Matrix metalloproteinases and their multiple roles in neurodegenerative diseases

Matrix Metalloproteinase Inhibitors and Cancer—Trials and Tribulations

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Silent Brain Infarcts and the Risk of Dementia and Cognitive Decline

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Intracellular amyloid-β in Alzheimer's disease

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Tissue inhibitors of metalloproteinases: evolution, structure and function

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Mechanisms, challenges and opportunities in stroke

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Mechanism Of Cell Surface Activation Of 72-kDa Type IV Collagenase

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

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

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

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

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Nanoparticle-Based and Bioengineered Probes and Sensors to Detect Physiological and Pathological Biomarkers in Neural Cells

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Gelatinase activity imaged by activatable cell-penetrating peptides in cell-based and in vivo models of stroke

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Identification and Preliminary Validation of a Plasma Profile Associated with Cognitive Decline in Dementia and At-Risk Individuals: A Retrospective Cohort Analysis

Iulita, M. F., Ganesh, A., Pentz, R., Aguilar, L. F., Gubert, P., Ducatenzeiler, A., Christie, S., Wilcock, G. K., & Cuello, A. C. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-180970 · Cited by 45

Neuroprotective potential of isothiocyanates in an in vitro model of neuroinflammation

Latronico, T., Larocca, M., Milella, S., Fasano, A., Rossano, R., & Liuzzi, G. M. (2020) · Inflammopharmacology · doi:10.1007/s10787-020-00772-w · Cited by 43

Long-Term Neuromodulatory Effects of Repetitive Transcranial Magnetic Stimulation (rTMS) on Plasmatic Matrix Metalloproteinases (MMPs) Levels and Visuospatial Abilities in Mild Cognitive Impairment (MCI)

Cirillo, G., Pepe, R., Siciliano, M., Ippolito, D., Ricciardi, D., Stefano, M. D., Buonanno, D., Atripaldi, D., Abbadessa, S., Perfetto, B., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043231 · Cited by 42

MMP2 is a immunotherapy related biomarker and correlated with cancer-associated fibroblasts infiltrate in melanoma

Peng, K., Zhang, Y., Liu, D.-Y., & Chen, J. (2023) · Cancer Cell International · doi:10.1186/s12935-023-02862-5 · Cited by 42

Matrix metalloproteinase-9 controls proliferation of NG2+ progenitor cells immediately after spinal cord injury

Liu, H., & Shubayev, V. I. (2011) · Experimental Neurology · doi:10.1016/j.expneurol.2011.06.015 · Cited by 44

Critical role of calpain in spinal cord degeneration in P arkinson's disease

Samantaray, S., Knaryan, V. H., Shields, D. C., & Banik, N. L. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12374 · Cited by 42

Bazedoxifene protects cerebral autoregulation after traumatic brain injury and attenuates impairments in blood–brain barrier damage: involvement of anti-inflammatory pathways by blocking MAPK signaling

Lan, Y., Wang, X., Zou, Y., Xing, J., Lou, J., Zou, S., Ma, B., Ding, Y. P., & Zhang, B. (2019) · Inflammation Research · doi:10.1007/s00011-019-01217-z · Cited by 41

Pristimerin Inhibits MMP-9 Expression and Cell Migration Through Attenuating NOX/ROS-Dependent NF-κB Activation in Rat Brain Astrocytes Challenged with LPS

Yang, C.-C., Hsiao, L., Tseng, H., Kuo, C.-M., & Yang, C. (2020) · Journal of Inflammation Research · doi:10.2147/jir.s252659 · Cited by 42

Matrix metalloproteinases (MMPs) and their tissue inhibitors (TIMPs) in amyotrophic lateral sclerosis (ALS)

Łukaszewicz‐Zając, M., Mroczko, B., & Słowik, A. (2014) · Journal of Neural Transmission · doi:10.1007/s00702-014-1205-3 · Cited by 45

The multifaceted role of metalloproteinases in physiological and pathological conditions in embryonic and adult brains

Stefano, M. E. D., & Herrero, M. T. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.08.002 · Cited by 42

Mixed dementia: Neglected clinical entity or nosographic artifice?

Fierini, F. (2019) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2019.116662 · Cited by 46

Ten years of proteomics in multiple sclerosis

Farias, A. S., Pradella, F., Schmitt, A., Santos, L. M. B., & Martins‐de‐Souza, D. (2014) · PROTEOMICS · doi:10.1002/pmic.201300268 · Cited by 40

Influence of plasma matrix metalloproteinase levels on longitudinal changes in Alzheimer's disease (AD) biomarkers and cognitive function in patients with mild cognitive impairment due to AD registered in the Alzheimer's Disease Neuroimaging Initiative database

Abe, K., Chiba, Y., Hattori, S., Yoshimi, A., Asami, T., Katsuse, O., Suda, A., & Hishimoto, A. (2020) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2020.116989 · Cited by 41

Role of Rho kinase in lysophosphatidic acid-induced altering of blood-brain barrier permeability

Yu, Y., Qin, J., Liu, M., RUAN, Q., Li, Y., & Zhang, Z. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1618 · Cited by 40

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 International Edition · doi:10.1002/anie.201209286 · Cited by 40

Vascular Dementia: From Pathophysiology to Therapeutic Frontiers

Yang, H. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14186611 · Cited by 48

Matrix metalloproteinase‐9 and intercellular adhesion molecule 1 are powerful staging markers for human African trypanosomiasis

Hainard, A., Tiberti, N., Robin, X., Ngoyi, D. M., Matovu, E., Enyaru, J., Müller, M., Turck, N., Ndung’u, J. M., Lejon, V., et al. (2010) · Tropical Medicine & International Health · doi:10.1111/j.1365-3156.2010.02642.x · Cited by 39

Merging Allosteric and Active Site Binding Motifs: De novo Generation of Target Selectivity and Potency via Natural‐Product‐Derived Fragments

Lanz, J., & Riedl, R. (2014) · ChemMedChem · doi:10.1002/cmdc.201402478 · Cited by 38

Inhibition of matrix metalloproteinases attenuates brain damage in experimental meningococcal meningitis

Ricci, S., Grandgirard, D., Wenzel, M., Braccini, T., Salvatore, P., Oggioni, M. R., Leib, S. L., & Koedel, U. (2014) · BMC Infectious Diseases · doi:10.1186/s12879-014-0726-6 · Cited by 40

Ectodomain shedding of the receptor for advanced glycation end products: a novel therapeutic target for Alzheimer’s disease

Zhang, L., Postina, R., & Wang, Y. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0121-4 · Cited by 40

Recent insights into natural product inhibitors of matrix metalloproteinases

Kumar, G. B., Nair, B. G., Perry, J. J. P., & Martin, D. B. C. (2019) · MedChemComm · doi:10.1039/c9md00165d · Cited by 39

Insoluble Vascular Amyloid Deposits Trigger Disruption of the Neurovascular Unit in Alzheimer’s Disease Brains

Soto-Rojas, L. O., Campa-Córdoba, B. B., Harrington, C. R., Salas‐Casas, A., Hernándes‐Alejandro, M., Villanueva‐Fierro, I., Bravo-Muñoz, M., Garcés‐Ramírez, L., de la Cruz‐López, F., Ontiveros‐Torres, M. Á., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22073654 · Cited by 41

GDF15/MIC1 and MMP9 Cerebrospinal Fluid Levels in Parkinson’s Disease and Lewy Body Dementia

Maetzler, W., Deleersnijder, W., Hanssens, V., Bernard, A., Brockmann, K., Marquetand, J., Wurster, I., Rattay, T. W., Roncoroni, L., Schaeffer, E., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0149349 · Cited by 36

Neuroprotective effects of carvacrol against cadmium-induced neurotoxicity in rats: role of oxidative stress, inflammation and apoptosis

Yıldız, M. O., Çelik, H., Çağlayan, C., Genç, A., Doğan, T., & Satıcı, E. (2022) · Metabolic Brain Disease · doi:10.1007/s11011-022-00945-2 · Cited by 39

Immune response and pathogen invasion at the choroid plexus in the onset of cerebral toxoplasmosis

Figueiredo, C. A., Steffen, J., Morton, L., Arumugam, S., Liesenfeld, O., Deli, M. A., Kröger, A., Schüler, T., & Dunay, I. R. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02370-1 · Cited by 37

Matrix metalloproteinases as promising regulators of axonal regrowth in the injured adult zebrafish retinotectal system

Lemmens, K., Bollaerts, I., Bhumika, S., Groef, L. D., houcke, J. V., Darras, V., Hove, I. V., & Moons, L. (2015) · The Journal of Comparative Neurology · doi:10.1002/cne.23920 · Cited by 38

Matrix metalloproteinase (MMP)-2 gene polymorphisms affect circulating MMP-2 levels in patients with migraine with aura

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Impact of Manganese Neurotoxicity on MMP-9 Production and Superoxide Dismutase Activity in Rat Primary Astrocytes. Effect of Resveratrol and Therapeutical Implications for the Treatment of CNS Diseases

Latronico, T., Branà, M. T., Merra, E., Fasano, A., Bari, G. D., Casalino, E., & Liuzzi, G. M. (2013) · Toxicological Sciences · doi:10.1093/toxsci/kft146 · Cited by 38

MMP-3 Deficiency Alleviates Endotoxin-Induced Acute Inflammation in the Posterior Eye Segment

Hove, I. V., Lefevere, E., Groef, L. D., Sergeys, J., Salinas‐Navarro, M., Libert, C., Vandenbroucke, R. E., & Moons, L. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17111825 · Cited by 37

Lipopolysaccharide-Induced Matrix Metalloproteinase-9 Expression Associated with Cell Migration in Rat Brain Astrocytes

Yang, C.-C., Lin, C.-C., Hsiao, L.-D., Kuo, J., Tseng, H., & Yang, C.-M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010259 · Cited by 35

Validation of biomarkers in subcortical ischaemic vascular disease of the Binswanger type: approach to targeted treatment trials

Rosenberg, G. A., Prestopnik, J., Adair, J. C., Huisa, B. N., Knoefel, J. E., Caprihan, A., Gasparovic, C., Thompson, J. F., Erhardt, E. B., & Schrader, R. (2015) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2014-309421 · Cited by 39

TRIF-Mediated TLR3 and TLR4 Signaling Is Negatively Regulated by ADAM15

Ahmed, S., Maratha, A., Butt, A. Q., Shevlin, E., & Miggin, S. M. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201630 · Cited by 38

Metal complexes and metalloproteases: targeting conformational diseases

Grasso, G., & Bonnet, S. A. (2014) · Metallomics · doi:10.1039/c4mt00076e · Cited by 37

Elevated levels of plasma homocysteine, deficiencies in dietary folic acid and uracil–DNA glycosylase impair learning in a mouse model of vascular cognitive impairment

Jadavji, N. M., Farr, T. D., Lips, J., Khalil, A. A., Boehm‐Sturm, P., Foddis, M., Harms, C., Füchtemeier, M., & Dirnagl, U. (2015) · Behavioural Brain Research · doi:10.1016/j.bbr.2015.01.040 · Cited by 36

Substrate stiffness regulated migration and invasion ability of adenoid cystic carcinoma cells via RhoA/ ROCK pathway

Zhao, D., Li, Q., Liu, M., Ma, W., Zhou, T., Xue, C., & Cai, X. (2018) · Cell Proliferation · doi:10.1111/cpr.12442 · Cited by 37

Strain differences in the effects of chronic corticosterone exposure in the hippocampus

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Matrix Metalloproteinase-8 is a Novel Pathogenetic Factor in Focal Cerebral Ischemia

Han, J. E., Lee, E., Moon, E., Ryu, J. H., Choi, J. W., & Kim, H.-S. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8996-y · Cited by 36

Sex differences in Alzheimer’s disease: plasma MMP-9 and markers of disease severity

Tsiknia, A. A., Sundermann, E. E., Reas, E. T., Edland, S. D., Brewer, J. B., Galasko, D. R., Banks, S. J., & Initiative, A. D. N. (2022) · Alzheimer s Research & Therapy · doi:10.1186/s13195-022-01106-4 · Cited by 39

Type IV collagen induces expression of thrombospondin‐1 that is mediated by integrin α1β1 in astrocytes

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Interactions between the extracellular matrix and inflammation during viral myocarditis

Papageorgiou, A., & Heymans, S. R. B. (2011) · Immunobiology · doi:10.1016/j.imbio.2011.07.011 · Cited by 36

Mechanotransduction: Exploring New Therapeutic Avenues in Central Nervous System Pathology

Rocha, D. N., Carvalho, E. D., Relvas, J. B., Oliveira, M. J., & Pêgo, A. P. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.861613 · Cited by 41

Redox-active endosomes mediate α5β1 integrin signaling and promote chondrocyte matrix metalloproteinase production in osteoarthritis

Miao, M. Z., Su, Q. P., Cui, Y., Bahnson, E. M., Li, G., Wang, M., Yang, Y., Collins, J. A., Wu, D., Gu, Q., et al. (2023) · Science Signaling · doi:10.1126/scisignal.adf8299 · Cited by 37

Zinc Metalloproteinases and Amyloid Beta-Peptide Metabolism: The Positive Side of Proteolysis in Alzheimer's Disease

Gough, M., Parr-Sturgess, C. A., & Parkin, E. T. (2010) · Biochemistry Research International · doi:10.1155/2011/721463 · Cited by 37

Cannabidiol affects the expression of genes involved in zinc homeostasis in BV-2 microglial cells

Juknat, A., Rimmerman, N., Levy, R., Vogel, Z., & Kozela, E. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.12.002 · Cited by 35

Biodegradable bilayer hydrogel membranes loaded with bazedoxifene attenuate blood–spinal cord barrier disruption via the NF-κB pathway after acute spinal cord injury

Wang, X., Baokun, Z., Chen, Z., Qiang, S., Yang, E., Jianguang, X., & Xiaofeng, L. (2023) · Acta Biomaterialia · doi:10.1016/j.actbio.2023.01.056 · Cited by 34

Protease detection in the biosensor era: A review

Rai, P., Hoba, S. N., Buchmann, C., Subirana-Slotos, R. J., Kersten, C., Schirmeister, T., Endres, K., Bufe, B., & Tarasov, A. (2023) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2023.115788 · Cited by 37

Shared Molecular Signatures Across Neurodegenerative Diseases and Herpes Virus Infections Highlights Potential Mechanisms for Maladaptive Innate Immune Responses

Costa, A. C., Madsen, H., & Brown, J. R. (2019) · Scientific Reports · doi:10.1038/s41598-019-45129-8 · Cited by 36

Serum matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 levels in patients with tick-borne encephalitis

Palus, M., Žampachová, E., Elsterová, J., & Růžek, D. (2013) · Journal of Infection · doi:10.1016/j.jinf.2013.09.028 · Cited by 34

Brain ischaemia induces shedding of a BDNF ‐scavenger ectodomain from TrkB receptors by excitotoxicity activation of metalloproteinases and γ‐secretases

Tejeda, G. S., Ayuso‐Dolado, S., Arbeteta, R., Esteban-Ortega, G. M., Vidaurre, Ó. G., & Díaz‐Guerra, M. (2015) · The Journal of Pathology · doi:10.1002/path.4684 · Cited by 34

Suppression of MMP-9 Expression in Brain Microvascular Endothelial Cells (BMVEC) Using a Gold Nanorod (GNR)-siRNA Nanoplex

Mahajan, S. D., Aalinkeel, R., Reynolds, J. L., Nair, B. B., Sykes, D. E., Bonoiu, A. C., Roy, I., Yong, K., Law, W., Bergey, E. J., et al. (2011) · Immunological Investigations · doi:10.3109/08820139.2011.604863 · Cited by 32

Leukoaraiosis as an outcome predictor in the acute and subacute phases of stroke

Fierini, F., Poggesi, A., & Pantoni, L. (2017) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2017.1371013 · Cited by 33

A systematic review on potential mechanisms of minocycline in kidney diseases

Haghi‐Aminjan, H., Asghari, M. H., Goharbari, M. H., & Abdollahi, M. R. (2017) · Pharmacological Reports · doi:10.1016/j.pharep.2017.02.001 · Cited by 32

3,4-Methylenedioxymethamphetamine (MDMA, ecstasy) produces edema due to BBB disruption induced by MMP-9 activation in rat hippocampus

Pérez‐Hernández, M., Fernández-Valle, M. E., Rubio‐Araiz, A., Vidal, R., Gutiérrez‐López, M. D., O’Shea, E., & Colado, M. I. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.03.019 · Cited by 33

The MMP-2/TIMP-2 System in Alzheimer Disease

Wang, H., Huang, L., Wu, L., Lan, J., Feng, X., Li, P., & Peng, Y. (2020) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527319666200812223007 · Cited by 32

Multiple Particle Tracking Detects Changes in Brain Extracellular Matrix and Predicts Neurodevelopmental Age

McKenna, M., Shackelford, D. B., Pontes, C., Ball, B. K., Gao, T., & Nance, E. A. (2021) · ACS Nano · doi:10.1021/acsnano.1c00394 · Cited by 32

The uniqueness and superiority of energy utilization in yaks compared with cattle in the highlands: A review

Liu, X., Gao, J., Liu, S., Cheng, Y., Hao, L., Liu, S., & Zhu, W. (2022) · Animal nutrition · doi:10.1016/j.aninu.2022.09.011 · Cited by 36

MMPs: a novel drug target for schizophrenia

Chopra, K., Baveja, A., & Kuhad, A. (2014) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2014.957672 · Cited by 32

Matrix metalloproteinases and their pathological upregulation in multiple sclerosis: an overview

Javaid, M. A., Abdallah, M., Ahmed, A. S., & Sheikh, Z. (2013) · Acta Neurologica Belgica · doi:10.1007/s13760-013-0239-x · Cited by 32

Metalloproteinase alterations in the bone marrow of ALS patients

Bossolasco, P., Cova, L., Calzarossa, C., Servida, F., Mencacci, N. E., Onida, F., Polli, E. E., Deliliers, G. L., & Silani, V. (2010) · Journal of Molecular Medicine · doi:10.1007/s00109-009-0584-7 · Cited by 32

Metalloproteinases and Metalloproteinase Inhibitors in Age-Related Diseases

Gargiulo, S., Gamba, P., Poli, G., & Leonarduzzi, G. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113196660701 · Cited by 34

Fluorometric immunocapture assay for the specific measurement of matrix metalloproteinase-9 activity in biological samples: application to brain and plasma from rats with ischemic stroke

Hawkins, K. E., DeMars, K. M., Yang, C., Rosenberg, G. A., & Candelario‐Jalil, E. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-14 · Cited by 31

Interaction between genetic factors, Porphyromonas gingivalis and microglia to promote Alzheimer’s disease

Olsen, I., & Singhrao, S. K. (2020) · Journal of Oral Microbiology · doi:10.1080/20002297.2020.1820834 · Cited by 34

Thrombospondin‐4 promotes bladder cancer cell migration and invasion via MMP2 production

Chou, K., Chang, A., Ho, C., Tsai, T., Chen, H., Chen, P., & Hwang, T. I. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16463 · Cited by 30

Matrix Metalloproteinases and Glaucoma

Kim, M. H., & Lim, S. (2022) · Biomolecules · doi:10.3390/biom12101368 · Cited by 31

Lanthanum Chloride Impairs the Blood-Brain Barrier Integrity by Reduction of Junctional Proteins and Upregulation of MMP-9 in Rats

Wu, J., Yang, J., Lu, X., Jin, C., Wu, S., Zhang, L., Hu, X., Ma, H., & Cai, Y. (2018) · Biological Trace Element Research · doi:10.1007/s12011-018-1402-2 · Cited by 33

The neurovascular unit in healthy and injured spinal cord

Zhou, R., Li, J., Wang, R., Chen, Z., & Zhou, F. (2023) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x231172008 · Cited by 31

Solulin reduces infarct volume and regulates gene-expression in transient middle cerebral artery occlusion in rats

Ryang, Y.-M., Dang, J., Kipp, M., Petersen, K.-U., Fahlenkamp, A. V., Gempt, J., Wesp, D., Rossaint, R., Beyer, C., & Coburn, M. (2011) · BMC Neuroscience · doi:10.1186/1471-2202-12-113 · Cited by 30

Fisetin inhibits epidermal growth factor-induced migration of ARPE-19 cells by suppression of AKT activation and Sp1-dependent MMP-9 expression.

Lin, H., Chen, Y., Wang, K., Chien, H., Hsieh, Y., & Yang, S. (2017) · PubMed Central · Cited by 30

Increased MMP-3 and CTGF expression during lipopolysaccharide-induced dopaminergic neurodegeneration

McClain, J. A., Phillips, L. L., & Fillmore, H. L. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.05.044 · Cited by 30

TIMP-1 Protects Tight Junctions of Brain Endothelial Cells From MMP-Mediated Degradation

Ahmadighadykolaei, H., Lambert, J. A., & Raeeszadeh‐Sarmazdeh, M. (2023) · Pharmaceutical Research · doi:10.1007/s11095-023-03593-y · Cited by 30

Cerebral Microbleeds Associate with Brain Endothelial Cell Activation-Dysfunction and Blood–Brain Barrier Dysfunction/Disruption with Increased Risk of Hemorrhagic and Ischemic Stroke

Hayden, M. R. (2024) · Biomedicines · doi:10.3390/biomedicines12071463 · Cited by 34

The mechanics of the retina: Müller glia role on retinal extracellular matrix and modelling

Prieto-López, L., Pereiro, X., & Vecino, E. (2024) · Frontiers in Medicine · doi:10.3389/fmed.2024.1393057 · Cited by 37

Effects of progesterone vs. dexamethasone on brain oedema and inflammatory responses following experimental brain resection

Xu, F., Sun, S., Ho, A. S.-W., Lee, D. P. H., Kiang, K. M. Y., Zhang, X., Wang, A. M., Wu, E. X., Lui, W., Liu, B., et al. (2014) · Brain Injury · doi:10.3109/02699052.2014.943289 · Cited by 29

Matrix metalloproteinases in the mouse retina: a comparative study of expression patterns and MMP antibodies

Groef, L. D., Andries, L., Lemmens, K., Hove, I. V., & Moons, L. (2015) · BMC Ophthalmology · doi:10.1186/s12886-015-0176-y · Cited by 29

Serum metalloproteinase 9 levels increase after generalized tonic-clonic seizures

Cudna, A., Jopowicz, A., Mierzejewski, P., & Kurkowska‐Jastrzębska, I. (2016) · Epilepsy Research · doi:10.1016/j.eplepsyres.2016.11.006 · Cited by 30

Genome-wide RNA-seq of iPSC-derived motor neurons indicates selective cytoskeletal perturbation in Brown–Vialetto disease that is partially rescued by riboflavin

Rizzo, F., Ramirez, A., Compagnucci, C., Salani, S., Melzi, V., Bordoni, A., Fortunato, F., Niceforo, A., Bresolin, N., Comi, G. P., et al. (2017) · Scientific Reports · doi:10.1038/srep46271 · Cited by 29

Plasma proteome in multiple sclerosis disease progression

Malekzadeh, A., Leurs, C. E., van Wieringen, W. N., Steenwijk, M. D., Schoonheim, M. M., Amann, M., Naegelin, Y., Kühle, J., Killestein, J., & Teunissen, C. E. (2019) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.771 · Cited by 29

CSF MicroRNAs Reveal Impairment of Angiogenesis and Autophagy in Parkinson Disease

Fowler, A. J., Ahn, J., Hebron, M., Chiu, T., Ayoub, R., Mulki, S., Ressom, H., Torres-Yaghi, Y., Wilmarth, B., Pagan, F. L., et al. (2021) · Neurology Genetics · doi:10.1212/nxg.0000000000000633 · Cited by 29

Sex-Related Differences of Matrix Metalloproteinases (MMPs): New Perspectives for These Biomarkers in Cardiovascular and Neurological Diseases

Trentini, A., Manfrinato, M. C., Castellazzi, M., & Bellini, T. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12081196 · Cited by 30

Biomarkers and location of atherosclerosis: Matrix metalloproteinase-2 may be related to intracranial atherosclerosis

Jeon, S., Chun, S., Choi‐Kwon, S., Chi, H., Nah, H., Kwon, S. U., Kim, W.-K., & Kim, J. S. (2012) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2012.04.013 · Cited by 29

PGE2/EP4 signaling in peripheral immune cells promotes development of experimental autoimmune encephalomyelitis

Schiffmann, S., Weigert, A., Männich, J., Eberle, M., Birod, K., Häußler, A., Ferreirós, N., Schreiber, Y., Kunkel, H., Grez, M., et al. (2013) · Biochemical Pharmacology · doi:10.1016/j.bcp.2013.12.006 · Cited by 29

From the “little brain” gastrointestinal infection to the “big brain” neuroinflammation: A proposed fast axonal transport pathway involved in multiple sclerosis

Deretzi, G., Kountouras, J., Grigoriadis, N., Zavos, C., Chatzigeorgiou, S., Koutlas, E., & Tsiptsios, I. (2009) · Medical Hypotheses · doi:10.1016/j.mehy.2009.04.021 · Cited by 29

Matrix metalloproteinases and epileptogenesis

Ikonomidou, C. (2014) · Molecular and Cellular Pediatrics · doi:10.1186/s40348-014-0006-y · Cited by 28

Matrix Metalloproteinases During Axonal Regeneration, a Multifactorial Role from Start to Finish

Andries, L., Hove, I. V., Moons, L., & Groef, L. D. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9801-x · Cited by 27

Treatment with Trichuris suis soluble products during monocyte‐to‐macrophage differentiation reduces inflammatory responses through epigenetic remodeling

Hoeksema, M. A., Laan, L. C., Postma, J. J., Cummings, R. D., de Winther, M. P. J., Dijkstra, C. D., van Die, I., & Kooij, G. (2016) · The FASEB Journal · doi:10.1096/fj.201600343r · Cited by 27

Vesicular systems employing natural substances as promising drug candidates for MMP inhibition in glioblastoma: A nanotechnological approach

Agarwal, S., Muniyandi, P., Maekawa, T., & Kumar, D. S. (2018) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2018.09.033 · Cited by 27

Carnosine Protects against Cerebral Ischemic Injury by Inhibiting Matrix-Metalloproteinases

Kim, E.-H., Kim, E. S., Shin, D., Kim, D., Choi, S., Shin, Y., Kim, K.-A., Noh, D., Çağlayan, A. B., Rajanikant, G. K., et al. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147495 · Cited by 28

Metalloproteinases and their inhibitors in neurological disease

Lopez-Navarro, E. R., & Gutierrez, J. (2021) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-021-02188-x · Cited by 26

Volatile Anesthetics Reduce Biochemical Markers of Brain Injury and Brain Magnesium Disorders in Patients Undergoing Coronary Artery Bypass Graft Surgery

Dąbrowski, W., Rzecki, Z., Czajkowski, M., Piłat, J., Wacinski, P. J., Kotlińska-Hasiec, E., Sztanke, M., Sztanke, K., Stążka, K., & Pasternak, K. (2011) · Journal of Cardiothoracic and Vascular Anesthesia · doi:10.1053/j.jvca.2011.10.014 · Cited by 28

Microbleeds in ischemic stroke are associated with lower serum adiponectin and higher soluble E-selectin levels

Huang, Z., Yin, Q., Sun, W., Zhu, W., Li, Y., Liu, W., Xiao, L., Duan, Z., Cai, Q., Liu, D., et al. (2013) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2013.07.2513 · Cited by 28

TIMP-1 resistant matrix metalloproteinase-9 is the predominant serum active isoform associated with MRI activity in patients with multiple sclerosis

Trentini, A., Manfrinato, M. C., Castellazzi, M., Tamborino, C., Roversi, G., Volta, C. A., Baldi, E., Tola, M. R., Granieri, E., Dallocchio, F., et al. (2015) · Multiple Sclerosis Journal · doi:10.1177/1352458514560925 · Cited by 29

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

Pretreatment levels of the fatty acid handling proteins H-FABP and CD36 predict response to olanzapine in recent-onset schizophrenia patients

Tomasik, J., Schwarz, E., Lago, S. G., Rothermundt, M., Leweke, F. M., van Beveren, N. J. M., Guest, P. C., Rahmoune, H., Steiner, J. H., & Bahn, S. (2015) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2015.10.019 · Cited by 27

New phosphazine and phosphazide derivatives as multifunctional ligands targeting acetylcholinesterase and β-Amyloid aggregation for treatment of Alzheimer's disease

El‐Sayed, N. F., El‐Hussieny, M., Ewies, E. F., Fouad, M. A., & Boulos, L. S. (2019) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2019.103499 · Cited by 27

Brain organoids for hypoxic-ischemic studies: from bench to bedside

Gaston-Breton, R., Maïza, A., Hamoudi, R., Stonestreet, B. S., & Mabondzo, A. M. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04951-0 · Cited by 29

3,4-Methylenedioxymethamphetamine (MDMA, ecstasy) disrupts blood-brain barrier integrity through a mechanism involving P2X7 receptors

Rubio‐Araiz, A., Pérez‐Hernández, M., Urrutia, A. A., Porcu, F., Borcel, É., Gutiérrez‐López, M. D., O’Shea, E., & Colado, M. I. (2014) · The International Journal of Neuropsychopharmacology · doi:10.1017/s1461145714000145 · Cited by 27

Matrix Metalloproteinase-Mediated Neuroinflammation in Vascular Cognitive Impairment of the Binswanger Type

Rosenberg, G. A. (2016) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0277-4 · Cited by 27

Matrix Metalloproteinase-9 Expression in Calcified Human Aortic Valves

Perrotta, I. D., Sciangula, A., Aquila, S., & Mazzulla, S. (2014) · Applied immunohistochemistry & molecular morphology · doi:10.1097/pai.0000000000000144 · Cited by 27

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