Matrix metalloproteinases and their multiple roles in neurodegenerative diseases

Matrix Metalloproteinase Inhibitors and Cancer—Trials and Tribulations

Coussens, L. M., Fingleton, B., & Matrisian, L. M. (2002) · Science · doi:10.1126/science.1067100 · Cited by 2,761

Silent Brain Infarcts and the Risk of Dementia and Cognitive Decline

Vermeer, S. E., Prins, N. D., den Heijer, T., Hofman, A., Koudstaal, P. J., & Breteler, M. M. B. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa022066 · Cited by 2,313

Intracellular amyloid-β in Alzheimer's disease

LaFerla, F. M., Green, K. N., & Oddo, S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2168 · Cited by 1,942

Tissue inhibitors of metalloproteinases: evolution, structure and function

Brew, K., Dinakarpandian, D., & Nagase, H. (2000) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00279-4 · Cited by 1,932

Mechanisms, challenges and opportunities in stroke

Lo, E. H., Dalkara, T., & Moskowitz, M. A. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1106 · Cited by 1,808

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 1,589

The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.

Van Wart, H. E., & Birkedal-Hansen, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5578 · Cited by 1,475

Strategies for MMP inhibition in cancer: innovations for the post-trial era

Overall, C. M., & López-Otín, C. (2002) · Nature Reviews Cancer · doi:10.1038/nrc884 · Cited by 1,349

Neurovascular coupling in the normal brain and in hypertension, stroke, and Alzheimer disease

Girouard, H., & Iadecola, C. (2005) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00966.2005 · Cited by 1,311

VEGF enhances angiogenesis and promotes blood–brain barrier leakage in the ischemic brain

Zhang, Z. G., Zhang, L., Jiang, Q., Zhang, R., Davies, K., Powers, C., Bruggen, N. V., & Chopp, M. (2000) · Journal of Clinical Investigation · doi:10.1172/jci9369 · Cited by 1,296

Potential drug targets and treatment of schizophrenia

Kumar, A., Yadav, M., Parle, M., Dhingra, S., & Dhull, D. K. (2017) · Inflammopharmacology · doi:10.1007/s10787-017-0340-5 · Cited by 26

A R2p/R1p Ratiometric Procedure to Assess Matrix Metalloproteinase‐2 Activity by Magnetic Resonance Imaging

Catanzaro, V., Gringeri, C. V., Menchise, V., Padovan, S., Boffa, C., Dastrù, W., Chaabane, L., Digilio, G., & Aime, S. (2013) · Angewandte Chemie · doi:10.1002/ange.201209286 · Cited by 27

Serum tissue inhibitor of metalloproteinase‐1 and risk of cognitive impairment after acute ischaemic stroke

Ge, J., Li, R., Yuan, P., Che, B., Bu, X., Shao, H., Xu, T., Ju, Z., Zhang, J., Zhang, Y., et al. (2020) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.15369 · Cited by 26

Kaempferol prevents the activation of complement C3 protein and the generation of reactive A1 astrocytes that mediate rat brain degeneration induced by 3-nitropropionic acid

López‐Sánchez, C., Poejo, J., García‐López, V., Salazar, J., García‐Martínez, V., & Gutiérrez‐Merino, C. (2022) · Food and Chemical Toxicology · doi:10.1016/j.fct.2022.113017 · Cited by 27

Protective effect of a hydromethanolic extract from Fraxinus excelsior L. bark against a rat model of aluminum chloride-induced Alzheimer's disease: Relevance to its anti-inflammatory and antioxidant effects

Iranpanah, A., Fakhri, S., Bahrami, G., Majnooni, M. B., Gravandi, M. M., Taghavi, S., Badrbani, M. A., Amirian, R., & Farzaei, M. H. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.117708 · Cited by 26

Nanoparticle and liposome formulations of doxycycline: Transport properties through Caco-2 cell line and effects on matrix metalloproteinase secretion

Yücel, Ç., Değim, Z., & Yılmaz, Ş. (2013) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2013.03.001 · Cited by 26

Xiao-Xu-Ming Decoction Protects against Blood-Brain Barrier Disruption and Neurological Injury Induced by Cerebral Ischemia and Reperfusion in Rats

Lan, R., Xiang, J. Y., Wang, G., Li, W., Zhang, W., Xu, L., & Cai, D. (2013) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2013/629782 · Cited by 26

Niaspan Attenuates the Adverse Effects of Bone Marrow Stromal Cell Treatment of Stroke in Type One Diabetic Rats

Yan, T., Ye, X., Chopp, M., Zacharek, A., Ning, R., Venkat, P., Roberts, C. J., Lü, M., & Chen, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0081199 · Cited by 25

In silico-based screen synergistic drug combinations from herb medicines: a case using Cistanche tubulosa

Liu, J., Zhu, J., Xue, J., Qin, Z., Shen, F., Liu, J., Chen, X., Li, X., Wu, Z., Xiao, W., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-16571-3 · Cited by 25

Ratiometric magnetic resonance imaging: Contrast agent design towards better specificity and quantification

Genicio, N., Bañobre‐López, M., Gröhn, O. H. J., & Gallo, J. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214150 · Cited by 25

Maresin 1 improves cognitive decline and ameliorates inflammation and blood-brain barrier damage in rats with chronic cerebral hypoperfusion

Tian, L., Zheng, J., Wang, Z., Xu, L., Sun, D., Song, H., Wu, S., Du, M., Peng, S., & Zhang, J. (2022) · Brain Research · doi:10.1016/j.brainres.2022.147936 · Cited by 25

Comparison of the Effects of Matrix Metalloproteinase Inhibitors on TNF-α Release from Activated Microglia and TNF-α Converting Enzyme Activity

Lee, E.-J., Moon, P., Baek, M., & Kim, H.-S. (2014) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2014.099 · Cited by 25

Hypoxia-controlled matrix metalloproteinase-9 hyperexpression promotes behavioral recovery after ischemia

Cai, H., Mu, Z., Jiang, Z., Wang, Y., Yang, G., & Zhang, Z. (2015) · Neuroscience Bulletin · doi:10.1007/s12264-015-1533-1 · Cited by 25

Endoplasmic Reticulum Malfunction in the Nervous System

Jung, J., Michalak, M., & Agellon, L. B. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00220 · Cited by 25

Protection of blood-brain barrier as a potential mechanism for enriched environments to improve cognitive impairment caused by chronic cerebral hypoperfusion

Qu, C., Xu, L., Shen, J., Li, Y., Qu, C., Song, H., & Zhang, J. (2019) · Behavioural Brain Research · doi:10.1016/j.bbr.2019.112385 · Cited by 25

Therapeutic strategies to attenuate hemorrhagic transformation after tissue plasminogen activator treatment for acute ischemic stroke

Shimohata, T., Kanazawa, M., Kawamura, K., Takahashi, T., & Nishizawa, M. (2013) · Neurology and Clinical Neuroscience · doi:10.1111/ncn3.63 · Cited by 24

Impaired Cerebral Perfusion in Multiple Sclerosis: Relevance of Endothelial Factors

Monti, L., Morbidelli, L., & Rossi, A. (2018) · Biomarker Insights · doi:10.1177/1177271918774800 · Cited by 20

Marine Natural Products from the Russian Pacific as Sources of Drugs for Neurodegenerative Diseases

Khotimchenko, Y. S., Silachev, D. N., & Katanaev, V. L. (2022) · Marine Drugs · doi:10.3390/md20110708 · Cited by 25

Stem Cells in Amyotrophic Lateral Sclerosis: Motor Neuron Protection or Replacement?

Silani, V., Calzarossa, C., Cova, L., & Ticozzi, N. (2010) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152710791292666 · Cited by 24

Excitatory and Mitogenic Signaling in Cell Death, Blood–brain Barrier Breakdown, and BBB Repair after Intracerebral Hemorrhage

Liu, D., & Sharp, F. R. (2012) · Translational Stroke Research · doi:10.1007/s12975-012-0147-z · Cited by 25

Tightening the retinal glia limitans attenuates neuroinflammation after optic nerve injury

Lefevere, E., Salinas‐Navarro, M., Andries, L., Noterdaeme, L., Etienne, I., Wonterghem, E. V., Vinckier, S., Davis, B. M., Bergen, T. V., Hove, I. V., et al. (2020) · Glia · doi:10.1002/glia.23875 · Cited by 23

Metal Complexes as Promising Matrix Metalloproteinases Regulators

Nguyen, Y. T., Kim, N., & Lee, H. J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021258 · Cited by 25

Coadministration of Branched-Chain Amino Acids and Lipopolysaccharide Causes Matrix Metalloproteinase Activation and Blood–Brain Barrier Breakdown

Scaini, G., Morais, M. O. D. S., Galant, L. S., Vuolo, F. S., Dall’Igna, D. M., Pasquali, M. A. D. B., Ramos, V. D. M., Gelain, D. P., Moreira, J. C. F., Schuck, P. F., et al. (2014) · Molecular Neurobiology · doi:10.1007/s12035-013-8618-0 · Cited by 23

Effects of oxidative stress on amyloid precursor protein processing in rat and human platelets

Ehrlich, D., Hochstrasser, T., & Humpel, C. (2012) · Platelets · doi:10.3109/09537104.2012.661104 · Cited by 23

Matrix metalloproteinase-2 and -9 in the cerebellum of teleost fish: Functional implications for adult neurogenesis

Sîrbulescu, R. F., Ilieş, I., & Zupanc, G. K. H. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.03.015 · Cited by 22

The effect of age-related risk factors and comorbidities on white matter injury and repair after ischemic stroke

Xu, M., Wang, M. M., Gao, Y., Keep, R. F., & Shi, Y. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.07.008 · Cited by 22

Microglia in the Pathophysiology of Hemorrhagic Stroke and the Relationship Between Microglia and Pain After Stroke: A Narrative Review

He, C., Liu, R., Fan, Z., Li, Y., Yang, M., Wugang, H., Lu, Z., Fang, Z., & Su, B. (2021) · Pain and Therapy · doi:10.1007/s40122-021-00288-3 · Cited by 28

Decreased levels of cytokines implicate altered immune response in plasma of moderate-stage Alzheimer’s disease patients

Koca, S., Kiris, İ., Şahin, Ş., Çınar, N., Karşıdağ, S., Hanağası, H. A., Yıldız, G. B., & Baykal, A. T. (2022) · Neuroscience Letters · doi:10.1016/j.neulet.2022.136799 · Cited by 23

MMP-12 knockdown prevents secondary brain damage after ischemic stroke in mice

Arruri, V. K., Chokkalla, A. K., Jeong, S., Chelluboina, B., Mehta, S. L., Veeravalli, K. K., & Vemuganti, R. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105432 · Cited by 23

Matrix metalloproteinases and their tissue inhibitors in serum and cerebrospinal fluid of patients with moderate and severe traumatic brain injury

Wang, Z., Zheng, K., Li, C., Shan, X., Liu, H., Fan, W., & Zheng, P. (2013) · Neurology India · doi:10.4103/0028-3886.125258 · Cited by 22

Evaluation of matrix metalloproteinases in serum of patients with amyotrophic lateral sclerosis with pattern recognition methods.

Sokołowska, B., Jóźwik, A., Niebrój-Dobosz, I., Janik, P., & Kwieciński, H. (2009) · PubMed · Cited by 22

Decreased TNF Levels and Improved Retinal Ganglion Cell Survival in MMP‐2 Null Mice Suggest a Role for MMP‐2 as TNF Sheddase

Groef, L. D., Salinas‐Navarro, M., Imschoot, G. V., Libert, C., Vandenbroucke, R. E., & Moons, L. (2015) · Mediators of Inflammation · doi:10.1155/2015/108617 · Cited by 22

Antibiotics-Induced Obesity: A Mitochondrial Perspective

Andrade, M. J., Jayaprakash, C., Bhat, S., Evangelatos, N. G., Brand, A. M., & Satyamoorthy, K. (2017) · Public Health Genomics · doi:10.1159/000485095 · Cited by 23

Matrix metalloproteinases 2 and 9 in the cochlea: expression and activity after aminoglycoside exposition

Setz, C., Brand, Y., Radojevic, V., Hanusek, C., Mullen, P. J., Levano, S., Listyo, A., & Bodmer, D. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.02.043 · Cited by 22

Disturbance in Venous Outflow From the Cerebral Circulation Intensifies the Release of Blood-Brain Barrier Injury Biomarkers in Patients Undergoing Cardiac Surgery

Kotlińska-Hasiec, E., Czajkowski, M., Rzecki, Z., Stadnik, A., Olszewski, K. J., Rybojad, B., & Dąbrowski, W. (2013) · Journal of Cardiothoracic and Vascular Anesthesia · doi:10.1053/j.jvca.2013.05.008 · Cited by 22

Contributions of Drug Transporters to Blood-Brain Barriers

Liu, L., & Liu, X. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-7647-4_9 · Cited by 21

A synergy between the catalytic and structural Zn(II) ions and the enzyme and substrate dynamics underlies the structure–function relationships of matrix metalloproteinase collagenolysis

Varghese, A., Chaturvedi, S. S., Fields, G., & Karabencheva‐Christova, T. G. (2021) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-021-01876-6 · Cited by 22

Metalloproteinases and neurodegenerative diseases: pathophysiological and therapeutic perspectives

Rosenberg, G. A. (2015) · Metalloproteinases In Medicine · doi:10.2147/mnm.s68849 · Cited by 21

Plasma Matrix Metalloproteinases in Patients With Stroke During Intensive Rehabilitation Therapy

Ma, F., Rodríguez, S., Buxó, X., Morancho, A., Llena, I. R., Carrera, A., Bustamante, A., Giralt, D., Montaner, J., Martinez, C., et al. (2016) · Archives of Physical Medicine and Rehabilitation · doi:10.1016/j.apmr.2016.06.007 · Cited by 24

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

Transcriptomics of aged Drosophila motor neurons reveals a matrix metalloproteinase that impairs motor function

Azpurua, J., Mahoney, R. E., & Eaton, B. A. (2018) · Aging Cell · doi:10.1111/acel.12729 · Cited by 20

MiR-874-3p plays a protective role in intervertebral disc degeneration by suppressing MMP2 and MMP3

Song, Q., Zhang, F., Wang, K., Chen, Z., Li, Q., Liu, Z., & Shen, H. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173891 · Cited by 21

Sex-specific associations of matrix metalloproteinases in Alzheimer’s disease

Aksnes, M., Edwin, T. H., Saltvedt, I. T., Eldholm, R. S., Chaudhry, F. A., Halaas, N. B., Myrstad, M., Watne, L. O., & Knapskog, A. (2023) · Biology of Sex Differences · doi:10.1186/s13293-023-00514-x · Cited by 20

Cellular junction dynamics and Alzheimer’s disease: a comprehensive review

Asghari, K., Niknam, Z., Mohammadpour-Asl, S., & Chodari, L. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09242-w · Cited by 20

An Update of Kaempferol Protection against Brain Damage Induced by Ischemia-Reperfusion and by 3-Nitropropionic Acid

López‐Sánchez, C., Lagoa, R., Poejo, J., García‐López, V., García‐Martínez, V., & Gutiérrez‐Merino, C. (2024) · Molecules · doi:10.3390/molecules29040776 · Cited by 21

OXPHOS toxicogenomics and Parkinson's disease

López‐Gallardo, E., Iceta, R., Iglesias, E., Montoya, J., & Ruiz‐Pesini, E. (2011) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2011.06.004 · Cited by 19

HIV-1 Tat-induced cerebrovascular toxicity is enhanced in mice with amyloid deposits

Chen, L., Choi, J. J., Choi, Y. J., Hennig, B., & Toborek, M. J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.06.004 · Cited by 20

Matrix metalloproteinase-9 (MMP-9): A macromolecular mediator in CNS infections: A review

Mubarak, M. M., Baba, I. A., Wani, Z. A., Kantroo, H. A., & Ahmad, Z. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143902 · Cited by 20

Spinal Glia Division Contributes to Conditioning Lesion–Induced Axon Regeneration Into the Injured Spinal Cord

Liu, H., Angert, M., Nishihara, T., Shubayev, I., Dolkas, J., & Shubayev, V. I. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000192 · Cited by 19

Neurotoxic factors released by stimulated human monocytes and THP-1 cells

Lee, M., Suk, K., Kang, Y., McGeer, E. G., & McGeer, P. L. (2011) · Brain Research · doi:10.1016/j.brainres.2011.05.021 · Cited by 19

Chronic Cerebral Hypoperfusion Induces Alterations of Matrix Metalloproteinase-9 and Angiopoietin-2 Levels in the Rat Hippocampus

Kim, M., Choi, B., Lee, Y. W., Kim, D.-H., Han, Y. S., Jeon, W. K., & Han, J. (2018) · Experimental Neurobiology · doi:10.5607/en.2018.27.4.299 · Cited by 19

MicroRNA-195-5p Attenuates Intracerebral-Hemorrhage-Induced Brain Damage by Inhibiting MMP-9/MMP-2 Expression

Tsai, Y.-C., Chang, C.-H., Chong, Y. B., Wu, C., Tsai, H., Cheng, T., & Lin, C. (2024) · Biomedicines · doi:10.3390/biomedicines12061373 · Cited by 19

Matrix metalloproteinases are associated with brain atrophy in cognitively unimpaired individuals.

Aksnes, M., Capogna, E., Vidal-Piñeiro, D., Chaudhry, F., Myrstad, M., Idland, A., Halaas, N., Dakhil, S., Blennow, K., Zetterberg, H., et al. (2023) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2023.05.012 · Cited by 16

Minding the Gap: Exploring Neuroinflammatory and Microglial Sex Differences in Alzheimer’s Disease

Reed-Geaghan, E. G., & Keller-Norrell, P. R. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242417377 · Cited by 19

tPA in the Central Nervous System: Relations Between tPA and Cell Surface LRPs

Ortolano, S., & Spuch, C. (2012) · Recent Patents on Endocrine Metabolic & Immune Drug Discovery · doi:10.2174/187221413804660962 · Cited by 20

Marine pharmacology: therapeutic targeting of matrix metalloproteinases in neuroinflammation

Gentile, E., & Liuzzi, G. M. (2016) · Drug Discovery Today · doi:10.1016/j.drudis.2016.09.023 · Cited by 19

Amyloid-beta (25–35) peptide induces the release of pro-matrix metalloprotease 9 (pro-MMP-9) from human neutrophils

Achilli, C., Ciana, A., & Minetti, G. (2014) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-014-2178-0 · Cited by 18

Mechanical stretching induces matrix metalloproteinase-2 expression in rat retinal glial (Müller) cells

Wang, X., Xu, G., Fan, J., & Zhang, M. (2013) · Neuroreport · doi:10.1097/wnr.0b013e32835eb9d1 · Cited by 18

Correlation of matrix metalloproteinase 3 and matrix metalloproteinase 9 levels with non-motor symptoms in patients with Parkinson’s disease

Liu, C. Z., Guo, D. S., Ma, J. J., Dong, L. R., Chang, Q., Yang, H. Q., Liang, K., Li, X. H., Yang, D., Fan, Y., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.889257 · Cited by 19

Vascular Effects on Cerebrovascular Permeability and Neurodegeneration

Sulimai, N., Brown, J. D., & Lominadze, D. G. (2023) · Biomolecules · doi:10.3390/biom13040648 · Cited by 17

Effects of Dexmedetomidine-Isoflurane versus Isoflurane Anesthesia on Brain Injury After Cardiac Valve Replacement Surgery

Kang, F., Tang, C., Han, M., Chai, X., Huang, X., & Li, J. (2017) · Journal of Cardiothoracic and Vascular Anesthesia · doi:10.1053/j.jvca.2017.11.028 · Cited by 17

Efficiency of Protease-Activatable Virus Nanonodes Tuned Through Incorporation of Wild-Type Capsid Subunits

Ho, M. L., Judd, J., Kuypers, B. E., Yamagami, M., Wong, F. F., & Suh, J. (2014) · Cellular and Molecular Bioengineering · doi:10.1007/s12195-014-0334-y · Cited by 17

Associations of Matrix Metalloproteinase-9 and Tissue Inhibitory Factor-1 Polymorphisms With Parkinson Disease in Taiwan

Chen, Y., Wu, Y., Mesri, M., & Chen, C. (2016) · Medicine · doi:10.1097/md.0000000000002672 · Cited by 19

PR1P ameliorates neurodegeneration through activation of VEGF signaling pathway and remodeling of the extracellular environment

Chi, Z., Adini, A., Birsner, A. E., Bazinet, L. F., Akula, J. D., & D’Amato, R. J. (2018) · Neuropharmacology · doi:10.1016/j.neuropharm.2018.12.029 · Cited by 16

Cell Type-Specific Oxidative Stress Genomic Signatures in the Globus Pallidus of Dopamine-Depleted Mice

Lawler, A. J., Brown, A. R., Bouchard, R. S., Toong, N., Kim, Y., Velraj, N., Fox, G. A., Kleyman, M., Kang, B., Gittis, A. H., et al. (2020) · Journal of Neuroscience · doi:10.1523/jneurosci.1634-20.2020 · Cited by 18

Cerebrospinal fluid cytokines and metalloproteinases in cerebral amyloid angiopathy‐related inflammation

Sakai, K., Noguchi‐Shinohara, M., Ikeda, T., Hamaguchi, T., Ono, K., & Yamada, M. (2020) · Acta Neurologica Scandinavica · doi:10.1111/ane.13382 · Cited by 16

Histamine induces the production of matrix metalloproteinase-9 in human astrocytic cultures via H1-receptor subtype

Patel, A., Vasanthan, V., Fu, W., Fahlman, R. P., MacTavish, D., & Jhamandas, J. H. (2015) · Brain Structure and Function · doi:10.1007/s00429-015-1007-x · Cited by 19

Exploring in house glutamate inhibitors of matrix metalloproteinase-2 through validated robust chemico-biological quantitative approaches

Adhikari, N., Amin, S. A., Saha, A., & Jha, T. (2017) · Structural Chemistry · doi:10.1007/s11224-017-1028-6 · Cited by 16

Emerging Understanding of Roles for Arterioles in Inflammation

Sumagin, R., & Sarelius, I. H. (2013) · Microcirculation · doi:10.1111/micc.12068 · Cited by 16

Neutrophils and NETosis in Alzheimer’s disease: Unraveling pathogenic mechanisms and novel therapeutic targets

Chavoshinezhad, S., Beirami, E., & Izadpanah, E. (2025) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2025.118568 · Cited by 15

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 17

Altered matrix metalloproteinases and tissue inhibitors of metalloproteinases in embryos from diabetic rats during early organogenesis

Higa, R., Kurtz, M., Capobianco, E., Martínez, N., White, V., & Jawerbaum, A. (2011) · Reproductive Toxicology · doi:10.1016/j.reprotox.2011.09.003 · Cited by 15

Inhibitory Effect of Aqueous Extracts from Marine Sponges on the Activity and Expression of Gelatinases A (MMP-2) and B (MMP-9) in Rat Astrocyte Cultures

Bari, G. D., Gentile, E., Latronico, T., Corriero, G., Fasano, A., Marzano, C. N., & Liuzzi, G. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0129322 · Cited by 15

Altered expression of tissue remodeling genes in a mouse model of acute allergic rhinitis

Sautter, N. B., Delaney, K. L., & Trune, D. R. (2011) · International Forum of Allergy & Rhinology · doi:10.1002/alr.20059 · Cited by 15

Matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) in the tumors of central nervous system (CNS)

Łukaszewicz‐Zając, M., Mroczko, B., Kornhuber, J., & Lewczuk, P. (2013) · Journal of Neural Transmission · doi:10.1007/s00702-013-1143-5 · Cited by 15

Genetic variations in the ADAMTS12 gene are associated with schizophrenia in Puerto Rican patients of Spanish descent

Bespalova, I. N., Angelo, G. W., Ritter, B. P., Hunter, J., Reyes-Rabanillo, M. L., Siever, L. J., & Silverman, J. M. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8169-y · Cited by 14

The role of matrix metalloproteinases in liver function and disease

Mitropoulou, G., Kompoura, V., Saffioti, F., & Mavroeidis, V. K. (2025) · Frontiers in Bioscience-Landmark · doi:10.31083/fbl27127 · Cited by 14

Crosstalk Between Matrix Metalloproteinases and Their Inducer EMMPRIN/CD147: a Promising Therapeutic Target for Intracerebral Hemorrhage

Liu, Y., Qi, L., Li, Z., Yong, V. W., & Xue, M. (2023) · Translational Stroke Research · doi:10.1007/s12975-023-01225-6 · Cited by 15

CNS / PNS proteoglycans functionalize neuronal and astrocyte niche microenvironments optimizing cellular activity by preserving membrane polarization dynamics, ionic microenvironments, ion fluxes, neuronal activation, and network neurotransductive capacity

Melrose, J. (2024) · Journal of Neuroscience Research · doi:10.1002/jnr.25361 · Cited by 15

Fingolimod (FTY720-P) Does Not Stabilize the Blood–Brain Barrier under Inflammatory Conditions in an in Vitro Model

Schuhmann, M. K., Bittner, S., Meuth, S. G., Kleinschnitz, C., & Fluri, F. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161226177 · Cited by 14

Delayed Astrogliosis Associated with Reduced M1 Microglia Activation in Matrix Metalloproteinase 12 Knockout Mice during Theiler’s Murine Encephalomyelitis

Hansmann, F., Zhang, N., Herder, V., Leitzen, E., & Baumgärtner, W. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20071702 · Cited by 14

Vascular Dysfunction in Brain Hemorrhage: Translational Pathways to Developing New Treatments from Old Targets

Lapchak, P. A., & Wu, Q. (2011) · Journal of Neurology & Neurophysiology · doi:10.4172/2155-9562.s1-e001 · Cited by 14

System biology approaches to identify hub genes linked with ECM organization and inflammatory signaling pathways in schizophrenia pathogenesis

Bhuiyan, P., Sun, Z., Khan, M. A., Hossain, M. A., Rahman, M. H., & Qian, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e25191 · Cited by 14

Matrix metalloproteinase-degraded type I collagen is associated with APOE/TOMM40 variants and preclinical dementia

Tang, M. E., Blair, J., Bager, C. L., Bay‐Jensen, A., Henriksen, K., Christiansen, C., & Karsdal, M. A. (2020) · Neurology Genetics · doi:10.1212/nxg.0000000000000508 · Cited by 13

Two-Dimensional Zymography Differentiates Gelatinase Isoforms in Stimulated Microglial Cells and in Brain Tissues of Acute Brain Injuries

Chen, S., Meng, F., Chen, Z., Tomlinson, B. N., Wesley, J. M., Sun, G. Y., Whaley‐Connell, A. T., Sowers, J. R., Cui, J., & Gu, Z. (2015) · PLoS ONE · doi:10.1371/journal.pone.0123852 · Cited by 12

Retinal glia in myopia: current understanding and future directions

Chen, P., Ji, J., Chen, X., Zhang, J., Wen, X., & Liu, L. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1512988 · Cited by 13

Mycobacterium tuberculosis causes a leaky blood‐brain barrier and neuroinflammation in the prefrontal cortex and cerebellum regions of infected mice offspring

Manjeese, W., Mvubu, N. E., Steyn, A. J. C., & Mpofana, T. (2021) · International Journal of Developmental Neuroscience · doi:10.1002/jdn.10116 · Cited by 12

Compartmentalization of Proteolysis

Brix, K., Scott, C. J., & Heck, M. M. S. (2013) · Springer eBooks · doi:10.1007/978-3-7091-0885-7_3 · Cited by 12

Multiplexing and multivariate analysis in neurodegeneration

Andréasson, U., Portelius, E., Pannee, J., Zetterberg, H., & Blennow, K. (2012) · Methods · doi:10.1016/j.ymeth.2012.02.004 · Cited by 12

Women and Chest Pain: Recognizing the Different Faces of Angina in the Emergency Department.

Safdar, B., & D’Onofrio, G. (2016) · PubMed Central · Cited by 12

Zbtb7c is a molecular ‘off’ and ‘on’ switch of Mmp gene transcription

Jeon, B., Yoon, J.-H., Kim, M.-K., Choi, W., Koh, D., Hur, B., Kim, K., Kim, K., & Hur, M. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2016.09.004 · Cited by 12

Dolichoectasia: a brain arterial disease with an elusive treatment

Lopez-Navarro, E. R., Park, S., Willey, J. Z., & Gutierrez, J. (2022) · Neurological Sciences · doi:10.1007/s10072-022-06078-9 · Cited by 12

Pediatric Ischemic Stroke: Acute Management and Areas of Research

Titomanlio, L., Zanin, A., Sachs, P., Khaled, J., Elmaleh, M., Blanc, R., & Piotin, M. (2012) · The Journal of Pediatrics · doi:10.1016/j.jpeds.2012.09.018 · Cited by 12

Cypermethrin Induces the Activation of Rat Primary Microglia and Expression of Inflammatory Proteins

Mishra, S., Rajput, C., & Singh, M. P. (2020) · Journal of Molecular Neuroscience · doi:10.1007/s12031-020-01753-y · Cited by 11

Potent therapeutic targets for treatment of Alzheimer's disease: Amyloid degrading enzymes

Choi, H. S., Kim, E., Choi, J. Y., Park, E., & Lee, H. J. (2021) · Bulletin of the Korean Chemical Society · doi:10.1002/bkcs.12390 · Cited by 11

Plasma levels of matrix metalloproteinases in early psychosis, anxiety and depression: Evidence from the ALSPAC cohort

Ghelfi, L., Mongan, D., Susai, S. R., Föcking, M., Cotter, D., & Cannon, M. D. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.11.035 · Cited by 12

Protective effects of polydatin amphiphilic chitosan nanocarriers against an aluminum chloride-induced model of Alzheimer’s disease in rats: relevance to its anti-inflammatory and antioxidant effects

Zarneshan, S. N., Arkan, E., Kiani, A., Hosseini, S. Z., Abbaszadeh, F., & Fakhri, S. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03696-2 · Cited by 12

Ginsenoside Rb1 from Panax notoginseng Suppressed TNF-α-Induced Matrix Metalloproteinase-9 via the Suppression of Double-Strand RNA-Dependent Protein Kinase (PKR)/NF-κB Pathway

Sun, W., Yang, C. L.-H., Or, T. C. T., Luo, D., & Li, J. (2022) · Molecules · doi:10.3390/molecules27228050 · Cited by 11

Ghrelin ameliorates blood–brain barrier disruption during systemic hypoxia

Mohaddes, G., Abdolalizadeh, J., Babri, S., & Hossienzadeh, F. (2017) · Experimental Physiology · doi:10.1113/ep086068 · Cited by 10

Structural, computational and in silico studies of 4-bromo-3-flurobenzonitrile as anti-Alzheimer and anti-Parkinson agents

Hegde, V. N., Shyambhargav, J. S., Chethan, B. S., Leoma, M. B., & Lokanath, N. K. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2226755 · Cited by 10

Review Matrix

(2009)

Multiple Roles of Metalloproteinases in Neurological Disorders

Yang, Y. R., Hill, J. W., & Rosenberg, G. A. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385504-6.00006-3 · Cited by 62

Implication of matrix metalloproteinases in regulating neuronal disorder

Mukherjee, A. K., & Swarnakar, S. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3752-y · Cited by 27

The Role of Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in the Pathophysiology of Neurodegeneration: A Literature Study

Mroczko, B., Groblewska, M., & Barcikowska, M. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130647 · Cited by 61

Matrix Metalloproteinases, New Insights into the Understanding of Neurodegenerative Disorders

Kim, Y.-S., & Joh, T. H. (2012) · Biomolecules & Therapeutics · doi:10.4062/biomolther.2012.20.2.133 · Cited by 103