MMP-3 Contributes to Nigrostriatal Dopaminergic Neuronal Loss, BBB Damage, and Neuroinflammation in an MPTP Mouse Model of Parkinson’s Disease

Astrocyte-endothelial interactions at the blood-brain barrier

Abbott, N. J., Rönnbäck, L., & Hansson, E. (2006) · Nature Reviews Neuroscience · doi:10.1038/nrn1824 · Cited by 5,595 · see citing works

Microglia-mediated neurotoxicity: uncovering the molecular mechanisms

Block, M. L., Zecca, L., & Hong, J.-S. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2038 · Cited by 4,110 · see citing works

The Blood-Brain Barrier in Health and Chronic Neurodegenerative Disorders

Zlokovic, B. V. (2008) · Neuron · doi:10.1016/j.neuron.2008.01.003 · Cited by 3,280 · see citing works

Unbiased stereological estimation of the total number of neurons in the subdivisions of the rat hippocampus using the optical fractionator

West, M. J., Slomianka, L., & Gundersen, H. J. G. (1991) · The Anatomical Record · doi:10.1002/ar.1092310411 · Cited by 2,994 · see citing works

The blood-brain barrier/neurovascular unit in health and disease

Hawkins, B. T., & Davis, T. P. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.2.4 · Cited by 2,661 · see citing works

Neuroinflammation in Parkinson’s disease: A target for neuroprotection?

Hirsch, E. C., & Hunot, S. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70062-6 · Cited by 1,984 · see citing works

Blockade of Microglial Activation Is Neuroprotective in the 1-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine Mouse Model of Parkinson Disease

Wu, D. C., Jackson-Lewis, V., Vila, M., Tieu, K., Teismann, P., Vadseth, C., Choi, D.-K., Ischiropoulos, H., & Przedborski, S. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01763.2002 · Cited by 1,183 · see citing works

Infiltration of CD4+ lymphocytes into the brain contributes to neurodegeneration in a mouse model of Parkinson disease

Brochard, V., Combadière, B., Prigent, A., Laouar, Y., Perrin, A., Beray-Berthat, V., Bonduelle, O., Alvarez-Fischer, D., Callebert, J., Launay, J.-M., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci36470 · Cited by 1,172 · see citing works

Neuroinflammation in Parkinson's disease: Its role in neuronal death and implications for therapeutic intervention

Tansey, M. G., & Goldberg, M. S. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.11.004 · Cited by 1,045 · see citing works

Blood–brain barrier dysfunction in parkinsonian midbrain in vivo

Kortekaas, R., Leenders, K. L., van Oostrom, J. C. H., Vaalburg, W., Bart, J., Willemsen, A. T. M., & Hendrikse, N. H. (2005) · Annals of Neurology · doi:10.1002/ana.20369 · Cited by 733 · see citing works

The Blood-Brain Barrier in Brain Homeostasis and Neurological Diseases

Weiss, N., Miller, F., Cazaubon, S., & Couraud, P.-O. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.022 · Cited by 731 · see citing works

Microglia, major player in the brain inflammation: their roles in the pathogenesis of Parkinson's disease

Kim, Y. S., & Joh, T. H. (2006) · Experimental & Molecular Medicine · doi:10.1038/emm.2006.40 · Cited by 655 · see citing works

Diagnosis and treatment of Parkinson disease: molecules to medicine

Savitt, J. M. (2006) · Journal of Clinical Investigation · doi:10.1172/jci29178 · Cited by 649 · see citing works

NADPH oxidase mediates oxidative stress in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine model of Parkinson's disease

Wu, D., Teismann, P., Tieu, K., Vila, M., Jackson-Lewis, V. R., Ischiropoulos, H., & Przedborski, S. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0937239100 · Cited by 634 · see citing works

Neuroinflammatory processes in Parkinson's disease

Hunot, S., & Hirsch, É. C. (2003) · Annals of Neurology · doi:10.1002/ana.10481 · Cited by 399 · see citing works

Blood–Brain Barrier Pathology in Alzheimer's and Parkinson's Disease: Implications for Drug Therapy

Desai, B. S., Monahan, A. J., Carvey, P. M., & Hendey, B. (2007) · Cell Transplantation · doi:10.3727/000000007783464731 · Cited by 339 · see citing works

Neuroinflammatory processes in Parkinson's disease

Hirsch, É. C., Hunot, S., & Hartmann, A. (2005) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2004.10.013 · Cited by 298 · see citing works

Effects of extracellular matrix‐degrading proteases matrix metalloproteinases 3 and 9 on spatial learning and synaptic plasticity

Meighan, S. E., Meighan, P. C., Choudhury, P., Davis, C. J., Olson, M. L., Zornes, P. A., Wright, J. W., & Harding, J. W. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03565.x · Cited by 285 · see citing works

Ablation of the Inflammatory Enzyme Myeloperoxidase Mitigates Features of Parkinson's Disease in Mice

Choi, D., Pennathur, S., Perier, C., Tieu, K., Teismann, P., Wu, D.-C., Jackson-Lewis, V. R., Vila, M., Vonsattel, J., Heinecke, J. W., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0970-05.2005 · Cited by 284 · see citing works

Matrix Metalloproteinase-3: A Novel Signaling Proteinase from Apoptotic Neuronal Cells That Activates Microglia

Kim, Y.-S., Kim, S. S., Cho, J., Choi, D.-H., Hwang, O., Shin, D., Hong, S.-C., Beal, M., & Joh, T. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4346-04.2005 · Cited by 272 · see citing works

Exendin-4 protects dopaminergic neurons by inhibition of microglial activation and matrix metalloproteinase-3 expression in an animal model of Parkinson's disease

Kim, S., Moon, M., & Park, S. (2009) · Journal of Endocrinology · doi:10.1677/joe-09-0132 · Cited by 263 · see citing works

Blood-brain barrier disruption by stromelysin-1 facilitates neutrophil infiltration in neuroinflammation.

Gurney, K., Estrada, E. Y., & Rosenberg, G. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.02.006 · Cited by 243 · see citing works

Proteolytic Cleavage of Extracellular Secreted α-Synuclein via Matrix Metalloproteinases

Sung, J. Y., Park, S., Lee, C.-H., Um, J. W., Lee, H. J., Kim, J., Oh, Y. J., Lee, S., Paik, S. R., & Chung, K. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503341200 · Cited by 238 · see citing works

Blood vessels change in the mesencephalon of patients with Parkinson's disease

Faucheux, B. A., Agid, Y., Hirsch, É. C., & Bonnet, A.-M. (1999) · The Lancet · doi:10.1016/s0140-6736(99)00641-8 · Cited by 218 · see citing works

6-Hydroxydopamine-induced alterations in blood-brain barrier permeability

Carvey, P. M., Zhao, C. H., Hendey, B., Lum, H., Trachtenberg, J., Desai, B. S., Snyder, J., Zhu, Y. G., & Ling, Z. D. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04281.x · Cited by 218 · see citing works

Neuroprotective Effect of Ghrelin in the 1-Methyl-4-Phenyl-1,2,3,6-Tetrahydropyridine Mouse Model of Parkinson’s Disease by Blocking Microglial Activation

Moon, M., Kim, H. G., Hwang, L., Seo, J.-H., Kim, S., Hwang, S., Kim, S., Lee, D., Chung, H., Oh, M. S., et al. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9037-x · Cited by 203 · see citing works

A pivotal role of matrix metalloproteinase‐3 activity in dopaminergic neuronal degeneration via microglial activation

Kim, Y. S., Choi, D. H., Block, M. L., Lorenzl, S., Yang, L., Kim, Y., Sugama, S., Cho, B. P., Hwang, O., Browne, S. E., et al. (2006) · The FASEB Journal · doi:10.1096/fj.06-5865com · Cited by 199 · see citing works

Caffeine protects against MPTP‐induced blood‐brain barrier dysfunction in mouse striatum

Chen, X., Lan, X., Roche, I., Liu, R., & Geiger, J. D. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05697.x · Cited by 189 · see citing works

Biochemistry of postmortem brains in Parkinson’s disease: historical overview and future prospects

Nagatsu, T., & Sawada, M. (2007) · Springer eBooks · doi:10.1007/978-3-211-73574-9_14 · Cited by 185 · see citing works

TNF-α knockout and minocycline treatment attenuates blood–brain barrier leakage in MPTP-treated mice

Zhao, C., Ling, Z., Newman, M. B., Bhatia, A., & Carvey, P. M. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.11.012 · Cited by 183 · see citing works

Paroxetine Prevents Loss of Nigrostriatal Dopaminergic Neurons by Inhibiting Brain Inflammation and Oxidative Stress in an Experimental Model of Parkinson’s Disease

Chung, Y. C., Kim, S. R., & Jin, B. K. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000208 · Cited by 159 · see citing works

Increased blood-cerebrospinal fluid transfer of albumin in advanced Parkinson’s disease

Pisani, V., Stefani, A., Pierantozzi, M., Natoli, S., Stanzione, P., Franciotta, D., & Pisani, A. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-188 · Cited by 158 · see citing works

The role of neuroinflammation on the pathogenesis of Parkinson's disease

Chung, Y. C., Ko, H. W., Bok, E., Park, E. S., Huh, S. H., Nam, J. H., & Jin, B. K. (2010) · BMB Reports · doi:10.5483/bmbrep.2010.43.4.225 · Cited by 148 · see citing works

Blood–brain barrier disruption induces <i>in vivo</i> degeneration of nigral dopaminergic neurons

Rite, I., Machado, A., Cano, J., & Venero, J. L. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04567.x · Cited by 147 · see citing works

Mesenchymal stem cell transplantation attenuates blood brain barrier damage and neuroinflammation and protects dopaminergic neurons against MPTP toxicity in the substantia nigra in a model of Parkinson's disease.

Chao, Y.-X., He, B., & Tay, S. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.09.003 · Cited by 133 · see citing works

Neuroinflammation and Peripheral Immune Infiltration in Parkinson's Disease: An Autoimmune Hypothesis

Monahan, A. J., Warren, M., & Carvey, P. M. (2008) · Cell Transplantation · doi:10.3727/096368908784423328 · Cited by 126 · see citing works

Fluoxetine prevents MPTP-induced loss of dopaminergic neurons by inhibiting microglial activation

Chung, Y. C., Kim, S. R., Park, J. Y., Chung, E. S., Park, K. W., Won, S.-Y., Bok, E., Jin, M., Park, E. S., & Yoon, S.-H. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.01.043 · Cited by 126 · see citing works

A novel intracellular role of matrix metalloproteinase‐3 during apoptosis of dopaminergic cells

Choi, D. H., Kim, E., Son, H. J., JOH, T. H., Kim, Y. S., Kim, D., Beal, M. F., & Hwang, O. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05399.x · Cited by 124 · see citing works

Cannabinoid Receptor Type 1 Protects Nigrostriatal Dopaminergic Neurons against MPTP Neurotoxicity by Inhibiting Microglial Activation

Chung, Y. C., Bok, E., Huh, S. H., Park, J., Yoon, S., Kim, S. R., Kim, Y., Maeng, S., Park, S. H., & Jin, B. K. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1102435 · Cited by 123 · see citing works

Role of Matrix Metalloproteinase 3-mediated α-Synuclein Cleavage in Dopaminergic Cell Death

Choi, D.-H., Kim, Y.-J., Kim, Y.-G., Joh, T. H., Beal, M. F., & Kim, Y.-S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.222430 · Cited by 123 · see citing works

Role of matrix metalloproteinase-3 in neurodegeneration

Kim, E., & Hwang, O. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07082.x · Cited by 114 · see citing works

Matrix metalloproteinase‐3 in the central nervous system: a look on the bright side

Hove, I. V., Lemmens, K., de Velde, S. V., Verslegers, M., & Moons, L. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07900.x · Cited by 112 · see citing works

Brain-resident microglia predominate over infiltrating myeloid cells in activation, phagocytosis and interaction with T-lymphocytes in the MPTP mouse model of Parkinson disease.

Depboylu, C., Stricker, S., Ghobril, J.-P., Oertel, W., Priller, J., & Höglinger, G. (2012) · Experimental Neurology · doi:10.1016/j.expneurol.2012.08.020 · Cited by 94 · see citing works

CD4+ T cells mediate cytotoxicity in neurodegenerative diseases

Appel, S. H. (2008) · Journal of Clinical Investigation · doi:10.1172/jci38096 · Cited by 92 · see citing works

Doxycycline Is Neuroprotective Against Nigral Dopaminergic Degeneration by a Dual Mechanism Involving MMP-3

Cho, Y., Son, H. J., Kim, E.-M., Choi, J. H., Kim, S. T., Ji, I. J., Choi, D. H., Joh, T. H., Kim, Y. S., & Hwang, O. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9078-1 · Cited by 85 · see citing works

Ethyl Pyruvate Rescues Nigrostriatal Dopaminergic Neurons by Regulating Glial Activation in a Mouse Model of Parkinson’s Disease

Huh, S. H., Chung, Y. C., Piao, Y., Jin, M. Y., Son, H. J., Yoon, N. S., Hong, J. Y., Pak, Y. K., Kim, Y. S., Hong, J. K., et al. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1100009 · Cited by 79 · see citing works

Matrix Metalloproteinase-3 Is Increased and Participates in Neuronal Apoptotic Signaling Downstream of Caspase-12 during Endoplasmic Reticulum Stress

Kim, E., Shin, E.-J., Choi, J. H., Son, H. J., Park, I., JOH, T. H., & Hwang, O. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.093799 · Cited by 72 · see citing works

Functional Interaction between Matrix Metalloproteinase-3 and Semaphorin-3C during Cortical Axonal Growth and Guidance

Gonthier, B., Nasarre, C., Roth, L., Perraut, M., Thomasset, N., Roussel, G., Aunis, D., & Bagnard, D. (2006) · Cerebral Cortex · doi:10.1093/cercor/bhl082 · Cited by 50 · see citing works

An Aberrant Cerebellar Development in Mice Lacking Matrix Metalloproteinase-3

Hove, I. V., Verslegers, M., Buyens, T., Delorme, N., Lemmens, K., Stroobants, S., Gantois, I., D’Hooge, R., & Moons, L. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8215-z · Cited by 34 · see citing works

Partial dopamine depletion in MPTP-treated mice differentially altered motor skill learning and action control

Chagniel, L., Robitaille, C., Lacharité-Mueller, C., Bureau, G., & Cyr, M. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.11.019 · Cited by 30 · see citing works

A novel compound PTIQ protects the nigral dopaminergic neurones in an animal model of Parkinson's disease induced by MPTP

Son, H. J., Lee, J. A., Shin, N., Choi, J. H., Seo, J. W., Yoon, D., Lee, C.-S., Kim, E., Choe, H., & Hwang, O. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01692.x · Cited by 26 · see citing works

Matrix metalloproteinase-3 contributes to vulnerability of the nigral dopaminergic neurons

Kim, S. T., Kim, E., Choi, J. H., Son, H. J., Ji, I. J., JOH, T. H., Chung, S. J., & Hwang, O. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.09.014 · Cited by 16 · see citing works

Blood-Brain Barrier: From Physiology to Disease and Back

Sweeney, M. D., Zhao, Z., Montagne, A., Nelson, A. R., & Zlokovic, B. V. (2019) · Physiological Reviews · doi:10.1152/physrev.00050.2017 · Cited by 2,294 · see citing works

The Roles of Matrix Metalloproteinases and Their Inhibitors in Human Diseases

Cabral-Pacheco, G. A., Garza-Veloz, I., Castruita-De la Rosa, C., Ramirez-Acuña, J. M., Perez-Romero, B. A., Guerrero-Rodriguez, J. F., Martinez-Avila, N., & Martinez-Fierro, M. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249739 · Cited by 1,820 · see citing works

Nanoparticle-mediated brain drug delivery: Overcoming blood–brain barrier to treat neurodegenerative diseases

Saraiva, C., Praça, C., Ferreira, R., Santos, T., Ferreira, L., & Bernardino, L. (2016) · Journal of Controlled Release · doi:10.1016/j.jconrel.2016.05.044 · Cited by 1,609 · see citing works

Matrix metalloproteinases in the brain and blood–brain barrier: Versatile breakers and makers

Rempe, R. G., Hartz, A. M. S., & Bauer, B. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16655551 · Cited by 784 · see citing works

Factors controlling permeability of the blood–brain barrier

Almutairi, M. M., Chen, G., Xu, Y. G., Chang, Y., & Shi, H. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2050-8 · Cited by 308 · see citing works

The neuroprotective effects of glucagon-like peptide 1 in Alzheimer’s and Parkinson’s disease: An in-depth review

Reich, N., & Hölscher, C. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.970925 · Cited by 248 · see citing works

Multifaceted role of matrix metalloproteinases (MMPs)

Singh, D., Srivastava, S., Chaudhuri, T., & Upadhyay, G. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00019 · Cited by 194 · see citing works

Blood–brain barrier alterations and their impact on Parkinson’s disease pathogenesis and therapy

Lau, K., Kotzur, R., & Richter, F. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00430-z · Cited by 165 · see citing works

Evidence of Inflammatory System Involvement in Parkinson’s Disease

Chao, Y., Wong, S. C., & Tan, E. K. (2014) · BioMed Research International · doi:10.1155/2014/308654 · Cited by 150 · see citing works

CB2 receptor activation prevents glial-derived neurotoxic mediator production, BBB leakage and peripheral immune cell infiltration and rescues dopamine neurons in the MPTP model of Parkinson’s disease

Chung, Y. C., Shin, W.-H., Baek, J. Y., Cho, E. J., Baik, H. H., Kim, S. R., Won, S.-Y., & Jin, B. K. (2016) · Experimental & Molecular Medicine · doi:10.1038/emm.2015.100 · Cited by 126 · see citing works

Modulation of M1/M2 polarization by capsaicin contributes to the survival of dopaminergic neurons in the lipopolysaccharide-lesioned substantia nigra in vivo

Bok, E., Chung, Y. C., Kim, K., Baik, H. H., Shin, W.-H., & Jin, B. K. (2018) · Experimental & Molecular Medicine · doi:10.1038/s12276-018-0111-4 · Cited by 125 · see citing works

Exploring the Association Between Rosacea and Parkinson Disease

Egeberg, A., Hansen, P. R., Gislason, G., & Thyssen, J. P. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.0022 · Cited by 119 · see citing works

Metalloproteinases and their tissue inhibitors in Alzheimer’s disease and other neurodegenerative disorders

Rivera, S., García‐González, L., Khrestchatisky, M., & Baranger, K. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03178-2 · Cited by 112 · see citing works

Mast Cells in Neurodegenerative Disease

Jones, M. K., Nair, A. A., & Gupta, M. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00171 · Cited by 109 · see citing works

Impairment of blood-brain barrier is an early event in R6/2 mouse model of Huntington Disease

Pardo, A. D., Amico, E., Scalabrì, F., Pepe, G., Castaldo, S., Elifani, F., Capocci, L., Sanctis, C. D., Comerci, L., Pompeo, F., et al. (2017) · Scientific Reports · doi:10.1038/srep41316 · Cited by 99 · see citing works

The role of the blood–brain barrier in hypertension

Setiadi, A., Korim, W. S., Elsaafien, K., & Yao, S. T. (2017) · Experimental Physiology · doi:10.1113/ep086434 · Cited by 103 · see citing works

Matrix metalloproteinase-3 promotes early blood-spinal cord barrier disruption and hemorrhage and impairs long-term neurological recovery after spinal cord injury.

Lee, J., Choi, H., Ahn, H., Ju, B., & Yune, T. (2014) · American Journal of Pathology · doi:10.1016/j.ajpath.2014.07.016 · Cited by 93 · see citing works

Beyond muscles: The untapped potential of creatine

Riesberg, L. A., Weed, S. A., McDonald, T. L., Eckerson, J. M., & Drescher, K. M. (2016) · International Immunopharmacology · doi:10.1016/j.intimp.2015.12.034 · Cited by 95 · see citing works

Matrix Metalloproteinases in Non-Neoplastic Disorders

Tokito, A., & Jougasaki, M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17071178 · Cited by 96 · see citing works

Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges

Zipfel, P., Rochais, C., Baranger, K., Rivera, S., & Dallemagne, P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00352 · Cited by 94 · see citing works

Type‐1 interferons contribute to the neuroinflammatory response and disease progression of the MPTP mouse model of Parkinson's disease

Main, B. S., Zhang, M., Brody, K. M., Ayton, S., Frugier, T., Steer, D., Finkelstein, D., Crack, P. J., & Taylor, J. M. (2016) · Glia · doi:10.1002/glia.23028 · Cited by 92 · see citing works

Ginsenoside Rg1 attenuates motor impairment and neuroinflammation in the MPTP-probenecid-induced parkinsonism mouse model by targeting α-synuclein abnormalities in the substantia nigra

Heng, Y., Zhang, Q.-S., Mu, Z., Hu, J., Yuan, Y., & Chen, N. (2015) · Toxicology Letters · doi:10.1016/j.toxlet.2015.12.005 · Cited by 92 · see citing works

Blood–Brain Barrier and Neurodegenerative Diseases—Modeling with iPSC-Derived Brain Cells

Wu, Y., Sonninen, T.-M., Peltonen, S., Koıstınaho, J., & Lehtonen, Š. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147710 · Cited by 88 · see citing works

Potential role of gut microbiota and tissue barriers in Parkinson's disease and amyotrophic lateral sclerosis

Fang, X. (2015) · International Journal of Neuroscience · doi:10.3109/00207454.2015.1096271 · Cited by 84 · see citing works

A “multi-omics” analysis of blood–brain barrier and synaptic dysfunction in <i>APOE4</i> mice

Barisano, G., Kisler, K., Wilkinson, B., Nikolakopoulou, A. M., Sagare, A. P., Wang, Y., Gilliam, W., Huuskonen, M. T., Hung, S.-T., Ichida, J. K., et al. (2022) · Journal of Experimental Medicine · doi:10.1084/jem.20221137 · Cited by 78 · see citing works

Long-term characterization of activated microglia/macrophages facilitating the development of experimental brain metastasis through intravital microscopic imaging

Qiao, S., Qian, Y., Xu, G., Luo, Q., & Zhang, Z. (2019) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1389-9 · Cited by 76 · see citing works

Neurotoxin Mechanisms and Processes Relevant to Parkinson’s Disease: An Update

Segura‐Aguilar, J., & Kostrzewa, R. M. (2015) · Neurotoxicity Research · doi:10.1007/s12640-015-9519-y · Cited by 73 · see citing works

The Cleavage Effect of Mesenchymal Stem Cell and Its Derived Matrix Metalloproteinase-2 on Extracellular α-Synuclein Aggregates in Parkinsonian Models

Oh, S. H., Kim, H., Park, H.-J., Shin, J. Y., Kim, D. Y., & Lee, P. H. (2016) · Stem Cells Translational Medicine · doi:10.5966/sctm.2016-0111 · Cited by 66 · see citing works

Unique signatures of stress-induced senescent human astrocytes

Simmnacher, K., Krach, F., Schneider, Y., Alecu, J. E., Mautner, L., Klein, P., Roybon, L., Prots, I., Xiang, W., & Winner, B. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113466 · Cited by 63 · see citing works

Mechanisms Underlying Brain Aging Under Normal and Pathological Conditions

Jin, M., & Cai, S. (2022) · Neuroscience Bulletin · doi:10.1007/s12264-022-00969-9 · Cited by 59 · see citing works

Cold-Inducible RNA-Binding Protein Is an Important Mediator of Alcohol-Induced Brain Inflammation

Rajayer, S. R., Jacob, A., Yang, W.-L., Zhou, M., Chaung, W. W., & Wang, P. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079430 · Cited by 53 · see citing works

Parkinson's disease pathogenesis, evolution and alternative pathways: A review

Alexoudi, A., Alexoudi, I., & Gatzonis, S. D. (2018) · Revue Neurologique · doi:10.1016/j.neurol.2017.12.003 · Cited by 52 · see citing works

N‐myc downstream‐regulated gene 2 protects blood–brain barrier integrity following cerebral ischemia

Takarada‐Iemata, M., Yoshikawa, A., Ta, H. M., Okitani, N., Nishiuchi, T., Aida, Y., Kamide, T., Hattori, T., Ishii, H., Tamatani, T., et al. (2018) · Glia · doi:10.1002/glia.23315 · Cited by 51 · see citing works

Matrix metalloproteinase profiling and their roles in disease

Chang, M. (2023) · RSC Advances · doi:10.1039/d2ra07005g · Cited by 50 · see citing works

Protease-activatable adeno-associated virus vector for gene delivery to damaged heart tissue

Guenther, C. M., Brun, M. J., Bennett, A. D., Ho, M. L., Chen, W., Zhu, B., Lam, M., Yamagami, M., Kwon, S., Bhattacharya, N., et al. (2019) · Molecular Therapy · doi:10.1016/j.ymthe.2019.01.015 · Cited by 46 · see citing works

Acylated Ghrelin as a Multi-Targeted Therapy for Alzheimer's and Parkinson's Disease

Reich, N., & Hölscher, C. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.614828 · Cited by 48 · see citing works

Aging Neurovascular Unit and Potential Role of DNA Damage and Repair in Combating Vascular and Neurodegenerative Disorders

Li, Y., Xie, L., Huang, T., Zhang, Y., Zhou, J., Qi, B., Wang, X., Chen, Z., & Li, P. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00778 · Cited by 46 · see citing works

Matrix Metalloproteinase-3 Causes Dopaminergic Neuronal Death through Nox1-Regenerated Oxidative Stress

Choi, D.-H., Kim, J.-H., Seo, J.-H., Lee, J., Choi, W. S., & Kim, Y.-S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115954 · Cited by 43 · see citing works

Cholecystokinin (CCK): a neuromodulator with therapeutic potential in Alzheimer's and Parkinson's disease.

Reich, N., & Hölscher, C. (2024) · Frontiers in neuroendocrinology (Print) · doi:10.1016/j.yfrne.2024.101122 · Cited by 35 · see citing works

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 · see citing works

Interleukin-4 Contributes to Degeneration of Dopamine Neurons in the Lipopolysaccharide-treated Substantia Nigrain vivo

Bok, E., Cho, E. J., Chung, E. S., Shin, W.-H., & Jin, B. K. (2018) · Experimental Neurobiology · doi:10.5607/en.2018.27.4.309 · Cited by 36 · see citing works

Photobiomodulation Mitigates Cerebrovascular Leakage Induced by the Parkinsonian Neurotoxin MPTP

Miguel, M. S., Martin, K. L., Stone, J., & Johnstone, D. M. (2019) · Biomolecules · doi:10.3390/biom9100564 · Cited by 37 · see citing works

Protective Role of Capsaicin in Neurological Disorders: An Overview

Tyagi, S., Shekhar, N., & Thakur, A. K. (2022) · Neurochemical Research · doi:10.1007/s11064-022-03549-5 · Cited by 37 · see citing works

Bidirectional communication between mast cells and the gut-brain axis in neurodegenerative diseases: Avenues for therapeutic intervention

Bhuiyan, P., Chen, Y., Karim, M., Dong, H., & Qian, Y. (2021) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2021.04.010 · Cited by 33 · see citing works

REMOVED: Nanodelivery of cerebrolysin reduces pathophysiology of Parkinson's disease

Ozkızılcık, A., Sharma, A., Lafuente, J. V., Muresanu, D. F., Nozari, A., Tian, Z. R., Mössler, H., & Sharma, H. S. (2019) · Progress in brain research · doi:10.1016/bs.pbr.2019.03.014 · Cited by 29 · see citing works

Regulation of striatal astrocytic receptor for advanced glycation end‐products variants in an early stage of experimental Parkinson's disease

Viana, S., Valero, J., Rodrigues‐Santos, P., Couceiro, P., Silva, A. M., Carvalho, F. D., Ali, S. F., Ribeiro, C., & Pereira, F. C. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13682 · Cited by 29 · see citing works

Papaverine inhibits α-synuclein aggregation by modulating neuroinflammation and matrix metalloproteinase-3 expression in the subacute MPTP/P mouse model of Parkinson’s disease

Leem, Y., Park, J., Park, J.-E., Kim, D.-Y., Kang, J. L., & Kim, H.-S. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110576 · Cited by 26 · see citing works

Lignans of Schisandra chinensis (Turcz.) Baill inhibits Parkinson's disease progression through mediated neuroinflammation-TRPV1 expression in microglia

Wang, S., Li, M., Wu, J.-T., Sun, Y., Pan, J., Guan, W., Naseem, A., Algradi, A. M., Kuang, H., Jiang, Y.-K., et al. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.156146 · Cited by 25 · see citing works

Interleukin-4 Protects Dopaminergic Neurons In vitro but Is Dispensable for MPTP-Induced Neurodegeneration In vivo

Hühner, L., Rilka, J., Gilsbach, R., Zhou, X., Machado, V., & Spittau, B. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00062 · Cited by 25 · see citing works

Infiltrating peripheral monocyte TREM-1 mediates dopaminergic neuron injury in substantia nigra of Parkinson’s disease model mice

Song, W., Zhou, Z.-M., Zhang, L., Shu, H.-F., Xia, J.-R., Qin, X., Hua, R., & Zhang, Y. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07333-5 · Cited by 24 · see citing works

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 · see citing works

Emerging diagnostic markers and therapeutic targets in post-stroke hemorrhagic transformation and brain edema

Yao, Y., Liu, F., Gu, Z., Wang, J., Xu, L., Yu, Y., Cai, J., & Ren, R. (2023) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2023.1286351 · Cited by 23 · see citing works

Perspectives and New Aspects of Metalloproteinases’ Inhibitors in the Therapy of CNS Disorders: From Chemistry to Medicine

Boguszewska‐Czubara, A., Budzyńska, B., Skalicka‐Woźniak, K., & Kurzepa, J. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180514111500 · Cited by 22 · see citing works

β-Ecdysterone Protects SH-SY5Y Cells Against 6-Hydroxydopamine-Induced Apoptosis via Mitochondria-Dependent Mechanism: Involvement of p38MAPK–p53 Signaling Pathway

Pan, Z., Niu, Y., Liang, Y., Zhang, X., & Dong, M. (2016) · Neurotoxicity Research · doi:10.1007/s12640-016-9631-7 · Cited by 21 · see citing works

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 20 · see citing works

A Systematic Review of Extracellular Matrix-Related Alterations in Parkinson’s Disease

Chapman, M. A., & Sorg, B. A. (2024) · Brain Sciences · doi:10.3390/brainsci14060522 · Cited by 20 · see citing works

Microvascular blood-brain barrier alterations in isolated brain capillaries of mice over-expressing alpha-synuclein (Thy1-aSyn line 61)

Lau, K., Porschen, L. T., Richter, F., & Gericke, B. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106298 · Cited by 18 · see citing works

Potentiating a non-neuronal cardiac cholinergic system reinforces the functional integrity of the blood brain barrier associated with systemic anti-inflammatory responses

Oikawa, S., Kai, Y., Mano, A., Sugama, S., Mizoguchi, N., Tsuda, M., Muramoto, K., & Kakinuma, Y. (2019) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2019.06.005 · Cited by 18 · see citing works

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 16 · see citing works

Rosacea and subsequent diagnosis for Parkinson's disease: a large, urban, single center, US patient population retrospective study

Mathieu, R. J., Guido, N., Ibler, E., Serrano, L., Rangel, S. M., Schlosser, B. J., West, D. P., Laumann, A. E., & Nardone, B. (2017) · Journal of the European Academy of Dermatology and Venereology · doi:10.1111/jdv.14638 · Cited by 15 · see citing works

Impact of MMP2 rs243865 and MMP3 rs3025058 Polymorphisms on Clinical Findings in Alzheimer’s Disease Patients

Ďurmanová, V., Javor, J., Párnická, Z., Minárik, G., Ocenasova, A., Vašečková, B., Režnáková, V., Kralova, M., Hromádka, T., & Shawkatová, I. (2021) · Mediators of Inflammation · doi:10.1155/2021/5573642 · Cited by 15 · see citing works

The Therapeutic Benefits of Intravenously Administrated Nanoparticles in Stroke and Age-related Neurodegenerative Diseases

Farhoudi, M., Sadigh‐Eteghad, S., Mahmoudi, J., Farjami, A., Mahmoudian, M., & Salatin, S. (2022) · Current Pharmaceutical Design · doi:10.2174/1381612828666220608093639 · Cited by 13 · see citing works

Nei-like 1 inhibition results in motor dysfunction and promotes inflammation in Parkinson’s disease mice model

Bai, X., Xiao, W. Q., & Tian, H. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.10.118 · Cited by 12 · see citing works

The tetrapartite synapse in neuropsychiatric disorders: Matrix metalloproteinases (MMPs) as promising targets for treatment and rational drug design

Filho, A. J. M. C., Mottin, M., Lós, D. B., Andrade, C. H., & Macêdo, D. S. (2022) · Biochimie · doi:10.1016/j.biochi.2022.07.015 · Cited by 11 · see citing works

Impaired tissue barriers as potential therapeutic targets for Parkinson’s disease and amyotrophic lateral sclerosis

Fang, X. (2018) · Metabolic Brain Disease · doi:10.1007/s11011-018-0239-x · Cited by 11 · see citing works

Skin Conditions and Movement Disorders: Hiding in Plain Sight

Kulcsárová, K., Baloghová, J., Necpál, J., & Škorvánek, M. (2022) · Movement Disorders Clinical Practice · doi:10.1002/mdc3.13436 · Cited by 10 · see citing works

Genetic variation of matrix metalloproteinase enzyme in HIV-associated neurocognitive disorder

Singh, H., Nain, S., Krishnaraj, A., Lata, S., & Dhole, T. N. (2019) · Gene · doi:10.1016/j.gene.2019.02.057 · Cited by 10 · see citing works

Parkinson’s Disease and Its Dermatological Associations: Is Your Skin Whispering You a Diagnosis?

Shah, P., Sagar, P. R., Alhumaidi, N., Bollampally, V. C., & Malik, B. H. (2020) · Cureus · doi:10.7759/cureus.9933 · Cited by 9 · see citing works

Platelet Behavior Contributes to Neuropathologies: A Focus on Alzheimer's and Parkinson's Disease

Page, M. J., & Pretorius, E. (2021) · Seminars in Thrombosis and Hemostasis · doi:10.1055/s-0041-1733960 · Cited by 9 · see citing works

Alpha synuclein processing by MMP-3 – implications for synucleinopathies

Bluhm, A., Schrempel, S., Moceri, S., Stieler, J., Feja, M., Schilling, S., Schulze, A., von Hörsten, S., Hartlage‐Rübsamen, M., Richter, F., et al. (2022) · Behavioural Brain Research · doi:10.1016/j.bbr.2022.114020 · Cited by 8 · see citing works

Aqueous extract of Terminalia arjuna bark attenuates blood brain barrier disruption in rat model of transient focal cerebral ischemia

Kaliyappan, K., Sathyamoorthy, Y. K., Nambi, P., & Radhakrishnan, R. (2021) · Phytomedicine Plus · doi:10.1016/j.phyplu.2021.100092 · Cited by 7 · see citing works

Role of Cellular Senescence in Parkinson’s Disease: Potential for Disease-Modification Through Senotherapy

Rademacher, D. J., Exline, J. E., & Foecking, E. M. (2025) · Biomedicines · doi:10.3390/biomedicines13061400 · Cited by 7 · see citing works

Multiomics of parkinsonism cynomolgus monkeys highlights significance of metabolites in interaction between host and microbiota

Gao, J.-M., Xia, S.-Y., Hide, G., Li, B.-H., Liu, Y.-Y., Wei, Z.-Y., Zhuang, X.-J., Yan, Q., Wang, Y., Yang, W., et al. (2024) · npj Biofilms and Microbiomes · doi:10.1038/s41522-024-00535-3 · Cited by 5 · see citing works

Blood-Brain Barrier Dysfunction in the Detrimental Brain Function

González‐Candia, A., Rogers, N. K., & Castillo, R. L. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.94572 · Cited by 5 · see citing works

LRRK2 G2019S Mutated iPSC-Derived Endothelial Cells Exhibit Increased α-Synuclein, Mitochondrial Impairment, and Altered Inflammatory Responses

Sonninen, T.-M., Peltonen, S., Niskanen, J., Hämäläinen, R. H., Koıstınaho, J., & Lehtonen, Š. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312874 · Cited by 4 · see citing works

Neuroprotective effects of hypoactive Akkermansia muciniphila in MPTP-induced mouse models of Parkinson’s disease

Xi, J., Tang, C., Xiao, X., Chen, M., Zou, Q., & Zhou, X. (2025) · Microbiology Spectrum · doi:10.1128/spectrum.03379-24 · Cited by 3 · see citing works

Doxycycline, an anti-inflammatory agent, alleviates dyskinesia induced by L-DOPA in Parkinsonian ratsPreprint

Bortolanza, M., Nascimento, G. C., Raisman‐Vozari, R., & Bel, E. A. D. (2020) · doi:10.22541/au.159285563.30385356 · Cited by 3 · see citing works

Dysregulation of the Extracellular Matrix in the Synaptic Pathology of Parkinson’s Disease: Molecular Mechanisms and Novel Therapeutic Approaches

Rubio, C., Pérez-Rubio, R., Pérez-Villavicencio, J., Serrano‐García, N., Lee, Á., Granados-Rojas, L., Tena‐Suck, M. L., & Rubio‐Osornio, M. (2026) · Life · doi:10.3390/life16061007 · Cited by 2 · see citing works

Immunity in Parkinson's disease – The role of innate responses

Iyengar, A. S., Dunkley, P. R., & Dickson, P. W. (2025) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2025.578716 · Cited by 3 · see citing works

Central nervous system diseases associated with blood brain barrier breakdown - A Comprehensive update of existing literature

Dutta, R. (2020) · Journal of Neuroscience and Neurological Disorders · doi:10.29328/journal.jnnd.1001035 · Cited by 2 · see citing works

Immune and Long Interspersed Nuclear Element-1 Dysregulation in Schizophrenia: An Exploratory Case–Control Study in a Brazilian Cohort with Ultra-Treatment Resistance

de Pinho, C. S. N., Pinto, J. P., Martins, P. L. B., Fiorenza, N. G., Clemente, D. C. D. S., Castro, H. I. R., Viana, M. D. S., Teles, C. B. M., Rebouças, M. D. O., Silva, M. F. S., et al. (2025) · Schizophrenia Bulletin · doi:10.1093/schbul/sbaf209 · Cited by 1 · see citing works

Potential Mechanisms of Tetramethylpyrazine in the Treatment of Traumatic Brain Injury Based on Network Pharmacology, Molecular Docking, Molecular Dynamics Simulations, and in vivo Experiments

Tang, L., Xu, R., Wu, Y. C., & Cheng, H. (2025) · International Journal of General Medicine · doi:10.2147/ijgm.s553186 · Cited by 1 · see citing works

Comparative Analysis of T-Cell Signatures and Astroglial Reactivity in Parkinson’s Pathology Across Animal Models with Distinct Regenerative Capacities

Intonti, S., Enzmann, V., Perna, A., Spagnolo, F., Curcio, C., & Conedera, F. M. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27020965 · Cited by 1 · see citing works

The Role of Blood-Retinal Barrier in Retinal Neurodegenerative Diseases

Blankenborg, L., Anand‐Apte, B., & Biswas, S. (2026) · American Journal Of Pathology · doi:10.1016/j.ajpath.2026.05.002 · Cited by 1 · see citing works

Correlation of Stromelysin-1 and Tissue Inhibitor of Metalloproteinase-1 with Lipid Profile and Atherogenic Indices in End-Stage Renal Disease Patients: A Neural Network Study

Abdalsada, H. K., Hadi, H. H., Almulla, A. F., Najm, A. H., Al-Isa, A., & Al‐Hakeim, H. K. (2023) · Pertanika journal of science & technology · doi:10.47836/pjst.31.4.27 · Cited by 1 · see citing works

Book review: Zhang, X., Yang, E., & Thomas, N: Enterprise Management Control Systems in China

Asdullah, M. A., & Yazdifar, H. (2019) · Asia-Pacific Journal of Management Research and Innovation · doi:10.1177/2319510x19883075 · Cited by 1 · see citing works

Rosacea and Neurological Comorbidities

Wienholtz, N. K. F., Thyssen, J. P., & Egeberg, A. (2020) · Updates in clinical dermatology · doi:10.1007/978-3-030-52097-7_9

Etude de l'interaction du TIMP-1 avec ses récepteurs

Verzeaux, L. (2015) · doi:10.70675/02b3787dze0bbz4a18z9bd2zc42bb1e85844

Repurposing of doxycycline as a novel therapeutic avenue for management of parkinson’s disease

Ali, N. H., Al-Kuraishy, H. M., Hussain, N. R., Al-Gareeb, A. I., Albuhadily, A. K., Waheeb, T. S., & Batiha, G. E. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02156-y

Molecular mechanisms of action of MT-MMPs involved in the pathogenesis of Alzheimer’s disease

García‐González, L. (2020) · theses.fr (ABES) · doi:10.70675/a04672c0z1f4az472ezbcd5zbea446eac50c

Parkinson’s Disease, Microglia, and Extracellular Matrix Remodeling

Serrano‐García, N., Ponce-Juárez, A., Ganado, M., Pérez-Villavicencio, J., & Rubio‐Osornio, M. (2026) · Neuroglia · doi:10.3390/neuroglia7030027

Matrix metalloproteinases (MMPs) in neurodegenerative diseases, an updated overview of the role of MT1-MMP and MT5-MMP in Alzheimer’s disease

Frank, M., Barthélémy, C., Dufour, A., Rivera, S., & Baranger, K. (2026) · The Enzymes · doi:10.1016/bs.enz.2026.07.004

Renal stress-associated extracellular vesicle signaling linked to lysosomal cathepsin D and NEK7–NLRP3 neuroinflammation

Park, G., Yoo, H.-R., & Lim, H.-S. (2026) · Molecular Biomedicine · doi:10.1186/s43556-026-00608-z

BindingDB Entry 50011295: Matrix Metalloproteinases as New Targets in Alzheimer's Disease: Opportunities and Challenges.

BindingDB (2022) · UC San Diego · doi:10.7270/q2bv7m7k

Research Article MMP-3 Contributes to Nigrostriatal Dopaminergic Neuronal Loss, BBB Damage, and Neuroinflammation in an MPTP Mouse Model of Parkinson’s Disease

Chung, Y. C., Kim, Y.-S., Bok, E., Yune, T. Y., 맹성호, & Jin, B. K. (2016)

Microglial Activation Damages Dopaminergic Neurons through MMP-2/-9-Mediated Increase of Blood-Brain Barrier Permeability in a Parkinson’s Disease Mouse Model

Ruan, Z., Zhang, D., Huang, R., Sun, W., Hou, L., Zhao, J., & Wang, Q. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23052793 · Cited by 82 · see citing works

TLR3 contributes to degeneration of dopamine neurons in an MPTP mouse model of Parkinson’s disease

Chung, Y. C., Jeong, J., & Jin, B. K. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.200.supp.166.55 · Cited by 3 · see citing works

Metalloproteinase-9 contributes to inflammatory glia activation and nigro-striatal pathway degeneration in both mouse and monkey models of 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced Parkinsonism

Annese, V., Herrero, M. T., Pentima, M. D., Gómez, A., Lombardi, L., Ros, C. M. B., de Pablos, V., Fernández‐Villalba, E., & Stefano, M. E. D. (2014) · Brain Structure and Function · doi:10.1007/s00429-014-0718-8 · Cited by 76 · see citing works

Matrix metalloproteinase-3 contributes to vulnerability of the nigral dopaminergic neurons

Kim, S. T., Kim, E., Choi, J. H., Son, H. J., Ji, I. J., JOH, T. H., Chung, S. J., & Hwang, O. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.09.014 · Cited by 16 · see citing works