The DOI matches its Crossref record; 269 of the 269 references it cites were found in a registry or an index.
MMPs in learning and memory and neuropsychiatric disorders
Open accessAbstract
Matrix metalloproteinases (MMPs) are a group of over twenty proteases, operating chiefly extracellularly to cleave components of the extracellular matrix, cell adhesion molecules as well as cytokines and growth factors. By virtue of their expression and activity patterns in animal models and clinical investigations, as well as functional studies with gene knockouts and enzyme inhibitors, MMPs have been demonstrated to play a paramount role in many physiological and pathological processes in the brain. In particular, they have been shown to influence learning and memory processes, as well as major neuropsychiatric disorders such as schizophrenia, various kinds of addiction, epilepsy, fragile X syndrome, and depression. A possible link connecting all those conditions is either physiological or aberrant synaptic plasticity where some MMPs, e.g., MMP-9, have been demonstrated to contribute to the structural and functional reorganization of excitatory synapses that are located on dendritic spines. Another common theme linking the aforementioned pathological conditions is neuroinflammation and MMPs have also been shown to be important mediators of immune responses.
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?
The cited source says what the claim attributes to it.
In the citing paper
“The ECM can be modified rapidly by the release of proteases [36], by microglial action and by internalization, all of which can be activated by memory events [37–39].”
From The extracellular matrix and perineuronal nets in memory (2022) · cites this paper as [37]
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
Diagnostic and Statistical Manual of Mental Disorders
American Psychiatric Association (2013) · doi:10.1176/appi.books.9780890425596 · Cited by 116,369
Diagnostic and Statistical Manual of Mental Disorders(DSM)
Leong, F. T. L. (2008) · Sage eBooks · doi:10.4135/9781412963978.n182 · Cited by 10,861
Diagnostic and Statistical Manual of Mental Disorders ( DSM ‐ IV ‐ TR )
Segal, D. L. (2010) · Wiley eBooks · doi:10.1002/9780470479216.corpsy0271 · Cited by 4,687
How Matrix Metalloproteinases Regulate Cell Behavior
Sternlicht, M. D., & Werb, Z. (2001) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.17.1.463 · Cited by 3,959
Yatham, L. N., & Malhi, G. S. (2011) · Oxford University Press eBooks · doi:10.1093/med/9780199562305.001.0001 · Cited by 3,515
A Systematic Review of the Prevalence of Schizophrenia
Saha, S., Chant, D., Welham, J., & McGrath, J. (2005) · PLoS Medicine · doi:10.1371/journal.pmed.0020141 · Cited by 2,168
Regulation of Cell Survival by Secreted Proneurotrophins
Lee, R., Kermani, P., Teng, K. K., & Hempstead, B. L. (2001) · Science · doi:10.1126/science.1065057 · Cited by 1,670
Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase
Strongin, A. Y., Collier, I. E., Bannikov, G. A., Marmer, B. L., Grant, G. A., & Goldberg, G. I. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.10.5331 · Cited by 1,605
Liao, D., Hessler, N. A., & Malinow, R. (1995) · Nature · doi:10.1038/375400a0 · Cited by 1,365
The brain on drugs: from reward to addiction
Volkow, N. D., & Morales, M. (2015) · Cell · doi:10.1016/j.cell.2015.07.046 · Cited by 1,306
Cited by
Sorted by citations
Items 201–208 of 208
Kargar, M., Shirvani-Farsani, Z., Sharma, R., & Ghafouri‐Fard, S. (2026) · Molecular Biology Reports · doi:10.1007/s11033-026-12119-9
Hodebourg, R., Duncan, L., Dereschewitz, E., & Kalivas, P. W. (2026) · Molecular Psychiatry · doi:10.1038/s41380-026-03687-0
Cramer, T. L. M., Hannan, S. B., Petre, L., Bear, M. F., Hensch, T. K., & Tyagarajan, S. K. (2026) · Molecular Psychiatry · doi:10.1038/s41380-026-03672-7
Pedraz-Petrozzi, B., Wilkening, J., Ziegler, N., Arns, M., Sartorius, A., & Goya‐Maldonado, R. (2026) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2026.111814
Ogbu, J. I., Moreira, C. V. L., Olusola, A. J., Lacerda, R. F., Maggi, L. E., Filho, A. S. S., Xavier, C. H., Pedrino, G. R., Costa, É. A., & Fajemiroye, J. O. (2026) · Current Pharmacology Reports · doi:10.1007/s40495-026-00472-z
Liang, R., Li, M., Li, J., Zhou, Y., Li, T., Zhu, X., & Zhou, X. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.117376
Role of diallyl disulfide in cancer: Molecular mechanisms and therapeutic interventions
Liu, M.-Y., Wang, B., Xu, J.-X., Wei, Y.-C., Wang, W.-Q., Hao, M.-Y., Si, W.-R., Jiang, Q., & Wu, D. (2026) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2026.119348
Metadata
- Authors
- Beroun, A., Mitra, S., Michaluk, P., Pijet, B., Stefaniuk, M., & Kaczmarek, L.
- Affiliations
- Instytut Biologii Doświadczalnej im. Marcelego Nenckiego (PL)
- Corresponding author
- Kaczmarek, Leszek
- Venue
- Cellular and Molecular Life Sciences
- Published
- 2019-06-06
- Volume
- 76
- Issue
- 16
- Pages
- 3207-3228
- ISSN
- 1420-682X (ISSN-L)
- 1420-9071
- PMC
- PMC6647627
- OpenAlex
- W2954884521
- Cited by
- 207
- References
- 269
- Citations by year
- 2026: 16 · 2025: 24 · 2024: 34 · 2023: 31 · 2022: 40 · 2021: 25 · 2020: 32 · 2019: 4
- FWCI
- 2.44
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Cellular and Molecular Life Sciences (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Foundation for Polish Science (BRAINCITY)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- matrix metalloproteinases, MMP-9, learning and memory, neuropsychiatric disorders, schizophrenia, addiction, epilepsy, fragile X syndrome, depression, synaptic plasticity, dendritic spines, neuroinflammation, extracellular matrix, cytokines and growth factors
- MeSH terms
- Animals, Mental Disorders, Brain, Epilepsy, Humans, Learning, Memory, Neuronal Plasticity, Tissue Inhibitor of Metalloproteinases, Matrix Metalloproteinases
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
