptic and circuit level reorganization. It is becoming increasingly clear that the regulated activity of MMP-9 is critical for central nervous system (CNS) development. In particular, MMP-9 has a role in the development of sensory circuits during early postnatal periods, called 'critical periods.' MMP-9 can regulate sensory-mediated, local circuit reorganization through its ability to control synaptogenesis, axonal pathfinding and myelination. Although activity-dependent activation of MMP-9 at specific synapses plays an important role in multiple plasticity mechanisms throughout the CNS, misregulated activation of the enzyme is implicated in a number of neurodegenerative disorders, including traumatic brain injury, multiple sclerosis, and Alzheimer's disease. Growing evidence also suggests a role for MMP-9 in the pathophysiology of neurodevelopmental disorders including Fragile X Syndrome. This review outlines the various actions of MMP-9 during postnatal brain development, critical for future studies exploring novel therapeutic strategies for neurodevelopmental disorders.
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
“MMP-9 is a zinc-dependent endopeptidase expressed in various cells within the CNS which is capable of cleaving ECM proteins, including collagen and laminin (reviewed in Reinhard et al., 2015).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Reinhard et al., 2015
In the citing paper
“Peak MMP-9 expression is observed during postnatal development and is reduced during adulthood (Bednarek et al., 2009; Reinhard et al., 2015; Wen et al., 2017).”
From The Perineuronal ‘Safety’ Net? Perineuronal Net Abnormalities in Neurological Disorders (2018) · cites this paper as Reinhard et al., 2015
In the citing paper
“Although MMP-9 is involved in sensory system development (reviewed in Reinhard et al., 2015), we found that auditory ERP N1 amplitude and habituation are mostly unaffected by the removal of MMP-9 (Mmp9 KO mice).”
From Matrix metalloproteinase-9 deletion rescues auditory evoked potential habituation deficit in a mouse model of Fragile X Syndrome (2016) · cites this paper as Reinhard et al., 2015
In the citing paper
“In addition, we found a significant reduction in PV expression and PV/PNN colocalization in MMP-9 -/mice (not shown), which is consistent with MMP-9 role in neurodevelopment (reviewed in Reinhard et al. 2015), suggesting that too much or too little MMP-9 would affect PV cell development.”
From Genetic Reduction of Matrix Metalloproteinase-9 Promotes Formation of Perineuronal Nets Around Parvalbumin-Expressing Interneurons and Normalizes Auditory Cortex Responses in Developing Fmr1 Knock-Out Mice (2018) · cites this paper as Reinhard et al. 2015
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
RGD AND OTHER RECOGNITION SEQUENCES FOR INTEGRINS
Ruoslahti, E. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.697 · Cited by 3,191
Cellular Scaling Rules for the Brains of Marsupials: Not as “Primitive” as Expected
Santos, S. E. D., Porfírio, J., Cunha, F., Manger, P. R., Tavares, W. C., Pessôa, L. M., Raghanti, M. A., Sherwood, C. C., & Herculano‐Houzel, S. (2017) · Brain Behavior and Evolution · doi:10.1159/000452856 · Cited by 2,652
Chondroitinase ABC promotes functional recovery after spinal cord injury
Bradbury, E. J., Moon, L. D. F., Popat, R. J., King, V. R., Bennett, G. S., Patel, P. N., Fawcett, J. W., & McMahon, S. B. (2002) · Nature · doi:10.1038/416636a · Cited by 2,357
Azevedo, F. A. C., Carvalho, L. R. B., Grinberg, L. T., Farfel, J. M., Ferretti, R. E. L., Leite, R. E. P., Filho, W. J., Lent, R., & Herculano‐Houzel, S. (2009) · Journal of Comparative Neurology · doi:10.1002/cne.21974 · Cited by 2,337
Critical period plasticity in local cortical circuits
Hensch, T. K. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1787 · Cited by 2,323
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
MMP-9 Supplied by Bone Marrow–Derived Cells Contributes to Skin Carcinogenesis
Coussens, L. M., Tinkle, C. L., Hanahan, D., & Werb, Z. (2000) · Cell · doi:10.1016/s0092-8674(00)00139-2 · Cited by 1,306
Hensch, T. K. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.27.070203.144327 · Cited by 1,300
Altman, J. (1972) · Journal of Comparative Neurology · doi:10.1002/cne.901450402 · Cited by 996
Biochemistry and Molecular Biology of Gelatinase B or Matrix Metalloproteinase-9 (MMP-9)
den Steen, P. E. V., Dubois, B., Nelissen, I., Rudd, P., Dwek, R., & Opdenakker, G. (2002) · Critical reviews in biochemistry and molecular biology · doi:10.1080/10409230290771546 · Cited by 948
Flagged first, then by citations
1 of the 145 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Uhm, 1998, Oligodendrocytes utilize a matrix metalloproteinase, MMP-9, to extend processes along an astrocyte extracellular matrix., Glia, 22, 53, 10.1002/(SICI)1098-1136(199801)22:153::AID-GLIA53.0.CO;2-9 · DOI
Cited by
Sorted by citations
Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances
Huang, H. (2018) · Sensors · doi:10.3390/s18103249 · Cited by 769
Resveratrol regulates neuro-inflammation and induces adaptive immunity in Alzheimer’s disease
Moussa, C., Hebron, M. L., Huang, X., Ahn, J., Rissman, R. A., Aisen, P. S. S., & Turner, R. S. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-016-0779-0 · Cited by 712
Neuronal regulation of the blood–brain barrier and neurovascular coupling
Kaplan, L., Chow, B. W., & Gu, C. (2020) · Nature reviews. Neuroscience · doi:10.1038/s41583-020-0322-2 · Cited by 455
MMP ‐9 in translation: from molecule to brain physiology, pathology, and therapy
Vafadari, B., Salamian, A., & Kaczmarek, L. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13415 · Cited by 393
Perineuronal Nets: Plasticity, Protection, and Therapeutic Potential
Reichelt, A. C., Hare, D. J., Bussey, T. J., & Saksida, L. M. (2019) · Trends in Neurosciences · doi:10.1016/j.tins.2019.04.003 · Cited by 219
Plasticity of Spine Structure: Local Signaling, Translation and Cytoskeletal Reorganization
Nakahata, Y., & Yasuda, R. (2018) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2018.00029 · Cited by 209
MMPs in learning and memory and neuropsychiatric disorders
Beroun, A., Mitra, S., Michaluk, P., Pijet, B., Stefaniuk, M., & Kaczmarek, L. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03180-8 · Cited by 207
Oxidative Stress-Mediated Blood-Brain Barrier (BBB) Disruption in Neurological Diseases
Song, K., Li, Y., Zhang, H., An, N., Wei, Y., Wang, L., Tian, C., Yuan, M., Sun, Y., Xing, Y., et al. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/4356386 · Cited by 208
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
Self-citationWen, T. H., Afroz, S., Reinhard, S. M., Palacios, A. R., Tapia, K., Binder, D. K., Razak, K. A., & Ethell, I. M. (2018) · Cerebral Cortex · doi:10.1093/cercor/bhx258 · Cited by 165
Self-citationShaping Synapses by the Neural Extracellular Matrix
Ferrer-Ferrer, M., & Dityatev, A. (2018) · Frontiers in Neuroanatomy · doi:10.3389/fnana.2018.00040 · Cited by 169
Venturino, A., Schulz, R., De Jesús-Cortés, H., Maes, M. E., Nagy, B., Reilly-Andújar, F., Colombo, G., Cubero, R. J. A., Schoot Uiterkamp, F. E., Bear, M. F., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109313 · Cited by 140
Greiss Hess, L., Fitzpatrick, S. E., Nguyen, D. V., Chen, Y., Gaul, K. N., Schneider, A., Lemons Chitwood, K., Eldeeb, M. A. A. A., Polussa, J., Hessl, D., et al. (2016) · Journal of Developmental & Behavioral Pediatrics · doi:10.1097/dbp.0000000000000334 · Cited by 122
Lovelace, J. W., Wen, T. H., Reinhard, S., Hsu, M. S., Sidhu, H., Ethell, I. M., Binder, D. K., & Razak, K. A. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.02.002 · Cited by 115
Self-citationNovel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment
Rashid, Z. A., & Bardaweel, S. K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512133 · Cited by 119
Banerjee, A., Ifrim, M. F., Valdez‐Sinon, A. N., Raj, N., & Bassell, G. J. (2018) · Brain Research · doi:10.1016/j.brainres.2018.04.008 · Cited by 111
The Degradome database: expanding roles of mammalian proteases in life and disease
Pérez-Silva, J. G., Español, Y., Velasco, G., & Quesada, V. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1201 · Cited by 97
Gene expression profiling reveals a conserved microglia signature in larval zebrafish
Mazzolini, J., Clerc, S. L., Morisse, G., Coulonges, C., Kuil, L. E., van Ham, T. J., Zagury, J., & Sieger, D. (2019) · Glia · doi:10.1002/glia.23717 · Cited by 94
Vahsen, B. F., Nalluru, S., Morgan, G. R., Farrimond, L. E., Carroll, E., Xu, Y., Cramb, K. M. L., Amein, B., Scaber, J., Katsikoudi, A., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41603-0 · Cited by 83
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
Campanari, M.-L., García-Ayllón, M.-S., Ciura, S., Sáez-Valero, J., & Kabashi, E. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00160 · Cited by 69
Role of MMP-9 in epithelial-mesenchymal transition of thyroid cancer
Li, Y., He, J., Wang, F., Wang, X., Yang, F., Zhao, C., Feng, C., & Li, T. (2020) · World Journal of Surgical Oncology · doi:10.1186/s12957-020-01958-w · Cited by 67
MMPs and ADAMs in neurological infectious diseases and multiple sclerosis
Muri, L., Leppert, D., Grandgirard, D., & Leib, S. L. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03174-6 · Cited by 64
Research progress of mechanisms for tight junction damage on blood–brain barrier inflammation
Zhao, B., Yin, Q., Fei, Y., Zhu, J., Qiu, Y.-Y., Fang, W., & Li, Y. (2020) · Archives of Physiology and Biochemistry · doi:10.1080/13813455.2020.1784952 · Cited by 68
Koskinen, M.-K., van Mourik, Y., Smit, A. B., Riga, D., & Spijker, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-73173-2 · Cited by 64
Age-Related Deterioration of Perineuronal Nets in the Primary Auditory Cortex of Mice
Brewton, D. H., Kokash, J., Jimenez, O., Pena, E. R., & Razak, K. A. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00270 · Cited by 54
Self-citationBlast-induced temporal alterations in blood–brain barrier properties in a rodent model
Kawoos, U., Abutarboush, R., Gu, M., Chen, Y., Statz, J. K., Goodrich, S. Y., & Ahlers, S. T. (2021) · Scientific Reports · doi:10.1038/s41598-021-84730-8 · Cited by 58
Incubation of depression: ECM assembly and parvalbumin interneurons after stress
Spijker, S., Koskinen, M.-K., & Riga, D. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.07.015 · Cited by 55
Long, K. R., & Huttner, W. Β. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.804649 · Cited by 58
Matrix metalloproteinases in the CNS: interferons get nervous
Chopra, S., Overall, C. M., & Dufour, A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03171-9 · Cited by 56
Jorgačevski, J., Zorec, R., & Potokar, M. (2020) · Cells · doi:10.3390/cells9122622 · Cited by 54
Do, P. T., Wu, C.-C., Chiang, Y. H., Hu, C., & Chen, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221810045 · Cited by 56
Ahluwalia, M., Kumar, M., Ahluwalia, P. K., Rahimi, S. Y., Vender, J. R., Raju, R. P., Hess, D. C., Baban, B., Vale, F. Ĺ., Dhandapani, K. M., et al. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105192 · Cited by 55
Matrix Metalloproteinase-9 as an Important Contributor to the Pathophysiology of Depression
Li, H., Sheng, Z., Khan, S., Zhang, R., Liu, Y., Zhang, Y., Yong, V. W., & Xue, M. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.861843 · Cited by 58
Neural Correlates of Auditory Hypersensitivity in Fragile X Syndrome
Razak, K. A., Binder, D. K., & Ethell, I. M. (2021) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2021.720752 · Cited by 55
Self-citationAutism‐related behaviors in the cyclooxygenase‐2‐deficient mouse model
Wong, C. T., Bestard‐Lorigados, I., & Crawford, D. A. (2018) · Genes Brain & Behavior · doi:10.1111/gbb.12506 · Cited by 55
Sevenoaks, T., Wedderburn, C. J., Donald, K. A., Barnett, W., Zar, H. J., Stein, D. J., & Naudé, P. J. W. (2020) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2020.08.021 · Cited by 50
Two matrix metalloproteinase classes reciprocally regulate synaptogenesis
Dear, M. L., Dani, N., Parkinson, W. M., Zhou, S., & Broadie, K. S. (2015) · Development · doi:10.1242/dev.124461 · Cited by 48
Shabani, E., Abdekhodaie, M. J., Mousavi, S. A., & Taghipour, F. (2020) · Biochemical Engineering Journal · doi:10.1016/j.bej.2020.107772 · Cited by 47
A randomized controlled trial of sertraline in young children with autism spectrum disorder
Potter, L. A., Scholze, D. A., Biag, H. M. B., Schneider, A., Chen, Y., Nguyen, D. V., Rajaratnam, A., Rivera, S. M., Dwyer, P. S., Tassone, F., et al. (2019) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2019.00810 · Cited by 43
Nadanaka, S., Miyata, S., Yaqiang, B., Tamura, J.-I., Habuchi, O., & Kitagawa, H. (2020) · Biomolecules · doi:10.3390/biom10111499 · Cited by 43
Stefano, M. E. D., & Herrero, M. T. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.08.002 · Cited by 42
The Search for an Effective Therapy to Treat Fragile X Syndrome: Dream or Reality?
Castagnola, S., Bardoni, B., & Maurin, T. (2017) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2017.00015 · Cited by 42
Mani, S., Dubey, R., Lai, I., Babu, M. A., Tyagi, S., Swargiary, G., Mody, D., Singh, M., Agarwal, S., Iqbal, D., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220700 · Cited by 43
Reichelt, A. C., Lemieux, C. A., Princz‐Lebel, O., Singh, A., Bussey, T. J., & Saksida, L. M. (2021) · Scientific Reports · doi:10.1038/s41598-021-85092-x · Cited by 40
Cheung, S. W., Bhavnani, E., Simmons, D. G., Bellingham, M. C., & Noakes, P. G. (2024) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12982 · Cited by 36
Minocycline Treatment Reverses Sound Evoked EEG Abnormalities in a Mouse Model of Fragile X Syndrome
Lovelace, J. W., Ethell, I. M., Binder, D. K., & Razak, K. A. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00771 · Cited by 39
Self-citationNon-Cell-Autonomous Factors Implicated in Parvalbumin Interneuron Maturation and Critical Periods
Gibel-Russo, R., Benacom, D., & Nardo, A. A. D. (2022) · Frontiers in Neural Circuits · doi:10.3389/fncir.2022.875873 · Cited by 37
Le, N. D., Muri, L., Grandgirard, D., Kühle, J., Leppert, D., & Leib, S. L. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01966-3 · Cited by 37
Wang, J., & Zhang, Y. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.8674 · Cited by 35
Neuro-Axonal Damage and Alteration of Blood–Brain Barrier Integrity in COVID-19 Patients
Zingaropoli, M. A., Iannetta, M., Piermatteo, L., Pasculli, P., Latronico, T., Mazzuti, L., Campogiani, L., Duca, L., Ferraguti, G., Michele, M. D., et al. (2022) · Cells · doi:10.3390/cells11162480 · Cited by 35
Molecular Biomarkers in Fragile X Syndrome
Zafarullah, M., & Tassone, F. (2019) · Brain Sciences · doi:10.3390/brainsci9050096 · Cited by 36
A conceptualized model linking matrix metalloproteinase-9 to schizophrenia pathogenesis
Bitanihirwe, B. K. Y., & Woo, T.-U. W. (2020) · Schizophrenia Research · doi:10.1016/j.schres.2019.12.015 · Cited by 35
Deckmann, I., Santos‐Terra, J., Fontes‐Dutra, M., Rockenbach, M. K., Bauer‐Negrini, G., Schwingel, G. B., Riesgo, R. D. S., Bambini-Júnior, V., & Gottfried, C. (2021) · International Journal of Developmental Neuroscience · doi:10.1002/jdn.10137 · Cited by 36
Reinhard, S. M., Rais, M., Afroz, S., Hanania, Y., Pendi, K., Espinoza, K., Rosenthal, R., Binder, D. K., Ethell, I. M., & Razak, K. A. (2019) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2019.107042 · Cited by 37
Self-citationBiswas, M. H. U., Almeida, S., Lopez-Gonzalez, R., Mao, W., Zhang, Z., Karydas, A., Geschwind, M. D., Biernat, J., Mandelkow, E., Futai, K., et al. (2016) · Stem Cell Reports · doi:10.1016/j.stemcr.2016.08.006 · Cited by 33
Therapeutic Effects of a Novel Form of Biotin on Propionic Acid-Induced Autistic Features in Rats
Şahin, K., Orhan, C., Karatoprak, S., Tuzcu, M., Deeh, P. B. D., Özercan, İ. H., Şahin, N., Bozoğlan, M. Y., Sylla, S., Ojalvo, S. P., et al. (2022) · Nutrients · doi:10.3390/nu14061280 · Cited by 33
Pasquet, N., Douceau, S., Naveau, M., Lesept, F., Louessard, M., Lebouvier, L., Hommet, Y., Vivien, D., & Bardou, I. (2018) · Cerebral Cortex · doi:10.1093/cercor/bhy119 · Cited by 43
Toledo, M. A., Wen, T. H., Binder, D. K., Ethell, I. M., & Razak, K. A. (2019) · Behavioural Brain Research · doi:10.1016/j.bbr.2019.112068 · Cited by 31
Self-citationMMP-9 Contributes to Dendritic Spine Remodeling Following Traumatic Brain Injury
Pijet, B., Stefaniuk, M., & Kaczmarek, L. (2019) · Neural Plasticity · doi:10.1155/2019/3259295 · Cited by 31
Tissue inhibitors of metalloproteinases are proteolytic targets of matrix metalloproteinase 9
Coates-Park, S., Lazaroff, C., Gurung, S., Rich, J. A., Colladay, A., O’Neill, M. J., Butler, G. S., Overall, C. M., Stetler‐Stevenson, W. G., & Peeney, D. (2023) · Matrix Biology · doi:10.1016/j.matbio.2023.09.002 · Cited by 31
Dear, M. L., Shilts, J., & Broadie, K. (2017) · Science Signaling · doi:10.1126/scisignal.aan3181 · Cited by 29
Kokash, J., Alderson, E. M., Reinhard, S. M., Crawford, C. A., Binder, D. K., Ethell, I. M., & Razak, K. A. (2019) · Brain Research · doi:10.1016/j.brainres.2019.05.029 · Cited by 31
Self-citationOvsepian, S. V., O’Leary, V. B., & Martı́nez, S. (2023) · Brain Structure and Function · doi:10.1007/s00429-023-02728-6 · Cited by 30
Impact of maternal immune activation on dendritic spine development
Pękała, M., Doliwa, M., & Kalita, K. B. (2020) · Developmental Neurobiology · doi:10.1002/dneu.22804 · Cited by 27
Sanapalli, B. K. R., Yele, V., Jupudi, S., & Karri, V. V. S. R. (2021) · RSC Advances · doi:10.1039/d1ra03891e · Cited by 28
Akol, I., Kalogeraki, E., Pielecka-Fortuna, J., Fricke, M., & Löwel, S. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.0902-21.2021 · Cited by 29
GPR18 drives FAAH inhibition-induced neuroprotection against HIV-1 Tat-induced neurodegeneration
Hermes, D. J., Yadav-Samudrala, B. J., Xu, C., Paniccia, J. E., Meeker, R. B., Armstrong, M., Reisdorph, N. A., Cravatt, B. F., Mackie, K., Lichtman, A. H., et al. (2021) · Experimental Neurology · doi:10.1016/j.expneurol.2021.113699 · Cited by 27
In Vivo Volume Dynamics of Dendritic Spines in the Neocortex of Wild-Type and Fmr1 KO Mice
Ishii, K., Nagaoka, A., Kishida, Y., Okazaki, H., Yagishita, S., Ucar, H., Takahashi, N. K., Saito, N., & Kasai, H. (2018) · eNeuro · doi:10.1523/eneuro.0282-18.2018 · Cited by 26
Lysophosphatidic Acid Signalling in Nervous System Development and Function
Birgbauer, E. (2020) · NeuroMolecular Medicine · doi:10.1007/s12017-020-08630-2 · Cited by 27
Sullivan, G., Galdi, P., Borbye‐Lorenzen, N., Stoye, D. Q., Lamb, G. J., Evans, M. J., Skogstrand, K., Chandran, S., & Boardman, J. P. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.722489 · Cited by 26
Dumbuya, J. S., Chen, X., Du, J., Li, S., Liang, L., Xie, H., & Zeng, Q. (2023) · International Immunopharmacology · doi:10.1016/j.intimp.2023.110758 · Cited by 26
Grochecki, P., Smaga, I., Łopatyńska-Mazurek, M., Gibuła‐Tarłowska, E., Kędzierska, E., Listos, J., Talarek, S., Marszałek‐Grabska, M., Hubalewska‐Mazgaj, M., Korga-Plewko, A., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020589 · Cited by 25
Computational study of effective matrix metalloproteinase 9 (MMP9) targeting natural inhibitors
Liu, N., Wang, X., Wu, H., Lv, X., Xie, H., Guo, Z., Wang, J., Dou, G., Zhang, C., & Sun, M. (2021) · Aging · doi:10.18632/aging.203581 · Cited by 25
Ibi, D., & Yamada, K. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161226092 · Cited by 23
Gore, S. V., James, E. J., Huang, L.-C., Park, J. J., Berghella, A. P., Thompson, A. C., Cline, H. T., & Aizenman, C. D. (2021) · eLife · doi:10.7554/elife.62147 · Cited by 26
Dolutegravir Inhibition of Matrix Metalloproteinases Affects Mouse Neurodevelopment
Bade, A. N., McMillan, J., Liu, Y., Edagwa, B., & Gendelman, H. E. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02508-5 · Cited by 29
Wang, J., Ren, D.-P., Sun, Y., Xu, C., Wang, C., Cheng, R., Wang, L., Jia, G., Ren, J., Ma, J., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14996 · Cited by 25
Ganguly, K., Adhikary, K., Acharjee, A., Acharjee, P., Trigun, S. K., Mutlaq, A. S., Ashique, S., Yasmin, S., Alshahrani, A. M., & Ansari, M. Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.135967 · Cited by 23
Arkadash, V., Radisky, E. S., & Papo, N. (2018) · Oncotarget · doi:10.18632/oncotarget.25885 · Cited by 23
Matrix metalloproteinase‐9: A magic drug target in neuropsychiatry?
Kaczmarek, K. T., Protokowicz, K., & Kaczmarek, L. (2023) · Journal of Neurochemistry · doi:10.1111/jnc.15976 · Cited by 23
Altered extracellular matrix structure and elevated stiffness in a brain organoid model for disease
Zur, M. K., Bhattacharya, B., Solomonov, I., Dror, S. B., Savidor, A., Levin, Y., Prior, A., Sapir, T., Harris, T., Olender, T., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59252-w · Cited by 23
MMP-9 Signaling Pathways That Engage Rho GTPases in Brain Plasticity
Figiel, I., Kruk, P. K., Zaręba-Kozioł, M., Rybak, P., Bijata, M., Włodarczyk, J., & Dzwonek, J. (2021) · Cells · doi:10.3390/cells10010166 · Cited by 23
Neuroglia Cells Transcriptomic in Brain Development, Aging and Neurodegenerative Diseases
Pinosanu, L. R., Căpitănescu, B., Glăvan, D., Godeanu, S., Fernández‐Cadenas, I., Doeppner, T. R., Hermann, D. M., Bălşeanu, T. A., Cătălin, B., & Popa‐Wagner, A. (2022) · Aging and Disease · doi:10.14336/ad.2022.0621 · Cited by 23
McGregor, N. W., Thompson, N., O’Connell, K. S., Emsley, R. A., van der Merwe, L., & Warnich, L. (2018) · Psychiatry Research · doi:10.1016/j.psychres.2018.01.044 · Cited by 24
NG2 Glia: Novel Roles beyond Re-/Myelination
Parolisi, R., & Boda, E. (2018) · Neuroglia · doi:10.3390/neuroglia1010011 · Cited by 23
An “Omic” Overview of Fragile X Syndrome
Dionne, O., & Corbin, F. (2021) · Biology · doi:10.3390/biology10050433 · Cited by 24
Agoston, D. V., McCullough, J., Aniceto, R., Lin, I.-H., Kamnaksh, A., Eklund, M., Graves, W. M., Dunbar, C., Engall, J., Schneider, E. B., et al. (2022) · Neurotrauma Reports · doi:10.1089/neur.2022.0029 · Cited by 21
Трофимов, А. Н., Strekalova, T. V., Mortimer, N., Zubareva, O. E., Schwarz, A. P., Svirin, E. P., Umriukhin, A., Svistunov, A. A., Lesch, K., & Клименко, В. М. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9720-2 · Cited by 21
HIV-1 Integrase Strand Transfer Inhibitors and Neurodevelopment
Foster, E. G., Gendelman, H. E., & Bade, A. N. (2022) · Pharmaceuticals · doi:10.3390/ph15121533 · Cited by 20
Metalloproteinases as Biomarkers and Sociomarkers in Human Health and Disease
Costa, D., Scalise, E., Ielapi, N., Bracale, U. M., Andreucci, M., & Serra, R. (2024) · Biomolecules · doi:10.3390/biom14010096 · Cited by 23
Islam, Y., Khalid, A., Pluchino, S., Sivakumaran, M., Teixidò, M., Leach, A. G., Fatokun, A. A., Downing, J., Coxon, C. R., & Ehtezazi, T. (2020) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2020.06.021 · Cited by 20
Çiçek, A. U., Işık, C. M., Bakır, S., Özbek, D. Ü., Sarı, S. A., Bakır, D., & Cam, S. (2020) · Journal of Neural Transmission · doi:10.1007/s00702-020-02231-w · Cited by 20
Bobotis, B. C., Halvorson, T., Carrier, M., & Tremblay, M. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1317125 · Cited by 21
BDNF-driven synaptic plasticity requires autocrine matrix metalloproteinase–9 activity
Legutko, D., Bijoch, Ł., Olszak, G., Kuźniewska, B., Kalita, K. B., Yasuda, R., Kaczmarek, L., & Michaluk, P. (2025) · Science Advances · doi:10.1126/sciadv.adx2369 · Cited by 22
Hodges, S. L., Nolan, S. O., Tomac, L. A., Muhammad, I. D. A., Binder, M. S., Taube, J. H., & Lugo, J. N. (2019) · Physiology & Behavior · doi:10.1016/j.physbeh.2019.112776 · Cited by 20
MicroRNAs: Possible Regulatory Molecular Switch Controlling the BBB Microenvironment
Chakraborty, C., Sharma, A. R., Sharma, G., Bhattacharya, M., & Lee, S. (2020) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2019.12.024 · Cited by 18
Porter, K. N., Sarkar, S. N., Dakhlallah, D. A., Vannoy, M. E., Quintana, D. D., & Simpkins, J. W. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00092 · Cited by 17
Włodarczyk, L., Cichoń, N., Karbownik, M. S., Saso, L., Saluk, J., & Miller, E. D. (2023) · Brain Sciences · doi:10.3390/brainsci13060846 · Cited by 18
Inhibition of MMP-9 attenuates hypertensive cerebrovascular dysfunction in Dahl salt-sensitive rats
Kalani, A., Pushpakumar, S. B., Vacek, J. C., Tyagi, S. C., & Tyagi, N. (2016) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-015-2623-8 · Cited by 18
Metadata
- Authors
- Reinhard, S. M., Razak, K., & Ethell, I. M.
- Affiliations
- University of California, Riverside (US)
- Corresponding author
- Ethell, Iryna M.
- Venue
- Frontiers in Cellular Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2015-07-29
- Volume
- 9
- Pages
- 280-280
- ISSN
- 1662-5102 (ISSN-L)
- PMC
- PMC4518323
- OpenAlex
- W1504544942
- Cited by
- 219
- References
- 145
- Citations by year
- 2026: 9 · 2025: 18 · 2024: 16 · 2023: 28 · 2022: 32 · 2021: 34 · 2020: 29 · 2019: 17 · 2018: 14 · 2017: 7 · 2016: 11 · 2015: 4
- FWCI
- 1.56
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Frontiers in Cellular Neuroscience (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Science Foundation
- FRAXA Research Foundation
- National Institute of Mental Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Keywords
- MMP-9, extracellular matrix, brain development, neurodevelopmental disorders, critical period, synaptogenesis, axon guidance, myelination, synaptic plasticity, fragile X syndrome, traumatic brain injury, multiple sclerosis, Alzheimer's disease
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