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Volumn 214, Issue , 2014, Pages 313-351

Endogenous and synthetic MMP inhibitors in CNS physiopathology

Author keywords

Alzheimer's disease; Bacterial meningitis; EAE; Multiple sclerosis; Synthetic MMP inhibitors

Indexed keywords

BATIMASTAT; BB 1001; COLLAGENASE; COLLAGENASE 3; DOXYCYCLINE; GELATINASE; GELATINASE A; GELATINASE B; ILOMASTAT; INTERSTITIAL COLLAGENASE; MACROPHAGE ELASTASE; MATRILYSIN; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE 15; MATRIX METALLOPROTEINASE 16; MATRIX METALLOPROTEINASE 17; MATRIX METALLOPROTEINASE 26; MATRIX METALLOPROTEINASE INHIBITOR; MEMBRANE PROTEIN; NEUTROPHIL COLLAGENASE; STROMELYSIN; STROMELYSIN 2; STROMELYSIN 3; TISSUE INHIBITOR OF METALLOPROTEINASE; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TISSUE INHIBITOR OF METALLOPROTEINASE 4; TNF 484; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84922270764     PISSN: 00796123     EISSN: 18757855     Source Type: Book Series    
DOI: 10.1016/B978-0-444-63486-3.00014-1     Document Type: Chapter
Times cited : (41)

References (227)
  • 1
    • 3543090958 scopus 로고    scopus 로고
    • Chemically modified tetracyclines as inhibitors of matrix metalloproteinases
    • Acharya M.R., Venitz J., Figg W.D., Sparreboom A. Chemically modified tetracyclines as inhibitors of matrix metalloproteinases. Drug Resist. Updat. 2004, 7:195-208.
    • (2004) Drug Resist. Updat. , vol.7 , pp. 195-208
    • Acharya, M.R.1    Venitz, J.2    Figg, W.D.3    Sparreboom, A.4
  • 3
    • 84908591066 scopus 로고    scopus 로고
    • Pathogenesis and pathophysiology of bacterial infections
    • Lippincott Williams & Wilkins, Philadelphia, PA, M.W. Scheld, R.J. Whitley, C.M. Marra (Eds.)
    • Agyeman P., Grandgirard D., Leib S. Pathogenesis and pathophysiology of bacterial infections. Infections of the Central Nervous System 2014, Lippincott Williams & Wilkins, Philadelphia, PA. fourth ed. M.W. Scheld, R.J. Whitley, C.M. Marra (Eds.).
    • (2014) Infections of the Central Nervous System
    • Agyeman, P.1    Grandgirard, D.2    Leib, S.3
  • 4
    • 33646379384 scopus 로고    scopus 로고
    • Cleavage of amyloid-beta precursor protein (APP) by membrane-type matrix metalloproteinases
    • Ahmad M., Takino T., Miyamori H., Yoshizaki T., Furukawa M., Sato H. Cleavage of amyloid-beta precursor protein (APP) by membrane-type matrix metalloproteinases. J. Biochem. 2006, 139:517-526.
    • (2006) J. Biochem. , vol.139 , pp. 517-526
    • Ahmad, M.1    Takino, T.2    Miyamori, H.3    Yoshizaki, T.4    Furukawa, M.5    Sato, H.6
  • 5
    • 77955022345 scopus 로고    scopus 로고
    • Alterations in serum MMP-8, MMP-9, IL-12p40 and IL-23 in multiple sclerosis patients treated with interferon-beta1b
    • Alexander J.S., Harris M.K., Wells S.R., Mills G., Chalamidas K., Ganta V.C., et al. Alterations in serum MMP-8, MMP-9, IL-12p40 and IL-23 in multiple sclerosis patients treated with interferon-beta1b. Mult. Scler. 2010, 16:801-809.
    • (2010) Mult. Scler. , vol.16 , pp. 801-809
    • Alexander, J.S.1    Harris, M.K.2    Wells, S.R.3    Mills, G.4    Chalamidas, K.5    Ganta, V.C.6
  • 7
    • 0025231284 scopus 로고
    • Expression of metalloproteinases and metalloproteinase inhibitors by fetal astrocytes and glioma cells
    • Apodaca G., Rutka J.T., Bouhana K., Berens M.E., Giblin J.R., Rosenblum M.L., et al. Expression of metalloproteinases and metalloproteinase inhibitors by fetal astrocytes and glioma cells. Cancer Res. 1990, 50:2322-2329.
    • (1990) Cancer Res. , vol.50 , pp. 2322-2329
    • Apodaca, G.1    Rutka, J.T.2    Bouhana, K.3    Berens, M.E.4    Giblin, J.R.5    Rosenblum, M.L.6
  • 8
    • 0035478029 scopus 로고    scopus 로고
    • Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia
    • Asahi M., Wang X., Mori T., Sumii T., Jung J.C., Moskowitz M.A., et al. Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia. J. Neurosci. 2001, 21:7724-7732.
    • (2001) J. Neurosci. , vol.21 , pp. 7724-7732
    • Asahi, M.1    Wang, X.2    Mori, T.3    Sumii, T.4    Jung, J.C.5    Moskowitz, M.A.6
  • 10
    • 0029852887 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1-40)
    • Backstrom J.R., Lim G.P., Cullen M.J., Tokes Z.A. Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1-40). J. Neurosci. 1996, 16:7910-7919.
    • (1996) J. Neurosci. , vol.16 , pp. 7910-7919
    • Backstrom, J.R.1    Lim, G.P.2    Cullen, M.J.3    Tokes, Z.A.4
  • 11
    • 0344443218 scopus 로고    scopus 로고
    • Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis
    • Bar-Or A., Nuttall R.K., Duddy M., Alter A., Kim H.J., Ifergan I., et al. Analyses of all matrix metalloproteinase members in leukocytes emphasize monocytes as major inflammatory mediators in multiple sclerosis. Brain 2003, 126:2738-2749.
    • (2003) Brain , vol.126 , pp. 2738-2749
    • Bar-Or, A.1    Nuttall, R.K.2    Duddy, M.3    Alter, A.4    Kim, H.J.5    Ifergan, I.6
  • 12
    • 77956602522 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha (TNF-alpha) regulates shedding of TNF-alpha receptor 1 by the metalloprotease-disintegrin ADAM8: evidence for a protease-regulated feedback loop in neuroprotection
    • Bartsch J.W., Wildeboer D., Koller G., Naus S., Rittger A., Moss M.L., et al. Tumor necrosis factor-alpha (TNF-alpha) regulates shedding of TNF-alpha receptor 1 by the metalloprotease-disintegrin ADAM8: evidence for a protease-regulated feedback loop in neuroprotection. J. Neurosci. 2010, 30:12210-12218.
    • (2010) J. Neurosci. , vol.30 , pp. 12210-12218
    • Bartsch, J.W.1    Wildeboer, D.2    Koller, G.3    Naus, S.4    Rittger, A.5    Moss, M.L.6
  • 13
    • 61849164425 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and matrix metalloproteinase-2 as biomarkers of various courses in multiple sclerosis
    • Benesova Y., Vasku A., Novotna H., Litzman J., Stourac P., Beranek M., et al. Matrix metalloproteinase-9 and matrix metalloproteinase-2 as biomarkers of various courses in multiple sclerosis. Mult. Scler. 2009, 15:316-322.
    • (2009) Mult. Scler. , vol.15 , pp. 316-322
    • Benesova, Y.1    Vasku, A.2    Novotna, H.3    Litzman, J.4    Stourac, P.5    Beranek, M.6
  • 14
    • 0030583282 scopus 로고    scopus 로고
    • Relaxed specificity of matrix metalloproteinases (MMPS) and TIMP insensitivity of tumor necrosis factor-alpha (TNF-alpha) production suggest the major TNF-alpha converting enzyme is not an MMP
    • Black R.A., Durie F.H., Otten-Evans C., Miller R., Slack J.L., Lynch D.H., et al. Relaxed specificity of matrix metalloproteinases (MMPS) and TIMP insensitivity of tumor necrosis factor-alpha (TNF-alpha) production suggest the major TNF-alpha converting enzyme is not an MMP. Biochem. Biophys. Res. Commun. 1996, 225:400-405.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 400-405
    • Black, R.A.1    Durie, F.H.2    Otten-Evans, C.3    Miller, R.4    Slack, J.L.5    Lynch, D.H.6
  • 15
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black R.A., Rauch C.T., Kozlosky C.J., Peschon J.J., Slack J.L., Wolfson M.F., et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 1997, 385:729-733.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peschon, J.J.4    Slack, J.L.5    Wolfson, M.F.6
  • 16
    • 80054930244 scopus 로고    scopus 로고
    • IL-10 limits production of pathogenic TNF by M1 myeloid cells through induction of nuclear NF-kappaB p50 member in Trypanosoma congolense infection-resistant C57BL/6 mice
    • Bosschaerts T., Morias Y., Stijlemans B., Herin M., Porta C., Sica A., et al. IL-10 limits production of pathogenic TNF by M1 myeloid cells through induction of nuclear NF-kappaB p50 member in Trypanosoma congolense infection-resistant C57BL/6 mice. Eur. J. Immunol. 2011, 41:3270-3280.
    • (2011) Eur. J. Immunol. , vol.41 , pp. 3270-3280
    • Bosschaerts, T.1    Morias, Y.2    Stijlemans, B.3    Herin, M.4    Porta, C.5    Sica, A.6
  • 17
    • 0037422243 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 deficiency impairs host defense mechanisms against Streptococcus pneumoniae in a mouse model of bacterial meningitis
    • Bottcher T., Spreer A., Azeh I., Nau R., Gerber J. Matrix metalloproteinase-9 deficiency impairs host defense mechanisms against Streptococcus pneumoniae in a mouse model of bacterial meningitis. Neurosci. Lett. 2003, 338:201-204.
    • (2003) Neurosci. Lett. , vol.338 , pp. 201-204
    • Bottcher, T.1    Spreer, A.2    Azeh, I.3    Nau, R.4    Gerber, J.5
  • 18
    • 84877787138 scopus 로고    scopus 로고
    • A crucial role for Lyn in TIMP-1 erythroid cell survival signalling pathway
    • Bridoux L., Etique N., Lambert E., Thevenard J., Sowa M.L., Belloy N., et al. A crucial role for Lyn in TIMP-1 erythroid cell survival signalling pathway. FEBS Lett. 2013, 587:1524-1528.
    • (2013) FEBS Lett. , vol.587 , pp. 1524-1528
    • Bridoux, L.1    Etique, N.2    Lambert, E.3    Thevenard, J.4    Sowa, M.L.5    Belloy, N.6
  • 19
    • 0036516460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: a tail of a frog that became a prince
    • Brinckerhoff C.E., Matrisian L.M. Matrix metalloproteinases: a tail of a frog that became a prince. Nat. Rev. Mol. Cell Biol. 2002, 3:207-214.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 207-214
    • Brinckerhoff, C.E.1    Matrisian, L.M.2
  • 20
    • 84868596712 scopus 로고    scopus 로고
    • Dilemmas in the diagnosis of acute community-acquired bacterial meningitis
    • Brouwer M.C., Thwaites G.E., Tunkel A.R., Van De Beek D. Dilemmas in the diagnosis of acute community-acquired bacterial meningitis. Lancet 2012, 380:1684-1692.
    • (2012) Lancet , vol.380 , pp. 1684-1692
    • Brouwer, M.C.1    Thwaites, G.E.2    Tunkel, A.R.3    Van De Beek, D.4
  • 21
    • 0036260089 scopus 로고    scopus 로고
    • Targeting leukocyte MMPs and transmigration: minocycline as a potential therapy for multiple sclerosis
    • Brundula V., Rewcastle N.B., Metz L.M., Bernard C.C., Yong V.W. Targeting leukocyte MMPs and transmigration: minocycline as a potential therapy for multiple sclerosis. Brain 2002, 125:1297-1308.
    • (2002) Brain , vol.125 , pp. 1297-1308
    • Brundula, V.1    Rewcastle, N.B.2    Metz, L.M.3    Bernard, C.C.4    Yong, V.W.5
  • 22
    • 63349092629 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7 facilitates immune access to the CNS in experimental autoimmune encephalomyelitis
    • Buhler L.A., Samara R., Guzman E., Wilson C.L., Krizanac-Bengez L., Janigro D., et al. Matrix metalloproteinase-7 facilitates immune access to the CNS in experimental autoimmune encephalomyelitis. BMC Neurosci. 2009, 10:17.
    • (2009) BMC Neurosci. , vol.10 , pp. 17
    • Buhler, L.A.1    Samara, R.2    Guzman, E.3    Wilson, C.L.4    Krizanac-Bengez, L.5    Janigro, D.6
  • 24
    • 77954202334 scopus 로고    scopus 로고
    • The synapsins: key actors of synapse function and plasticity
    • Cesca F., Baldelli P., Valtorta F., Benfenati F. The synapsins: key actors of synapse function and plasticity. Prog. Neurobiol. 2010, 91:313-348.
    • (2010) Prog. Neurobiol. , vol.91 , pp. 313-348
    • Cesca, F.1    Baldelli, P.2    Valtorta, F.3    Benfenati, F.4
  • 26
    • 78650780265 scopus 로고    scopus 로고
    • Long-term sequelae of childhood bacterial meningitis: an underappreciated problem
    • Chandran A., Herbert H., Misurski D., Santosham M. Long-term sequelae of childhood bacterial meningitis: an underappreciated problem. Pediatr. Infect. Dis. J. 2011, 30:3-6.
    • (2011) Pediatr. Infect. Dis. J. , vol.30 , pp. 3-6
    • Chandran, A.1    Herbert, H.2    Misurski, D.3    Santosham, M.4
  • 27
    • 49849085127 scopus 로고    scopus 로고
    • Non-cell-autonomous effects of presenilin 1 variants on enrichment-mediated hippocampal progenitor cell proliferation and differentiation
    • Choi S.H., Veeraraghavalu K., Lazarov O., Marler S., Ransohoff R.M., Ramirez J.M., et al. Non-cell-autonomous effects of presenilin 1 variants on enrichment-mediated hippocampal progenitor cell proliferation and differentiation. Neuron 2008, 59:568-580.
    • (2008) Neuron , vol.59 , pp. 568-580
    • Choi, S.H.1    Veeraraghavalu, K.2    Lazarov, O.3    Marler, S.4    Ransohoff, R.M.5    Ramirez, J.M.6
  • 29
    • 10744226623 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression during experimental autoimmune encephalomyelitis and effects of a combined matrix metalloproteinase and tumour necrosis factor-alpha inhibitor
    • Clements J.M., Cossins J.A., Wells G.M., Corkill D.J., Helfrich K., Wood L.M., et al. Matrix metalloproteinase expression during experimental autoimmune encephalomyelitis and effects of a combined matrix metalloproteinase and tumour necrosis factor-alpha inhibitor. J. Neuroimmunol. 1997, 74:85-94.
    • (1997) J. Neuroimmunol. , vol.74 , pp. 85-94
    • Clements, J.M.1    Cossins, J.A.2    Wells, G.M.3    Corkill, D.J.4    Helfrich, K.5    Wood, L.M.6
  • 30
    • 0038359549 scopus 로고    scopus 로고
    • Liquid chromatographic determination of minocycline in brain-to-plasma distribution studies in the rat
    • Colovic M., Caccia S. Liquid chromatographic determination of minocycline in brain-to-plasma distribution studies in the rat. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2003, 791:337-343.
    • (2003) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.791 , pp. 337-343
    • Colovic, M.1    Caccia, S.2
  • 31
    • 58049099896 scopus 로고    scopus 로고
    • Changes in matrix metalloproteinases and their inhibitors during interferon-beta treatment in multiple sclerosis
    • Comabella M., Rio J., Espejo C., Ruiz De Villa M., Al-Zayat H., Nos C., et al. Changes in matrix metalloproteinases and their inhibitors during interferon-beta treatment in multiple sclerosis. Clin. Immunol. 2009, 130:145-150.
    • (2009) Clin. Immunol. , vol.130 , pp. 145-150
    • Comabella, M.1    Rio, J.2    Espejo, C.3    Ruiz De Villa, M.4    Al-Zayat, H.5    Nos, C.6
  • 32
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: trials and tribulations
    • Coussens L.M., Fingleton B., Matrisian L.M. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002, 295:2387-2392.
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 33
    • 34250211033 scopus 로고    scopus 로고
    • Persistent macrophage/microglial activation and myelin disruption after experimental autoimmune encephalomyelitis in tissue inhibitor of metalloproteinase-1-deficient mice
    • Crocker S.J., Whitmire J.K., Frausto R.F., Chertboonmuang P., Soloway P.D., Whitton J.L., Campbell I.L. Persistent macrophage/microglial activation and myelin disruption after experimental autoimmune encephalomyelitis in tissue inhibitor of metalloproteinase-1-deficient mice. Am. J. Pathol. 2006, 169:2104-2116.
    • (2006) Am. J. Pathol. , vol.169 , pp. 2104-2116
    • Crocker, S.J.1    Whitmire, J.K.2    Frausto, R.F.3    Chertboonmuang, P.4    Soloway, P.D.5    Whitton, J.L.6    Campbell, I.L.7
  • 34
    • 59449101792 scopus 로고    scopus 로고
    • Restored degradation of the Alzheimer's amyloid-beta peptide by targeting amyloid formation
    • Crouch P.J., Tew D.J., Du T., Nguyen D.N., Caragounis A., Filiz G., et al. Restored degradation of the Alzheimer's amyloid-beta peptide by targeting amyloid formation. J. Neurochem. 2009, 108:1198-1207.
    • (2009) J. Neurochem. , vol.108 , pp. 1198-1207
    • Crouch, P.J.1    Tew, D.J.2    Du, T.3    Nguyen, D.N.4    Caragounis, A.5    Filiz, G.6
  • 35
    • 0033081796 scopus 로고    scopus 로고
    • Plasminogen activators and matrix metalloproteases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system
    • Cuzner M.L., Opdenakker G. Plasminogen activators and matrix metalloproteases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system. J. Neuroimmunol. 1999, 94:1-14.
    • (1999) J. Neuroimmunol. , vol.94 , pp. 1-14
    • Cuzner, M.L.1    Opdenakker, G.2
  • 36
    • 0037466395 scopus 로고    scopus 로고
    • Beta-amyloid induces the production of active, matrix-degrading proteases in cultured rat astrocytes
    • Deb S., Wenjun Zhang J., Gottschall P.E. Beta-amyloid induces the production of active, matrix-degrading proteases in cultured rat astrocytes. Brain Res. 2003, 970:205-213.
    • (2003) Brain Res. , vol.970 , pp. 205-213
    • Deb, S.1    Wenjun Zhang, J.2    Gottschall, P.E.3
  • 37
    • 78149250136 scopus 로고    scopus 로고
    • Insights from selective non-phosphinic inhibitors of MMP-12 tailored to fit with an S1' loop canonical conformation
    • Devel L., Garcia S., Czarny B., Beau F., Lajeunesse E., Vera L., et al. Insights from selective non-phosphinic inhibitors of MMP-12 tailored to fit with an S1' loop canonical conformation. J. Biol. Chem. 2010, 285:35900-35909.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35900-35909
    • Devel, L.1    Garcia, S.2    Czarny, B.3    Beau, F.4    Lajeunesse, E.5    Vera, L.6
  • 38
    • 0033405694 scopus 로고    scopus 로고
    • Resistance of young gelatinase B-deficient mice to experimental autoimmune encephalomyelitis and necrotizing tail lesions
    • Dubois B., Masure S., Hurtenbach U., Paemen L., Heremans H., Van Den Oord J., et al. Resistance of young gelatinase B-deficient mice to experimental autoimmune encephalomyelitis and necrotizing tail lesions. J. Clin. Invest. 1999, 104:1507-1515.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1507-1515
    • Dubois, B.1    Masure, S.2    Hurtenbach, U.3    Paemen, L.4    Heremans, H.5    Van Den Oord, J.6
  • 39
    • 78149282483 scopus 로고    scopus 로고
    • Prospective cohort study of disabling sequelae and quality of life in children with bacterial meningitis in urban Senegal
    • Edmond K., Dieye Y., Griffiths U.K., Fleming J., Ba O., Diallo N., et al. Prospective cohort study of disabling sequelae and quality of life in children with bacterial meningitis in urban Senegal. Pediatr. Infect. Dis. J. 2010, 29:1023-1029.
    • (2010) Pediatr. Infect. Dis. J. , vol.29 , pp. 1023-1029
    • Edmond, K.1    Dieye, Y.2    Griffiths, U.K.3    Fleming, J.4    Ba, O.5    Diallo, N.6
  • 40
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M., Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2002, 2:161-174.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 41
    • 25444533295 scopus 로고    scopus 로고
    • The paradox of matrix metalloproteinases in infectious disease
    • Elkington P.T., O'kane C.M., Friedland J.S. The paradox of matrix metalloproteinases in infectious disease. Clin. Exp. Immunol. 2005, 142:12-20.
    • (2005) Clin. Exp. Immunol. , vol.142 , pp. 12-20
    • Elkington, P.T.1    O'kane, C.M.2    Friedland, J.S.3
  • 42
    • 84869885852 scopus 로고    scopus 로고
    • Capture, crawl, cross: the T cell code to breach the blood-brain barriers
    • Engelhardt B., Ransohoff R.M. Capture, crawl, cross: the T cell code to breach the blood-brain barriers. Trends Immunol. 2012, 33:579-589.
    • (2012) Trends Immunol. , vol.33 , pp. 579-589
    • Engelhardt, B.1    Ransohoff, R.M.2
  • 43
    • 0034333458 scopus 로고    scopus 로고
    • Differential spatial distribution and temporal regulation of tissue inhibitor of metalloproteinase mRNA expression during rat central nervous system development
    • Fager N., Jaworski D.M. Differential spatial distribution and temporal regulation of tissue inhibitor of metalloproteinase mRNA expression during rat central nervous system development. Mech. Dev. 2000, 98:105-109.
    • (2000) Mech. Dev. , vol.98 , pp. 105-109
    • Fager, N.1    Jaworski, D.M.2
  • 44
    • 65349171869 scopus 로고    scopus 로고
    • Potential relevance of cerebrospinal fluid and serum levels and intrathecal synthesis of active matrix metalloproteinase-2 (MMP-2) as markers of disease remission in patients with multiple sclerosis
    • Fainardi E., Castellazzi M., Tamborino C., Trentini A., Manfrinato M.C., Baldi E., et al. Potential relevance of cerebrospinal fluid and serum levels and intrathecal synthesis of active matrix metalloproteinase-2 (MMP-2) as markers of disease remission in patients with multiple sclerosis. Mult. Scler. 2009, 15:547-554.
    • (2009) Mult. Scler. , vol.15 , pp. 547-554
    • Fainardi, E.1    Castellazzi, M.2    Tamborino, C.3    Trentini, A.4    Manfrinato, M.C.5    Baldi, E.6
  • 45
    • 0033836577 scopus 로고    scopus 로고
    • MMP-2 and MMP-9 increase the neurite-promoting potential of schwann cell basal laminae and are upregulated in degenerated nerve
    • Ferguson T.A., Muir D. MMP-2 and MMP-9 increase the neurite-promoting potential of schwann cell basal laminae and are upregulated in degenerated nerve. Mol. Cell. Neurosci. 2000, 16:157-167.
    • (2000) Mol. Cell. Neurosci. , vol.16 , pp. 157-167
    • Ferguson, T.A.1    Muir, D.2
  • 46
    • 36849073658 scopus 로고    scopus 로고
    • MMPs as therapeutic targets-still a viable option?
    • Fingleton B. MMPs as therapeutic targets-still a viable option?. Semin. Cell Dev. Biol. 2008, 19:61-68.
    • (2008) Semin. Cell Dev. Biol. , vol.19 , pp. 61-68
    • Fingleton, B.1
  • 47
  • 48
    • 44049090904 scopus 로고    scopus 로고
    • Collagenase-2 deficiency or inhibition impairs experimental autoimmune encephalomyelitis in mice
    • Folgueras A.R., Fueyo A., Garcia-Suarez O., Cox J., Astudillo A., Tortorella P., et al. Collagenase-2 deficiency or inhibition impairs experimental autoimmune encephalomyelitis in mice. J. Biol. Chem. 2008, 283:9465-9474.
    • (2008) J. Biol. Chem. , vol.283 , pp. 9465-9474
    • Folgueras, A.R.1    Fueyo, A.2    Garcia-Suarez, O.3    Cox, J.4    Astudillo, A.5    Tortorella, P.6
  • 49
    • 70350073423 scopus 로고    scopus 로고
    • Active site ring-opening of a thiirane moiety and picomolar inhibition of gelatinases
    • Forbes C., Shi Q., Fisher J.F., Lee M., Hesek D., Llarrull L.I., et al. Active site ring-opening of a thiirane moiety and picomolar inhibition of gelatinases. Chem. Biol. Drug Des. 2009, 74:527-534.
    • (2009) Chem. Biol. Drug Des. , vol.74 , pp. 527-534
    • Forbes, C.1    Shi, Q.2    Fisher, J.F.3    Lee, M.4    Hesek, D.5    Llarrull, L.I.6
  • 50
    • 84859454286 scopus 로고    scopus 로고
    • The involvement of cleavage of neural cell adhesion molecule in neuronal death under oxidative stress conditions in cultured cortical neurons
    • Fujita-Hamabe W., Tokuyama S. The involvement of cleavage of neural cell adhesion molecule in neuronal death under oxidative stress conditions in cultured cortical neurons. Biol. Pharm. Bull. 2012, 35:624-628.
    • (2012) Biol. Pharm. Bull. , vol.35 , pp. 624-628
    • Fujita-Hamabe, W.1    Tokuyama, S.2
  • 51
    • 0034790897 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their tissue inhibitors as markers of disease subtype and response to interferon-beta therapy in relapsing and secondary-progressive multiple sclerosis patients
    • Galboiz Y., Shapiro S., Lahat N., Rawashdeh H., Miller A. Matrix metalloproteinases and their tissue inhibitors as markers of disease subtype and response to interferon-beta therapy in relapsing and secondary-progressive multiple sclerosis patients. Ann. Neurol. 2001, 50:443-451.
    • (2001) Ann. Neurol. , vol.50 , pp. 443-451
    • Galboiz, Y.1    Shapiro, S.2    Lahat, N.3    Rawashdeh, H.4    Miller, A.5
  • 52
    • 65949120942 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition reduces oxidative stress associated with cerebral amyloid angiopathy in vivo in transgenic mice
    • Garcia-Alloza M., Prada C., Lattarulo C., Fine S., Borrelli L.A., Betensky R., et al. Matrix metalloproteinase inhibition reduces oxidative stress associated with cerebral amyloid angiopathy in vivo in transgenic mice. J. Neurochem. 2009, 109:1636-1647.
    • (2009) J. Neurochem. , vol.109 , pp. 1636-1647
    • Garcia-Alloza, M.1    Prada, C.2    Lattarulo, C.3    Fine, S.4    Borrelli, L.A.5    Betensky, R.6
  • 53
    • 77951950320 scopus 로고    scopus 로고
    • Mechanisms of injury in bacterial meningitis
    • Gerber J., Nau R. Mechanisms of injury in bacterial meningitis. Curr. Opin. Neurol. 2010, 23:312-318.
    • (2010) Curr. Opin. Neurol. , vol.23 , pp. 312-318
    • Gerber, J.1    Nau, R.2
  • 54
    • 2342477273 scopus 로고    scopus 로고
    • Increased mortality and spatial memory deficits in TNF-alpha-deficient mice in ceftriaxone-treated experimental pneumococcal meningitis
    • Gerber J., Bottcher T., Hahn M., Siemer A., Bunkowski S., Nau R. Increased mortality and spatial memory deficits in TNF-alpha-deficient mice in ceftriaxone-treated experimental pneumococcal meningitis. Neurobiol. Dis. 2004, 16:133-138.
    • (2004) Neurobiol. Dis. , vol.16 , pp. 133-138
    • Gerber, J.1    Bottcher, T.2    Hahn, M.3    Siemer, A.4    Bunkowski, S.5    Nau, R.6
  • 56
    • 0027368518 scopus 로고
    • Gelatinase B is present in the cerebrospinal fluid during experimental autoimmune encephalomyelitis and cleaves myelin basic protein
    • Gijbels K., Proost P., Masure S., Carton H., Billiau A., Opdenakker G. Gelatinase B is present in the cerebrospinal fluid during experimental autoimmune encephalomyelitis and cleaves myelin basic protein. J. Neurosci. Res. 1993, 36:432-440.
    • (1993) J. Neurosci. Res. , vol.36 , pp. 432-440
    • Gijbels, K.1    Proost, P.2    Masure, S.3    Carton, H.4    Billiau, A.5    Opdenakker, G.6
  • 57
    • 0028987928 scopus 로고
    • Retroviral infection (HTLV-I) induces cytokine-regulated immunomodulation and cytotoxicity of medulloblastoma cells
    • Giraudon P., Bernard A., Malcus C., Dufay N., Desgranges C., Belin M.F. Retroviral infection (HTLV-I) induces cytokine-regulated immunomodulation and cytotoxicity of medulloblastoma cells. J. Neuropathol. Exp. Neurol. 1995, 54:165-174.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 165-174
    • Giraudon, P.1    Bernard, A.2    Malcus, C.3    Dufay, N.4    Desgranges, C.5    Belin, M.F.6
  • 58
    • 0029077009 scopus 로고
    • Induction of MMP9 (92kDa gelatinase) activity and expression of tissue inhibitor of metalloproteinase-2 mRNA (TIMP-2) in primitive neuroectodermal cells infected with retrovirus HTLV-I
    • Giraudon P., Thomasset N., Bernard A., Verrier B., Belin M.F. Induction of MMP9 (92kDa gelatinase) activity and expression of tissue inhibitor of metalloproteinase-2 mRNA (TIMP-2) in primitive neuroectodermal cells infected with retrovirus HTLV-I. Eur. J. Neurosci. 1995, 7:841-848.
    • (1995) Eur. J. Neurosci. , vol.7 , pp. 841-848
    • Giraudon, P.1    Thomasset, N.2    Bernard, A.3    Verrier, B.4    Belin, M.F.5
  • 59
    • 0030176112 scopus 로고    scopus 로고
    • Extracellular matrix-remodeling metalloproteinases and infection of the central nervous system with retrovirus human T-lymphotropic virus type I (HTLV-I)
    • Giraudon P., Buart S., Bernard A., Thomasset N., Belin M.F. Extracellular matrix-remodeling metalloproteinases and infection of the central nervous system with retrovirus human T-lymphotropic virus type I (HTLV-I). Prog. Neurobiol. 1996, 49:169-184.
    • (1996) Prog. Neurobiol. , vol.49 , pp. 169-184
    • Giraudon, P.1    Buart, S.2    Bernard, A.3    Thomasset, N.4    Belin, M.F.5
  • 60
    • 0030935958 scopus 로고    scopus 로고
    • Cytokines secreted by glial cells infected with HTLV-I modulate the expression of matrix metalloproteinases (MMPs) and their natural inhibitor (TIMPs): possible involvement in neurodegenerative processes
    • 184
    • Giraudon P., Buart S., Bernard A., Belin M.F. Cytokines secreted by glial cells infected with HTLV-I modulate the expression of matrix metalloproteinases (MMPs) and their natural inhibitor (TIMPs): possible involvement in neurodegenerative processes. Mol. Psychiatry 1997, 2:107-110. 184.
    • (1997) Mol. Psychiatry , vol.2 , pp. 107-110
    • Giraudon, P.1    Buart, S.2    Bernard, A.3    Belin, M.F.4
  • 61
    • 70349559752 scopus 로고    scopus 로고
    • Estrogen treatment decreases matrix metalloproteinase (MMP)-9 in autoimmune demyelinating disease through estrogen receptor alpha (ERalpha)
    • Gold S.M., Sasidhar M.V., Morales L.B., Du S., Sicotte N.L., Tiwari-Woodruff S.K., Voskuhl R.R. Estrogen treatment decreases matrix metalloproteinase (MMP)-9 in autoimmune demyelinating disease through estrogen receptor alpha (ERalpha). Lab. Invest. 2009, 89:1076-1083.
    • (2009) Lab. Invest. , vol.89 , pp. 1076-1083
    • Gold, S.M.1    Sasidhar, M.V.2    Morales, L.B.3    Du, S.4    Sicotte, N.L.5    Tiwari-Woodruff, S.K.6    Voskuhl, R.R.7
  • 62
    • 0021677785 scopus 로고
    • Tetracyclines inhibit tissue collagenase activity. A new mechanism in the treatment of periodontal disease
    • Golub L.M., Ramamurthy N., Mcnamara T.F., Gomes B., Wolff M., Casino A., et al. Tetracyclines inhibit tissue collagenase activity. A new mechanism in the treatment of periodontal disease. J. Periodontal Res. 1984, 19:651-655.
    • (1984) J. Periodontal Res. , vol.19 , pp. 651-655
    • Golub, L.M.1    Ramamurthy, N.2    Mcnamara, T.F.3    Gomes, B.4    Wolff, M.5    Casino, A.6
  • 63
    • 62549162557 scopus 로고    scopus 로고
    • Matrix metalloproteinase-12 deficiency worsens relapsing-remitting experimental autoimmune encephalomyelitis in association with cytokine and chemokine dysregulation
    • Goncalves Dasilva A., Yong V.W. Matrix metalloproteinase-12 deficiency worsens relapsing-remitting experimental autoimmune encephalomyelitis in association with cytokine and chemokine dysregulation. Am. J. Pathol. 2009, 174:898-909.
    • (2009) Am. J. Pathol. , vol.174 , pp. 898-909
    • Goncalves Dasilva, A.1    Yong, V.W.2
  • 65
    • 0031596366 scopus 로고    scopus 로고
    • The interrelationship of alpha4 integrin and matrix metalloproteinase-2 in the pathogenesis of experimental autoimmune encephalomyelitis
    • Graesser D., Mahooti S., Haas T., Davis S., Clark R.B., Madri J.A. The interrelationship of alpha4 integrin and matrix metalloproteinase-2 in the pathogenesis of experimental autoimmune encephalomyelitis. Lab. Invest. 1998, 78:1445-1458.
    • (1998) Lab. Invest. , vol.78 , pp. 1445-1458
    • Graesser, D.1    Mahooti, S.2    Haas, T.3    Davis, S.4    Clark, R.B.5    Madri, J.A.6
  • 66
    • 77149180391 scopus 로고    scopus 로고
    • Attenuation of cerebrospinal fluid inflammation by the nonbacteriolytic antibiotic daptomycin versus that by ceftriaxone in experimental pneumococcal meningitis
    • Grandgirard D., Oberson K., Buhlmann A., Gaumann R., Leib S.L. Attenuation of cerebrospinal fluid inflammation by the nonbacteriolytic antibiotic daptomycin versus that by ceftriaxone in experimental pneumococcal meningitis. Antimicrob. Agents Chemother. 2010, 54:1323-1326.
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 1323-1326
    • Grandgirard, D.1    Oberson, K.2    Buhlmann, A.3    Gaumann, R.4    Leib, S.L.5
  • 68
    • 79951658367 scopus 로고    scopus 로고
    • CNS infection, CSF matrix metalloproteinase concentrations, and clinical/laboratory features
    • Green J.A., Thi Hong Chau T., Farrar J.J., Friedland J.S., Thwaites G.E. CNS infection, CSF matrix metalloproteinase concentrations, and clinical/laboratory features. Neurology 2011, 76:577-579.
    • (2011) Neurology , vol.76 , pp. 577-579
    • Green, J.A.1    Thi Hong Chau, T.2    Farrar, J.J.3    Friedland, J.S.4    Thwaites, G.E.5
  • 69
    • 0345935809 scopus 로고
    • Collagenolytic activity in amphibian tissues: a tissue culture assay
    • Gross J., Lapiere C.M. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc. Natl. Acad. Sci. USA 1962, 48:1014-1022.
    • (1962) Proc. Natl. Acad. Sci. USA , vol.48 , pp. 1014-1022
    • Gross, J.1    Lapiere, C.M.2
  • 70
    • 0037119624 scopus 로고    scopus 로고
    • S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death
    • Gu Z., Kaul M., Yan B., Kridel S.J., Cui J., Strongin A., et al. S-nitrosylation of matrix metalloproteinases: signaling pathway to neuronal cell death. Science 2002, 297:1186-1190.
    • (2002) Science , vol.297 , pp. 1186-1190
    • Gu, Z.1    Kaul, M.2    Yan, B.3    Kridel, S.J.4    Cui, J.5    Strongin, A.6
  • 71
    • 21844450866 scopus 로고    scopus 로고
    • A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia
    • Gu Z., Cui J., Brown S., Fridman R., Mobashery S., Strongin A.Y., Lipton S.A. A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia. J. Neurosci. 2005, 25:6401-6408.
    • (2005) J. Neurosci. , vol.25 , pp. 6401-6408
    • Gu, Z.1    Cui, J.2    Brown, S.3    Fridman, R.4    Mobashery, S.5    Strongin, A.Y.6    Lipton, S.A.7
  • 72
    • 33748300970 scopus 로고    scopus 로고
    • Effects of apoE isoforms on beta-amyloid-induced matrix metalloproteinase-9 in rat astrocytes
    • Guo S., Wang S., Kim W.J., Lee S.R., Frosch M.P., Bacskai B.J., et al. Effects of apoE isoforms on beta-amyloid-induced matrix metalloproteinase-9 in rat astrocytes. Brain Res. 2006, 1111:222-226.
    • (2006) Brain Res. , vol.1111 , pp. 222-226
    • Guo, S.1    Wang, S.2    Kim, W.J.3    Lee, S.R.4    Frosch, M.P.5    Bacskai, B.J.6
  • 73
    • 77953540128 scopus 로고    scopus 로고
    • Role of matrix metalloproteinase-9 in apoptosis of hippocampal neurons in rats during early brain injury after subarachnoid hemorrhage
    • Guo Z., Sun X., He Z., Jiang Y., Zhang X. Role of matrix metalloproteinase-9 in apoptosis of hippocampal neurons in rats during early brain injury after subarachnoid hemorrhage. Neurol. Sci. 2010, 31:143-149.
    • (2010) Neurol. Sci. , vol.31 , pp. 143-149
    • Guo, Z.1    Sun, X.2    He, Z.3    Jiang, Y.4    Zhang, X.5
  • 74
    • 84886057065 scopus 로고    scopus 로고
    • Selective inhibition of matrix metalloproteinase-9 attenuates secondary damage resulting from severe traumatic brain injury
    • Hadass O., Tomlinson B.N., Gooyit M., Chen S., Purdy J.J., Walker J.M., et al. Selective inhibition of matrix metalloproteinase-9 attenuates secondary damage resulting from severe traumatic brain injury. PLoS One 2013, 8:e76904.
    • (2013) PLoS One , vol.8 , pp. e76904
    • Hadass, O.1    Tomlinson, B.N.2    Gooyit, M.3    Chen, S.4    Purdy, J.J.5    Walker, J.M.6
  • 76
    • 15444347160 scopus 로고    scopus 로고
    • Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline
    • Hanemaaijer R., Sorsa T., Konttinen Y.T., Ding Y., Sutinen M., Visser H., et al. Matrix metalloproteinase-8 is expressed in rheumatoid synovial fibroblasts and endothelial cells. Regulation by tumor necrosis factor-alpha and doxycycline. J. Biol. Chem. 1997, 272:31504-31509.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31504-31509
    • Hanemaaijer, R.1    Sorsa, T.2    Konttinen, Y.T.3    Ding, Y.4    Sutinen, M.5    Visser, H.6
  • 77
    • 0034710362 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases in autoimmune damage to the central and peripheral nervous system
    • Hartung H.P., Kieseier B.C. The role of matrix metalloproteinases in autoimmune damage to the central and peripheral nervous system. J. Neuroimmunol. 2000, 107:140-147.
    • (2000) J. Neuroimmunol. , vol.107 , pp. 140-147
    • Hartung, H.P.1    Kieseier, B.C.2
  • 78
    • 65849506917 scopus 로고    scopus 로고
    • Neuronal TIMP-1 release accompanies astrocytic MMP-9 secretion and enhances astrocyte proliferation induced by beta-amyloid 25-35 fragment
    • Hernandez-Guillamon M., Delgado P., Ortega L., Pares M., Rosell A., Garcia-Bonilla L., et al. Neuronal TIMP-1 release accompanies astrocytic MMP-9 secretion and enhances astrocyte proliferation induced by beta-amyloid 25-35 fragment. J. Neurosci. Res. 2009, 87:2115-2125.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 2115-2125
    • Hernandez-Guillamon, M.1    Delgado, P.2    Ortega, L.3    Pares, M.4    Rosell, A.5    Garcia-Bonilla, L.6
  • 79
    • 77956232864 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 (MMP-2) degrades soluble vasculotropic amyloid-beta E22Q and L34V mutants, delaying their toxicity for human brain microvascular endothelial cells
    • Hernandez-Guillamon M., Mawhirt S., Fossati S., Blais S., Pares M., Penalba A., et al. Matrix metalloproteinase 2 (MMP-2) degrades soluble vasculotropic amyloid-beta E22Q and L34V mutants, delaying their toxicity for human brain microvascular endothelial cells. J. Biol. Chem. 2010, 285:27144-27158.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27144-27158
    • Hernandez-Guillamon, M.1    Mawhirt, S.2    Fossati, S.3    Blais, S.4    Pares, M.5    Penalba, A.6
  • 80
    • 0029046464 scopus 로고
    • Suppression of experimental allergic encephalomyelitis in the Lewis rat by the matrix metalloproteinase inhibitor Ro31-9790
    • Hewson A.K., Smith T., Leonard J.P., Cuzner M.L. Suppression of experimental allergic encephalomyelitis in the Lewis rat by the matrix metalloproteinase inhibitor Ro31-9790. Inflamm. Res. 1995, 44:345-349.
    • (1995) Inflamm. Res. , vol.44 , pp. 345-349
    • Hewson, A.K.1    Smith, T.2    Leonard, J.P.3    Cuzner, M.L.4
  • 81
    • 0037687306 scopus 로고    scopus 로고
    • Identification of a region of beta-amyloid precursor protein essential for its gelatinase A inhibitory activity
    • Higashi S., Miyazaki K. Identification of a region of beta-amyloid precursor protein essential for its gelatinase A inhibitory activity. J. Biol. Chem. 2003, 278:14020-14028.
    • (2003) J. Biol. Chem. , vol.278 , pp. 14020-14028
    • Higashi, S.1    Miyazaki, K.2
  • 82
    • 0038052349 scopus 로고    scopus 로고
    • Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase A
    • Higashi S., Miyazaki K. Novel processing of beta-amyloid precursor protein catalyzed by membrane type 1 matrix metalloproteinase releases a fragment lacking the inhibitor domain against gelatinase A. Biochemistry 2003, 42:6514-6526.
    • (2003) Biochemistry , vol.42 , pp. 6514-6526
    • Higashi, S.1    Miyazaki, K.2
  • 83
    • 35148831212 scopus 로고    scopus 로고
    • The metalloprotease inhibitor TIMP-3 regulates amyloid precursor protein and apolipoprotein E receptor proteolysis
    • Hoe H.S., Cooper M.J., Burns M.P., Lewis P.A., Van Der Brug M., Chakraborty G., et al. The metalloprotease inhibitor TIMP-3 regulates amyloid precursor protein and apolipoprotein E receptor proteolysis. J. Neurosci. 2007, 27:10895-10905.
    • (2007) J. Neurosci. , vol.27 , pp. 10895-10905
    • Hoe, H.S.1    Cooper, M.J.2    Burns, M.P.3    Lewis, P.A.4    Van Der Brug, M.5    Chakraborty, G.6
  • 84
    • 34447520043 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
    • Hu J., Van Den Steen P.E., Sang Q.X., Opdenakker G. Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases. Nat. Rev. Drug Discov. 2007, 6:480-498.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 480-498
    • Hu, J.1    Van Den Steen, P.E.2    Sang, Q.X.3    Opdenakker, G.4
  • 86
    • 33645892563 scopus 로고    scopus 로고
    • A cassette-dosing approach for improvement of oral bioavailability of dual TACE/MMP inhibitors
    • Janser P., Neumann U., Miltz W., Feifel R., Buhl T. A cassette-dosing approach for improvement of oral bioavailability of dual TACE/MMP inhibitors. Bioorg. Med. Chem. Lett. 2006, 16:2632-2636.
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 2632-2636
    • Janser, P.1    Neumann, U.2    Miltz, W.3    Feifel, R.4    Buhl, T.5
  • 87
    • 0034076682 scopus 로고    scopus 로고
    • Differential regulation of tissue inhibitor of metalloproteinase mRNA expression in response to intracranial injury
    • Jaworski D.M. Differential regulation of tissue inhibitor of metalloproteinase mRNA expression in response to intracranial injury. Glia 2000, 30:199-208.
    • (2000) Glia , vol.30 , pp. 199-208
    • Jaworski, D.M.1
  • 88
    • 22144470855 scopus 로고    scopus 로고
    • Prepulse inhibition and fear-potentiated startle are altered in tissue inhibitor of metalloproteinase-2 (TIMP-2) knockout mice
    • Jaworski D.M., Boone J., Caterina J., Soloway P., Falls W.A. Prepulse inhibition and fear-potentiated startle are altered in tissue inhibitor of metalloproteinase-2 (TIMP-2) knockout mice. Brain Res. 2005, 1051:81-89.
    • (2005) Brain Res. , vol.1051 , pp. 81-89
    • Jaworski, D.M.1    Boone, J.2    Caterina, J.3    Soloway, P.4    Falls, W.A.5
  • 90
    • 84903826557 scopus 로고    scopus 로고
    • MMP-9 inhibitor SB-3CT attenuates behavioral impairments and hippocampal loss after traumatic brain injury in rat
    • Jiang J.Y., Jia F., Yin Y., Gao G., Wang Y., Cen L. MMP-9 inhibitor SB-3CT attenuates behavioral impairments and hippocampal loss after traumatic brain injury in rat. J. Neurotrauma 2014, 31:1225-1234.
    • (2014) J. Neurotrauma , vol.31 , pp. 1225-1234
    • Jiang, J.Y.1    Jia, F.2    Yin, Y.3    Gao, G.4    Wang, Y.5    Cen, L.6
  • 93
    • 0038241040 scopus 로고    scopus 로고
    • Pathogenic A beta induces the expression and activation of matrix metalloproteinase-2 in human cerebrovascular smooth muscle cells
    • Jung S.S., Zhang W., Van Nostrand W.E. Pathogenic A beta induces the expression and activation of matrix metalloproteinase-2 in human cerebrovascular smooth muscle cells. J. Neurochem. 2003, 85:1208-1215.
    • (2003) J. Neurochem. , vol.85 , pp. 1208-1215
    • Jung, S.S.1    Zhang, W.2    Van Nostrand, W.E.3
  • 94
    • 0037121996 scopus 로고    scopus 로고
    • Matrix metalloproteinases in the adult brain physiology: a link between c-Fos, AP-1 and remodeling of neuronal connections?
    • Kaczmarek L., Lapinska-Dzwonek J., Szymczak S. Matrix metalloproteinases in the adult brain physiology: a link between c-Fos, AP-1 and remodeling of neuronal connections?. EMBO J. 2002, 21:6643-6648.
    • (2002) EMBO J. , vol.21 , pp. 6643-6648
    • Kaczmarek, L.1    Lapinska-Dzwonek, J.2    Szymczak, S.3
  • 95
    • 84857647125 scopus 로고    scopus 로고
    • Expression and activation of matrix metalloproteinase-9 and NADPH oxidase in tissues and plasma of experimental autoimmune encephalomyelitis in mice
    • Kandagaddala L.D., Kang M.J., Chung B.C., Patterson T.A., Kwon O.S. Expression and activation of matrix metalloproteinase-9 and NADPH oxidase in tissues and plasma of experimental autoimmune encephalomyelitis in mice. Exp. Toxicol. Pathol. 2012, 64:109-114.
    • (2012) Exp. Toxicol. Pathol. , vol.64 , pp. 109-114
    • Kandagaddala, L.D.1    Kang, M.J.2    Chung, B.C.3    Patterson, T.A.4    Kwon, O.S.5
  • 96
    • 78449294632 scopus 로고    scopus 로고
    • Redox-control of matrix metalloproteinase-1: a critical link between free radicals, matrix remodeling and degenerative disease
    • Kar S., Subbaram S., Carrico P.M., Melendez J.A. Redox-control of matrix metalloproteinase-1: a critical link between free radicals, matrix remodeling and degenerative disease. Respir. Physiol. Neurobiol. 2010, 174:299-306.
    • (2010) Respir. Physiol. Neurobiol. , vol.174 , pp. 299-306
    • Kar, S.1    Subbaram, S.2    Carrico, P.M.3    Melendez, J.A.4
  • 97
    • 0142090406 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibitors, modulators of neuro-immune interactions and of pathophysiological processes in the nervous system
    • Khrestchatisky M., Jourquin J., Ogier C., Charton G., Bernard A., Tremblay E., Rivera S. Matrix metalloproteinases and their inhibitors, modulators of neuro-immune interactions and of pathophysiological processes in the nervous system. J. Soc. Biol. 2003, 197:133-144.
    • (2003) J. Soc. Biol. , vol.197 , pp. 133-144
    • Khrestchatisky, M.1    Jourquin, J.2    Ogier, C.3    Charton, G.4    Bernard, A.5    Tremblay, E.6    Rivera, S.7
  • 99
    • 0032816550 scopus 로고    scopus 로고
    • Differential expression of matrix metalloproteinases in bacterial meningitis
    • Kieseier B.C., Paul R., Koedel U., Seifert T., Clements J.M., Gearing A.J., et al. Differential expression of matrix metalloproteinases in bacterial meningitis. Brain 1999, 122:1579-1587.
    • (1999) Brain , vol.122 , pp. 1579-1587
    • Kieseier, B.C.1    Paul, R.2    Koedel, U.3    Seifert, T.4    Clements, J.M.5    Gearing, A.J.6
  • 100
    • 0037868085 scopus 로고    scopus 로고
    • Pathogenesis of bacterial meningitis: from bacteriaemia to neuronal injury
    • Kim K.S. Pathogenesis of bacterial meningitis: from bacteriaemia to neuronal injury. Nat. Rev. Neurosci. 2003, 4:376-385.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 376-385
    • Kim, K.S.1
  • 101
    • 72149117409 scopus 로고    scopus 로고
    • Acute bacterial meningitis in infants and children
    • Kim K.S. Acute bacterial meningitis in infants and children. Lancet Infect. Dis. 2010, 10:32-42.
    • (2010) Lancet Infect. Dis. , vol.10 , pp. 32-42
    • Kim, K.S.1
  • 102
    • 0037393866 scopus 로고    scopus 로고
    • Morphological correlates of acute and permanent hearing loss during experimental pneumococcal meningitis
    • Klein M., Koedel U., Pfister H.W., Kastenbauer S. Morphological correlates of acute and permanent hearing loss during experimental pneumococcal meningitis. Brain Pathol. 2003, 13:123-132.
    • (2003) Brain Pathol. , vol.13 , pp. 123-132
    • Klein, M.1    Koedel, U.2    Pfister, H.W.3    Kastenbauer, S.4
  • 103
    • 0036900042 scopus 로고    scopus 로고
    • Pathogenesis and pathophysiology of pneumococcal meningitis
    • Koedel U., Scheld W.M., Pfister H.W. Pathogenesis and pathophysiology of pneumococcal meningitis. Lancet Infect. Dis. 2002, 2:721-736.
    • (2002) Lancet Infect. Dis. , vol.2 , pp. 721-736
    • Koedel, U.1    Scheld, W.M.2    Pfister, H.W.3
  • 104
    • 0037220060 scopus 로고    scopus 로고
    • Toll-like receptor 2 participates in mediation of immune response in experimental pneumococcal meningitis
    • Koedel U., Angele B., Rupprecht T., Wagner H., Roggenkamp A., Pfister H.W., et al. Toll-like receptor 2 participates in mediation of immune response in experimental pneumococcal meningitis. J. Immunol. 2003, 170:438-444.
    • (2003) J. Immunol. , vol.170 , pp. 438-444
    • Koedel, U.1    Angele, B.2    Rupprecht, T.3    Wagner, H.4    Roggenkamp, A.5    Pfister, H.W.6
  • 105
    • 17044364404 scopus 로고    scopus 로고
    • Minocycline protects against permanent cerebral ischemia in wild type but not in matrix metalloprotease-9-deficient mice
    • Koistinaho M., Malm T.M., Kettunen M.I., Goldsteins G., Starckx S., Kauppinen R.A., et al. Minocycline protects against permanent cerebral ischemia in wild type but not in matrix metalloprotease-9-deficient mice. J. Cereb. Blood Flow Metab. 2005, 25:460-467.
    • (2005) J. Cereb. Blood Flow Metab. , vol.25 , pp. 460-467
    • Koistinaho, M.1    Malm, T.M.2    Kettunen, M.I.3    Goldsteins, G.4    Starckx, S.5    Kauppinen, R.A.6
  • 106
    • 0032522261 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases in viral meningitis: upregulation of MMP-9 and TIMP-1 in cerebrospinal fluid
    • Kolb S.A., Lahrtz F., Paul R., Leppert D., Nadal D., Pfister H.W., Fontana A. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in viral meningitis: upregulation of MMP-9 and TIMP-1 in cerebrospinal fluid. J. Neuroimmunol. 1998, 84:143-150.
    • (1998) J. Neuroimmunol. , vol.84 , pp. 143-150
    • Kolb, S.A.1    Lahrtz, F.2    Paul, R.3    Leppert, D.4    Nadal, D.5    Pfister, H.W.6    Fontana, A.7
  • 108
    • 56949088583 scopus 로고    scopus 로고
    • Antibiotic treatment delay and outcome in acute bacterial meningitis
    • Koster-Rasmussen R., Korshin A., Meyer C.N. Antibiotic treatment delay and outcome in acute bacterial meningitis. J. Infect. 2008, 57:449-454.
    • (2008) J. Infect. , vol.57 , pp. 449-454
    • Koster-Rasmussen, R.1    Korshin, A.2    Meyer, C.N.3
  • 109
    • 77956392552 scopus 로고    scopus 로고
    • ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons
    • Kuhn P.H., Wang H., Dislich B., Colombo A., Zeitschel U., Ellwart J.W., et al. ADAM10 is the physiologically relevant, constitutive alpha-secretase of the amyloid precursor protein in primary neurons. EMBO J. 2010, 29:3020-3032.
    • (2010) EMBO J. , vol.29 , pp. 3020-3032
    • Kuhn, P.H.1    Wang, H.2    Dislich, B.3    Colombo, A.4    Zeitschel, U.5    Ellwart, J.W.6
  • 110
    • 33645643179 scopus 로고    scopus 로고
    • Myelin formation during development of the CNS is delayed in matrix metalloproteinase-9 and -12 null mice
    • Larsen P.H., Dasilva A.G., Conant K., Yong V.W. Myelin formation during development of the CNS is delayed in matrix metalloproteinase-9 and -12 null mice. J. Neurosci. 2006, 26:2207-2214.
    • (2006) J. Neurosci. , vol.26 , pp. 2207-2214
    • Larsen, P.H.1    Dasilva, A.G.2    Conant, K.3    Yong, V.W.4
  • 111
    • 33646551934 scopus 로고    scopus 로고
    • Dose-response effect of tetracyclines on cerebral matrix metalloproteinase-9 after vascular endothelial growth factor hyperstimulation
    • Lee C.Z., Yao J.S., Huang Y., Zhai W., Liu W., et al. Dose-response effect of tetracyclines on cerebral matrix metalloproteinase-9 after vascular endothelial growth factor hyperstimulation. J. Cereb. Blood Flow Metab. 2006, 26:1157-1164.
    • (2006) J. Cereb. Blood Flow Metab. , vol.26 , pp. 1157-1164
    • Lee, C.Z.1    Yao, J.S.2    Huang, Y.3    Zhai, W.4    Liu, W.5
  • 112
    • 0033984374 scopus 로고    scopus 로고
    • Matrix metalloproteinases contribute to brain damage in experimental pneumococcal meningitis
    • Leib S.L., Leppert D., Clements J., Tauber M.G. Matrix metalloproteinases contribute to brain damage in experimental pneumococcal meningitis. Infect. Immun. 2000, 68:615-620.
    • (2000) Infect. Immun. , vol.68 , pp. 615-620
    • Leib, S.L.1    Leppert, D.2    Clements, J.3    Tauber, M.G.4
  • 113
    • 0034845846 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases and tumour necrosis factor alpha converting enzyme as adjuvant therapy in pneumococcal meningitis
    • Leib S.L., Clements J.M., Lindberg R.L., Heimgartner C., Loeffler J.M., Pfister L.A., Tauber M.G., Leppert D. Inhibition of matrix metalloproteinases and tumour necrosis factor alpha converting enzyme as adjuvant therapy in pneumococcal meningitis. Brain 2001, 124:1734-1742.
    • (2001) Brain , vol.124 , pp. 1734-1742
    • Leib, S.L.1    Clements, J.M.2    Lindberg, R.L.3    Heimgartner, C.4    Loeffler, J.M.5    Pfister, L.A.6    Tauber, M.G.7    Leppert, D.8
  • 114
    • 0041467288 scopus 로고    scopus 로고
    • Dexamethasone aggravates hippocampal apoptosis and learning deficiency in pneumococcal meningitis in infant rats
    • Leib S.L., Heimgartner C., Bifrare Y.D., Loeffler J.M., Taauber M.G. Dexamethasone aggravates hippocampal apoptosis and learning deficiency in pneumococcal meningitis in infant rats. Pediatr. Res. 2003, 54:353-357.
    • (2003) Pediatr. Res. , vol.54 , pp. 353-357
    • Leib, S.L.1    Heimgartner, C.2    Bifrare, Y.D.3    Loeffler, J.M.4    Taauber, M.G.5
  • 115
    • 0034455606 scopus 로고    scopus 로고
    • Matrix metalloproteinase (MMP)-8 and MMP-9 in cerebrospinal fluid during bacterial meningitis: association with blood-brain barrier damage and neurological sequelae
    • Leppert D., Leib S.L., Grygar C., Miller K.M., Schaad U.B., Hollander G.A. Matrix metalloproteinase (MMP)-8 and MMP-9 in cerebrospinal fluid during bacterial meningitis: association with blood-brain barrier damage and neurological sequelae. Clin. Infect. Dis. 2000, 31:80-84.
    • (2000) Clin. Infect. Dis. , vol.31 , pp. 80-84
    • Leppert, D.1    Leib, S.L.2    Grygar, C.3    Miller, K.M.4    Schaad, U.B.5    Hollander, G.A.6
  • 116
    • 0034749944 scopus 로고    scopus 로고
    • Matrix metalloproteinases: multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis
    • Leppert D., Lindberg R.L., Kappos L., Leib S.L. Matrix metalloproteinases: multifunctional effectors of inflammation in multiple sclerosis and bacterial meningitis. Brain Res. Brain Res. Rev. 2001, 36:249-257.
    • (2001) Brain Res. Brain Res. Rev. , vol.36 , pp. 249-257
    • Leppert, D.1    Lindberg, R.L.2    Kappos, L.3    Leib, S.L.4
  • 117
    • 76749099393 scopus 로고    scopus 로고
    • Degradation of soluble and fibrillar amyloid beta-protein by matrix metalloproteinase (MT1-MMP) in vitro
    • Liao M.C., Van Nostrand W.E. Degradation of soluble and fibrillar amyloid beta-protein by matrix metalloproteinase (MT1-MMP) in vitro. Biochemistry 2010, 49:1127-1136.
    • (2010) Biochemistry , vol.49 , pp. 1127-1136
    • Liao, M.C.1    Van Nostrand, W.E.2
  • 118
    • 0032828062 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-9 and its inhibitors in mononuclear blood cells of patients with multiple sclerosis
    • Lichtinghagen R., Seifert T., Kracke A., Marckmann S., Wurster U., Heidenreich F. Expression of matrix metalloproteinase-9 and its inhibitors in mononuclear blood cells of patients with multiple sclerosis. J. Neuroimmunol. 1999, 99:19-26.
    • (1999) J. Neuroimmunol. , vol.99 , pp. 19-26
    • Lichtinghagen, R.1    Seifert, T.2    Kracke, A.3    Marckmann, S.4    Wurster, U.5    Heidenreich, F.6
  • 119
    • 84896447812 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition lowers mortality and brain injury in experimental pneumococcal meningitis
    • Liechti F.D., Grandgirard D., Leppert D., Leib S.L. Matrix metalloproteinase inhibition lowers mortality and brain injury in experimental pneumococcal meningitis. Infect. Immun. 2014, 82:1710-1718.
    • (2014) Infect. Immun. , vol.82 , pp. 1710-1718
    • Liechti, F.D.1    Grandgirard, D.2    Leppert, D.3    Leib, S.L.4
  • 120
    • 33646096986 scopus 로고    scopus 로고
    • Gelatinase B [matrix metalloproteinase (MMP)-9] and collagenases (MMP-8/-13) are upregulated in cerebrospinal fluid during aseptic and bacterial meningitis in children
    • Lindberg R.L., Sorsa T., Tervahartiala T., Hoffmann F., Mellanen L., Kappos L., Schaad U.B., Leib S.L., Leppert D. Gelatinase B [matrix metalloproteinase (MMP)-9] and collagenases (MMP-8/-13) are upregulated in cerebrospinal fluid during aseptic and bacterial meningitis in children. Neuropathol. Appl. Neurobiol. 2006, 32:304-317.
    • (2006) Neuropathol. Appl. Neurobiol. , vol.32 , pp. 304-317
    • Lindberg, R.L.1    Sorsa, T.2    Tervahartiala, T.3    Hoffmann, F.4    Mellanen, L.5    Kappos, L.6    Schaad, U.B.7    Leib, S.L.8    Leppert, D.9
  • 121
    • 41949132711 scopus 로고    scopus 로고
    • Dexamethasone regulation of matrix metalloproteinase expression in experimental pneumococcal meningitis
    • Liu X., Han Q., Sun R., Li Z. Dexamethasone regulation of matrix metalloproteinase expression in experimental pneumococcal meningitis. Brain Res. 2008, 1207:237-243.
    • (2008) Brain Res. , vol.1207 , pp. 237-243
    • Liu, X.1    Han, Q.2    Sun, R.3    Li, Z.4
  • 122
    • 0035863578 scopus 로고    scopus 로고
    • The free radical scavenger alpha-phenyl-tert-butyl nitrone aggravates hippocampal apoptosis and learning deficits in experimental pneumococcal meningitis
    • Loeffler J.M., Ringer R., Hablutzel M., Tauber M.G., Leib S.L. The free radical scavenger alpha-phenyl-tert-butyl nitrone aggravates hippocampal apoptosis and learning deficits in experimental pneumococcal meningitis. J. Infect. Dis. 2001, 183:247-252.
    • (2001) J. Infect. Dis. , vol.183 , pp. 247-252
    • Loeffler, J.M.1    Ringer, R.2    Hablutzel, M.3    Tauber, M.G.4    Leib, S.L.5
  • 124
    • 0024675010 scopus 로고
    • NGF induction of the gene encoding the protease transin accompanies neuronal differentiation in PC12
    • Machida C.M., Rodland K.D., Matrisian L., Magun B.E., Ciment G. NGF induction of the gene encoding the protease transin accompanies neuronal differentiation in PC12. Neuron 1989, 2:1587-1596.
    • (1989) Neuron , vol.2 , pp. 1587-1596
    • Machida, C.M.1    Rodland, K.D.2    Matrisian, L.3    Magun, B.E.4    Ciment, G.5
  • 126
    • 0033610854 scopus 로고    scopus 로고
    • Regulation of carboxyl-terminal domain phosphatase by HIV-1 tat protein
    • Marshall N.F., Dahmus G.K., Dahmus M.E. Regulation of carboxyl-terminal domain phosphatase by HIV-1 tat protein. J. Biol. Chem. 1998, 273:31726-31730.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31726-31730
    • Marshall, N.F.1    Dahmus, G.K.2    Dahmus, M.E.3
  • 128
    • 0025997534 scopus 로고
    • Kinetics and physiologic relevance of the inactivation of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin)
    • Mast A.E., Enghild J.J., Nagase H., Suzuki K., Pizzo S.V., Salvesen G. Kinetics and physiologic relevance of the inactivation of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, and antithrombin III by matrix metalloproteinases-1 (tissue collagenase), -2 (72-kDa gelatinase/type IV collagenase), and -3 (stromelysin). J. Biol. Chem. 1991, 266:15810-15816.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15810-15816
    • Mast, A.E.1    Enghild, J.J.2    Nagase, H.3    Suzuki, K.4    Pizzo, S.V.5    Salvesen, G.6
  • 130
    • 33645103421 scopus 로고    scopus 로고
    • 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., et al. Effects of extracellular matrix-degrading proteases matrix metalloproteinases 3 and 9 on spatial learning and synaptic plasticity. J. Neurochem. 2006, 96:1227-1241.
    • (2006) J. Neurochem. , vol.96 , pp. 1227-1241
    • Meighan, S.E.1    Meighan, P.C.2    Choudhury, P.3    Davis, C.J.4    Olson, M.L.5    Zornes, P.A.6
  • 131
    • 0037738484 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 in pneumococcal meningitis: activation via an oxidative pathway
    • Meli D.N., Christen S., Leib S.L. Matrix metalloproteinase-9 in pneumococcal meningitis: activation via an oxidative pathway. J. Infect. Dis. 2003, 187:1411-1415.
    • (2003) J. Infect. Dis. , vol.187 , pp. 1411-1415
    • Meli, D.N.1    Christen, S.2    Leib, S.L.3
  • 132
    • 2442451453 scopus 로고    scopus 로고
    • In pneumococcal meningitis a novel water-soluble inhibitor of matrix metalloproteinases and TNF-alpha converting enzyme attenuates seizures and injury of the cerebral cortex
    • Meli D.N., Loeffler J.M., Baumann P., Neumann U., Buhl T., Leppert D., Leib S.L. In pneumococcal meningitis a novel water-soluble inhibitor of matrix metalloproteinases and TNF-alpha converting enzyme attenuates seizures and injury of the cerebral cortex. J. Neuroimmunol. 2004, 151:6-11.
    • (2004) J. Neuroimmunol. , vol.151 , pp. 6-11
    • Meli, D.N.1    Loeffler, J.M.2    Baumann, P.3    Neumann, U.4    Buhl, T.5    Leppert, D.6    Leib, S.L.7
  • 134
    • 34249672834 scopus 로고    scopus 로고
    • The reversion-inducing cysteine-rich protein with Kazal motifs (RECK) interacts with membrane type 1 matrix metalloproteinase and CD13/aminopeptidase N and modulates their endocytic pathways
    • Miki T., Takegami Y., Okawa K., Muraguchi T., Noda M., Takahashi C. The reversion-inducing cysteine-rich protein with Kazal motifs (RECK) interacts with membrane type 1 matrix metalloproteinase and CD13/aminopeptidase N and modulates their endocytic pathways. J. Biol. Chem. 2007, 282:12341-12352.
    • (2007) J. Biol. Chem. , vol.282 , pp. 12341-12352
    • Miki, T.1    Takegami, Y.2    Okawa, K.3    Muraguchi, T.4    Noda, M.5    Takahashi, C.6
  • 136
    • 70349330693 scopus 로고    scopus 로고
    • Matrix metalloprotease-9 inhibition improves amyloid beta-mediated cognitive impairment and neurotoxicity in mice
    • Mizoguchi H., Takuma K., Fukuzaki E., Ibi D., Someya E., Akazawa K.H., et al. Matrix metalloprotease-9 inhibition improves amyloid beta-mediated cognitive impairment and neurotoxicity in mice. J. Pharmacol. Exp. Ther. 2009, 331:14-22.
    • (2009) J. Pharmacol. Exp. Ther. , vol.331 , pp. 14-22
    • Mizoguchi, H.1    Takuma, K.2    Fukuzaki, E.3    Ibi, D.4    Someya, E.5    Akazawa, K.H.6
  • 138
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss M.L., Jin S.L., Milla M.E., Bickett D.M., Burkhart W., Carter H.L., et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 1997, 385:733-736.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Bickett, D.M.4    Burkhart, W.5    Carter, H.L.6
  • 139
    • 0033955104 scopus 로고    scopus 로고
    • Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor
    • Mott J.D., Thomas C.L., Rosenbach M.T., Takahara K., Greenspan D.S., Banda M.J. Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor. J. Biol. Chem. 2000, 275:1384-1390.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1384-1390
    • Mott, J.D.1    Thomas, C.L.2    Rosenbach, M.T.3    Takahara, K.4    Greenspan, D.S.5    Banda, M.J.6
  • 140
    • 84901930783 scopus 로고    scopus 로고
    • Concentrations of matrix metalloproteinases and their tissue inhibitors in the cerebrospinal fluid of patients with Alzheimer's disease
    • Mroczko B., Groblewska M., Zboch M., Kulczynska A., Koper O.M., Szmitkowski M., et al. Concentrations of matrix metalloproteinases and their tissue inhibitors in the cerebrospinal fluid of patients with Alzheimer's disease. J. Alzheimers Dis. 2014, 40:351-357.
    • (2014) J. Alzheimers Dis. , vol.40 , pp. 351-357
    • Mroczko, B.1    Groblewska, M.2    Zboch, M.3    Kulczynska, A.4    Koper, O.M.5    Szmitkowski, M.6
  • 141
    • 0031831764 scopus 로고    scopus 로고
    • Gelatinase B modulates selective opening of the blood-brain barrier during inflammation
    • Mun-Bryce S., Rosenberg G.A. Gelatinase B modulates selective opening of the blood-brain barrier during inflammation. Am. J. Physiol. 1998, 274:R1203-R1211.
    • (1998) Am. J. Physiol. , vol.274 , pp. R1203-R1211
    • Mun-Bryce, S.1    Rosenberg, G.A.2
  • 142
    • 34347329150 scopus 로고    scopus 로고
    • RECK modulates Notch signaling during cortical neurogenesis by regulating ADAM10 activity
    • Muraguchi T., Takegami Y., Ohtsuka T., Kitajima S., Chandana E.P., Omura A., et al. RECK modulates Notch signaling during cortical neurogenesis by regulating ADAM10 activity. Nat. Neurosci. 2007, 10:838-845.
    • (2007) Nat. Neurosci. , vol.10 , pp. 838-845
    • Muraguchi, T.1    Takegami, Y.2    Ohtsuka, T.3    Kitajima, S.4    Chandana, E.P.5    Omura, A.6
  • 143
    • 84859508075 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 regulates survival of neurons in newborn hippocampus
    • Murase S., Mckay R.D. Matrix metalloproteinase-9 regulates survival of neurons in newborn hippocampus. J. Biol. Chem. 2012, 287:12184-12194.
    • (2012) J. Biol. Chem. , vol.287 , pp. 12184-12194
    • Murase, S.1    Mckay, R.D.2
  • 144
    • 81255188391 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases
    • Murphy G. Tissue inhibitors of metalloproteinases. Genome Biol. 2011, 12:233.
    • (2011) Genome Biol. , vol.12 , pp. 233
    • Murphy, G.1
  • 145
    • 33644522107 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 is required for hippocampal late-phase long-term potentiation and memory
    • Nagy V., Bozdagi O., Matynia A., Balcerzyk M., Okulski P., Dzwonek J., et al. Matrix metalloproteinase-9 is required for hippocampal late-phase long-term potentiation and memory. J. Neurosci. 2006, 26:1923-1934.
    • (2006) J. Neurosci. , vol.26 , pp. 1923-1934
    • Nagy, V.1    Bozdagi, O.2    Matynia, A.3    Balcerzyk, M.4    Okulski, P.5    Dzwonek, J.6
  • 147
    • 0027183404 scopus 로고
    • Numerous candidate plasticity-related genes revealed by differential cDNA cloning
    • Nedivi E., Hevroni D., Naot D., Israeli D., Citri Y. Numerous candidate plasticity-related genes revealed by differential cDNA cloning. Nature 1993, 363:718-722.
    • (1993) Nature , vol.363 , pp. 718-722
    • Nedivi, E.1    Hevroni, D.2    Naot, D.3    Israeli, D.4    Citri, Y.5
  • 148
    • 84897066284 scopus 로고    scopus 로고
    • Minocycline suppresses experimental autoimmune encephalomyelitis by increasing tissue inhibitors of metalloproteinases
    • Niimi N., Kohyama K., Matsumoto Y. Minocycline suppresses experimental autoimmune encephalomyelitis by increasing tissue inhibitors of metalloproteinases. Neuropathology 2013, 33:612-620.
    • (2013) Neuropathology , vol.33 , pp. 612-620
    • Niimi, N.1    Kohyama, K.2    Matsumoto, Y.3
  • 149
    • 0036096968 scopus 로고    scopus 로고
    • Up-regulation of MMP-8 and MMP-9 activity in the BALB/c mouse spinal cord correlates with the severity of experimental autoimmune encephalomyelitis
    • Nygardas P.T., Hinkkanen A.E. Up-regulation of MMP-8 and MMP-9 activity in the BALB/c mouse spinal cord correlates with the severity of experimental autoimmune encephalomyelitis. Clin. Exp. Immunol. 2002, 128:245-254.
    • (2002) Clin. Exp. Immunol. , vol.128 , pp. 245-254
    • Nygardas, P.T.1    Hinkkanen, A.E.2
  • 150
  • 151
    • 33748139021 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 (MMP-2) regulates astrocyte motility in connection with the actin cytoskeleton and integrins
    • Ogier C., Bernard A., Chollet A.M., Le Diguardher T., Hanessian S., Charton G., Khrestchatisky M., Rivera S. Matrix metalloproteinase-2 (MMP-2) regulates astrocyte motility in connection with the actin cytoskeleton and integrins. Glia 2006, 54:272-284.
    • (2006) Glia , vol.54 , pp. 272-284
    • Ogier, C.1    Bernard, A.2    Chollet, A.M.3    Le Diguardher, T.4    Hanessian, S.5    Charton, G.6    Khrestchatisky, M.7    Rivera, S.8
  • 152
    • 0033215979 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9/gelatinase B is required for process outgrowth by oligodendrocytes
    • Oh L.Y., Larsen P.H., Krekoski C.A., Edwards D.R., Donovan F., Werb Z., Yong V.W. Matrix metalloproteinase-9/gelatinase B is required for process outgrowth by oligodendrocytes. J. Neurosci. 1999, 19:8464-8475.
    • (1999) J. Neurosci. , vol.19 , pp. 8464-8475
    • Oh, L.Y.1    Larsen, P.H.2    Krekoski, C.A.3    Edwards, D.R.4    Donovan, F.5    Werb, Z.6    Yong, V.W.7
  • 153
    • 0033012984 scopus 로고    scopus 로고
    • Amino-terminal region of secreted form of amyloid precursor protein stimulates proliferation of neural stem cells
    • Ohsawa I., Takamura C., Morimoto T., Ishiguro M., Kohsaka S. Amino-terminal region of secreted form of amyloid precursor protein stimulates proliferation of neural stem cells. Eur. J. Neurosci. 1999, 11:1907-1913.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 1907-1913
    • Ohsawa, I.1    Takamura, C.2    Morimoto, T.3    Ishiguro, M.4    Kohsaka, S.5
  • 154
    • 34447528380 scopus 로고    scopus 로고
    • TIMP-1 abolishes MMP-9-dependent long-lasting long-term potentiation in the prefrontal cortex
    • Okulski P., Jay T.M., Jaworski J., Duniec K., Dzwonek J., Konopacki F.A., et al. TIMP-1 abolishes MMP-9-dependent long-lasting long-term potentiation in the prefrontal cortex. Biol. Psychiatry 2007, 62:359-362.
    • (2007) Biol. Psychiatry , vol.62 , pp. 359-362
    • Okulski, P.1    Jay, T.M.2    Jaworski, J.3    Duniec, K.4    Dzwonek, J.5    Konopacki, F.A.6
  • 157
    • 84868573143 scopus 로고    scopus 로고
    • Drug transport across the blood-brain barrier
    • Pardridge W.M. Drug transport across the blood-brain barrier. J. Cereb. Blood Flow Metab. 2012, 32:1959-1972.
    • (2012) J. Cereb. Blood Flow Metab. , vol.32 , pp. 1959-1972
    • Pardridge, W.M.1
  • 159
    • 0031723106 scopus 로고    scopus 로고
    • Matrix metalloproteinases contribute to the blood-brain barrier disruption during bacterial meningitis
    • Paul R., Lorenzl S., Koedel U., Sporer B., Vogel U., Frosch M., Pfister H.W. Matrix metalloproteinases contribute to the blood-brain barrier disruption during bacterial meningitis. Ann. Neurol. 1998, 44:592-600.
    • (1998) Ann. Neurol. , vol.44 , pp. 592-600
    • Paul, R.1    Lorenzl, S.2    Koedel, U.3    Sporer, B.4    Vogel, U.5    Frosch, M.6    Pfister, H.W.7
  • 160
    • 0028895806 scopus 로고
    • Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain
    • Peress N., Perillo E., Zucker S. Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain. J. Neuropathol. Exp. Neurol. 1995, 54:16-22.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 16-22
    • Peress, N.1    Perillo, E.2    Zucker, S.3
  • 161
    • 19044387522 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-2 promotes neuronal differentiation by acting as an anti-mitogenic signal
    • Perez-Martinez L., Jaworski D.M. Tissue inhibitor of metalloproteinase-2 promotes neuronal differentiation by acting as an anti-mitogenic signal. J. Neurosci. 2005, 25:4917-4929.
    • (2005) J. Neurosci. , vol.25 , pp. 4917-4929
    • Perez-Martinez, L.1    Jaworski, D.M.2
  • 162
    • 0034657410 scopus 로고    scopus 로고
    • Endogenous APP derivatives oppositely modulate apoptosis through an autocrine loop
    • Piccini A., Ciotti M.T., Vitolo O.V., Calissano P., Tabaton M., Galli C. Endogenous APP derivatives oppositely modulate apoptosis through an autocrine loop. Neuroreport 2000, 11:1375-1379.
    • (2000) Neuroreport , vol.11 , pp. 1375-1379
    • Piccini, A.1    Ciotti, M.T.2    Vitolo, O.V.3    Calissano, P.4    Tabaton, M.5    Galli, C.6
  • 163
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
    • Postina R., Schroeder A., Dewachter I., Bohl J., Schmitt U., Kojro E., et al. A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J. Clin. Invest. 2004, 113:1456-1464.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1456-1464
    • Postina, R.1    Schroeder, A.2    Dewachter, I.3    Bohl, J.4    Schmitt, U.5    Kojro, E.6
  • 164
    • 0034993141 scopus 로고    scopus 로고
    • In vivo collagenase-2 (MMP-8) expression by human bronchial epithelial cells and monocytes/macrophages in bronchiectasis
    • Prikk K., Maisi P., Pirila E., Sepper R., Salo T., Wahlgren J., Sorsa T. In vivo collagenase-2 (MMP-8) expression by human bronchial epithelial cells and monocytes/macrophages in bronchiectasis. J. Pathol. 2001, 194:232-238.
    • (2001) J. Pathol. , vol.194 , pp. 232-238
    • Prikk, K.1    Maisi, P.2    Pirila, E.3    Sepper, R.4    Salo, T.5    Wahlgren, J.6    Sorsa, T.7
  • 165
    • 84907927401 scopus 로고    scopus 로고
    • Differential spatio-temporal regulation of MMPs in the 5xFAD mouse model of Alzheimer's disease: evidence for a pro-amyloidogenic role of MT1-MMP
    • eCollection 2014
    • Py N.A., Bonnet A.E., Bernard A., Marchalant Y., Charrat E., Checler F., Khrestchatisky M., Baranger K., Rivera S. Differential spatio-temporal regulation of MMPs in the 5xFAD mouse model of Alzheimer's disease: evidence for a pro-amyloidogenic role of MT1-MMP. Front. Aging Neurosci. 2014, eCollection 2014. 10.3389/fnagi.2014.00247.
    • (2014) Front. Aging Neurosci.
    • Py, N.A.1    Bonnet, A.E.2    Bernard, A.3    Marchalant, Y.4    Charrat, E.5    Checler, F.6    Khrestchatisky, M.7    Baranger, K.8    Rivera, S.9
  • 166
    • 14044274265 scopus 로고    scopus 로고
    • Recent developments in the design of specific Matrix Metalloproteinase inhibitors aided by structural and computational studies
    • Rao B.G. Recent developments in the design of specific Matrix Metalloproteinase inhibitors aided by structural and computational studies. Curr. Pharm. Des. 2005, 11:295-322.
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 295-322
    • Rao, B.G.1
  • 168
    • 0030916121 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-1 (TIMP-1) is differentially induced in neurons and astrocytes after seizures: evidence for developmental, immediate early gene, and lesion response
    • Rivera S., Tremblay E., Timsit S., Canals O., Ben-Ari Y., Khrestchatisky M. Tissue inhibitor of metalloproteinases-1 (TIMP-1) is differentially induced in neurons and astrocytes after seizures: evidence for developmental, immediate early gene, and lesion response. J. Neurosci. 1997, 17:4223-4235.
    • (1997) J. Neurosci. , vol.17 , pp. 4223-4235
    • Rivera, S.1    Tremblay, E.2    Timsit, S.3    Canals, O.4    Ben-Ari, Y.5    Khrestchatisky, M.6
  • 169
    • 0036460593 scopus 로고    scopus 로고
    • Gelatinase B and TIMP-1 are regulated in a cell- and time dependent manner in association with neuronal death and glial reactivity after global forebrain ischemia
    • Rivera S., Ogier C., Jourquin J., Timsit S., Szklarczyk A.W., Miller K., Gearing A.J., Kaczmarek L., Khrestchatisky M. Gelatinase B and TIMP-1 are regulated in a cell- and time dependent manner in association with neuronal death and glial reactivity after global forebrain ischemia. Eur. J. Neurosci. 2002, 15:19-32.
    • (2002) Eur. J. Neurosci. , vol.15 , pp. 19-32
    • Rivera, S.1    Ogier, C.2    Jourquin, J.3    Timsit, S.4    Szklarczyk, A.W.5    Miller, K.6    Gearing, A.J.7    Kaczmarek, L.8    Khrestchatisky, M.9
  • 170
    • 78449239604 scopus 로고    scopus 로고
    • Metzincin proteases and their inhibitors, foes or friends in nervous system physiology?
    • Rivera S., Khrestchatisky M., Kaczmarek L., Rosenberg G.A., Jaworski D.M. Metzincin proteases and their inhibitors, foes or friends in nervous system physiology?. J. Neurosci. 2010, 30:15337-15357.
    • (2010) J. Neurosci. , vol.30 , pp. 15337-15357
    • Rivera, S.1    Khrestchatisky, M.2    Kaczmarek, L.3    Rosenberg, G.A.4    Jaworski, D.M.5
  • 171
    • 84902536769 scopus 로고    scopus 로고
    • Predictive value of cerebrospinal fluid matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 concentrations in childhood bacterial meningitis
    • Roine I., Pelkonen T., Bernardino L., Lauhio A., Tervahartiala T., Lappalainen M., et al. Predictive value of cerebrospinal fluid matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 concentrations in childhood bacterial meningitis. Pediatr. Infect. Dis. J. 2014, 33:675-679.
    • (2014) Pediatr. Infect. Dis. J. , vol.33 , pp. 675-679
    • Roine, I.1    Pelkonen, T.2    Bernardino, L.3    Lauhio, A.4    Tervahartiala, T.5    Lappalainen, M.6
  • 172
    • 0036737795 scopus 로고    scopus 로고
    • Matrix metalloproteinases in neuroinflammation
    • Rosenberg G.A. Matrix metalloproteinases in neuroinflammation. Glia 2002, 39:279-291.
    • (2002) Glia , vol.39 , pp. 279-291
    • Rosenberg, G.A.1
  • 173
    • 58249126857 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their multiple roles in neurodegenerative diseases
    • Rosenberg G.A. Matrix metalloproteinases and their multiple roles in neurodegenerative diseases. Lancet Neurol. 2009, 8:205-216.
    • (2009) Lancet Neurol. , vol.8 , pp. 205-216
    • Rosenberg, G.A.1
  • 174
    • 0025314978 scopus 로고
    • Collagenase-induced intracerebral hemorrhage in rats
    • Rosenberg G.A., Mun-Bryce S., Wesley M., Kornfeld M. Collagenase-induced intracerebral hemorrhage in rats. Stroke 1990, 21:801-807.
    • (1990) Stroke , vol.21 , pp. 801-807
    • Rosenberg, G.A.1    Mun-Bryce, S.2    Wesley, M.3    Kornfeld, M.4
  • 176
    • 0028973084 scopus 로고
    • Tumor necrosis factor-alpha-induced gelatinase B causes delayed opening of the blood-brain barrier: an expanded therapeutic window
    • Rosenberg G.A., Estrada E.Y., Dencoff J.E., Stetler-Stevenson W.G. Tumor necrosis factor-alpha-induced gelatinase B causes delayed opening of the blood-brain barrier: an expanded therapeutic window. Brain Res. 1995, 703:151-155.
    • (1995) Brain Res. , vol.703 , pp. 151-155
    • Rosenberg, G.A.1    Estrada, E.Y.2    Dencoff, J.E.3    Stetler-Stevenson, W.G.4
  • 177
    • 0031693557 scopus 로고    scopus 로고
    • Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain
    • Rosenberg G.A., Estrada E.Y., Dencoff J.E. Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain. Stroke 1998, 29:2189-2195.
    • (1998) Stroke , vol.29 , pp. 2189-2195
    • Rosenberg, G.A.1    Estrada, E.Y.2    Dencoff, J.E.3
  • 180
    • 77954054834 scopus 로고    scopus 로고
    • Neisseria meningitidis induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: a role for MMP-8
    • Schubert-Unkmeir A., Konrad C., Slanina H., Czapek F., Hebling S., Frosch M. Neisseria meningitidis induces brain microvascular endothelial cell detachment from the matrix and cleavage of occludin: a role for MMP-8. PLoS Pathog. 2010, 6:e1000874.
    • (2010) PLoS Pathog. , vol.6 , pp. e1000874
    • Schubert-Unkmeir, A.1    Konrad, C.2    Slanina, H.3    Czapek, F.4    Hebling, S.5    Frosch, M.6
  • 181
    • 33244490286 scopus 로고    scopus 로고
    • In bacterial meningitis cortical brain damage is associated with changes in parenchymal MMP-9/TIMP-1 ratio and increased collagen type IV degradation
    • Sellner J., Leib S.L. In bacterial meningitis cortical brain damage is associated with changes in parenchymal MMP-9/TIMP-1 ratio and increased collagen type IV degradation. Neurobiol. Dis. 2006, 21:647-656.
    • (2006) Neurobiol. Dis. , vol.21 , pp. 647-656
    • Sellner, J.1    Leib, S.L.2
  • 182
    • 33751504327 scopus 로고    scopus 로고
    • Herpes-simplex virus encephalitis is characterized by an early MMP-9 increase and collagen type IV degradation
    • Sellner J., Simon F., Meyding-Lamade U., Leib S.L. Herpes-simplex virus encephalitis is characterized by an early MMP-9 increase and collagen type IV degradation. Brain Res. 2006, 1125:155-162.
    • (2006) Brain Res. , vol.1125 , pp. 155-162
    • Sellner, J.1    Simon, F.2    Meyding-Lamade, U.3    Leib, S.L.4
  • 183
    • 80051685667 scopus 로고    scopus 로고
    • Cell cholesterol modulates metalloproteinase-dependent shedding of low-density lipoprotein receptor-related protein-1 (LRP-1) and clearance function
    • Selvais C., D'auria L., Tyteca D., Perrot G., Lemoine P., Troeberg L., et al. Cell cholesterol modulates metalloproteinase-dependent shedding of low-density lipoprotein receptor-related protein-1 (LRP-1) and clearance function. FASEB J. 2011, 25:2770-2781.
    • (2011) FASEB J. , vol.25 , pp. 2770-2781
    • Selvais, C.1    D'auria, L.2    Tyteca, D.3    Perrot, G.4    Lemoine, P.5    Troeberg, L.6
  • 184
    • 0037437674 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases, sICAM-1 and IL-8 in CSF from children with meningitis
    • Shapiro S., Miller A., Lahat N., Sobel E., Lerner A. Expression of matrix metalloproteinases, sICAM-1 and IL-8 in CSF from children with meningitis. J. Neurol. Sci. 2003, 206:43-48.
    • (2003) J. Neurol. Sci. , vol.206 , pp. 43-48
    • Shapiro, S.1    Miller, A.2    Lahat, N.3    Sobel, E.4    Lerner, A.5
  • 185
    • 64049085808 scopus 로고    scopus 로고
    • Matrix metalloproteinase proteolysis of the myelin basic protein isoforms is a source of immunogenic peptides in autoimmune multiple sclerosis
    • Shiryaev S.A., Savinov A.Y., Cieplak P., Ratnikov B.I., Motamedchaboki K., Smith J.W., Strongin A.Y. Matrix metalloproteinase proteolysis of the myelin basic protein isoforms is a source of immunogenic peptides in autoimmune multiple sclerosis. PLoS One 2009, 4:e4952.
    • (2009) PLoS One , vol.4 , pp. e4952
    • Shiryaev, S.A.1    Savinov, A.Y.2    Cieplak, P.3    Ratnikov, B.I.4    Motamedchaboki, K.5    Smith, J.W.6    Strongin, A.Y.7
  • 186
    • 0022622973 scopus 로고
    • Influence of body temperature on bacterial growth rates in experimental pneumococcal meningitis in rabbits
    • Small P.M., Tauber M.G., Hackbarth C.J., Sande M.A. Influence of body temperature on bacterial growth rates in experimental pneumococcal meningitis in rabbits. Infect. Immun. 1986, 52:484-487.
    • (1986) Infect. Immun. , vol.52 , pp. 484-487
    • Small, P.M.1    Tauber, M.G.2    Hackbarth, C.J.3    Sande, M.A.4
  • 187
    • 84883256038 scopus 로고    scopus 로고
    • Water-soluble MMP-9 inhibitor prodrug generates active metabolites that cross the blood-brain barrier
    • Song W., Peng Z., Gooyit M., Suckow M.A., Schroeder V.A., Wolter W.R., et al. Water-soluble MMP-9 inhibitor prodrug generates active metabolites that cross the blood-brain barrier. ACS Chem. Neurosci. 2013, 4:1168-1173.
    • (2013) ACS Chem. Neurosci. , vol.4 , pp. 1168-1173
    • Song, W.1    Peng, Z.2    Gooyit, M.3    Suckow, M.A.4    Schroeder, V.A.5    Wolter, W.R.6
  • 188
    • 0031656032 scopus 로고    scopus 로고
    • Presence of matrix metalloproteinase-9 activity in the cerebrospinal fluid of human immunodeficiency virus-infected patients
    • Sporer B., Paul R., Koedel U., Grimm R., Wick M., Goebel F.D., Pfister H.W. Presence of matrix metalloproteinase-9 activity in the cerebrospinal fluid of human immunodeficiency virus-infected patients. J. Infect. Dis. 1998, 178:854-857.
    • (1998) J. Infect. Dis. , vol.178 , pp. 854-857
    • Sporer, B.1    Paul, R.2    Koedel, U.3    Grimm, R.4    Wick, M.5    Goebel, F.D.6    Pfister, H.W.7
  • 189
    • 40349115902 scopus 로고    scopus 로고
    • Interplay between mechanisms of damage and repair in multiple sclerosis
    • Stadelmann C., Bruck W. Interplay between mechanisms of damage and repair in multiple sclerosis. J. Neurol. 2008, 255(Suppl. 1):12-18.
    • (2008) J. Neurol. , vol.255 , pp. 12-18
    • Stadelmann, C.1    Bruck, W.2
  • 190
    • 0028675733 scopus 로고
    • Progelatinase A activation during tumor cell invasion
    • Stetler-Stevenson W.G. Progelatinase A activation during tumor cell invasion. Invasion Metastasis 1994, 14:259-268.
    • (1994) Invasion Metastasis , vol.14 , pp. 259-268
    • Stetler-Stevenson, W.G.1
  • 191
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin A.Y., Collier I., Bannikov G., Marmer B.L., Grant G.A., Goldberg G.I. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 1995, 270:5331-5338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 192
    • 60549114340 scopus 로고    scopus 로고
    • Immunohistochemical analysis of MMP-9, MMP-2 and TIMP-1, TIMP-2 expression in the central nervous system following infection with viral and bacterial meningitis
    • Sulik A., Chyczewski L. Immunohistochemical analysis of MMP-9, MMP-2 and TIMP-1, TIMP-2 expression in the central nervous system following infection with viral and bacterial meningitis. Folia Histochem. Cytobiol. 2008, 46:437-442.
    • (2008) Folia Histochem. Cytobiol. , vol.46 , pp. 437-442
    • Sulik, A.1    Chyczewski, L.2
  • 193
    • 48749099979 scopus 로고    scopus 로고
    • Elevated levels of MMP-9 and TIMP-1 in the cerebrospinal fluid of children with echovirus type 30 and mumps meningitis
    • Sulik A., Wojtkowska M., Oldak E. Elevated levels of MMP-9 and TIMP-1 in the cerebrospinal fluid of children with echovirus type 30 and mumps meningitis. Scand. J. Immunol. 2008, 68:323-327.
    • (2008) Scand. J. Immunol. , vol.68 , pp. 323-327
    • Sulik, A.1    Wojtkowska, M.2    Oldak, E.3
  • 194
    • 0036470147 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus
    • Szklarczyk A., Lapinska J., Rylski M., Mckay R.D., Kaczmarek L. Matrix metalloproteinase-9 undergoes expression and activation during dendritic remodeling in adult hippocampus. J. Neurosci. 2002, 22:920-930.
    • (2002) J. Neurosci. , vol.22 , pp. 920-930
    • Szklarczyk, A.1    Lapinska, J.2    Rylski, M.3    Mckay, R.D.4    Kaczmarek, L.5
  • 196
    • 60649086817 scopus 로고    scopus 로고
    • RECK negatively regulates matrix metalloproteinase-9 transcription
    • Takagi S., Simizu S., Osada H. RECK negatively regulates matrix metalloproteinase-9 transcription. Cancer Res. 2009, 69:1502-1508.
    • (2009) Cancer Res. , vol.69 , pp. 1502-1508
    • Takagi, S.1    Simizu, S.2    Osada, H.3
  • 197
    • 36249015501 scopus 로고    scopus 로고
    • Abeta(1-40)-induced secretion of matrix metalloproteinase-9 results in sAPPalpha release by association with cell surface APP
    • Talamagas A.A., Efthimiopoulos S., Tsilibary E.C., Figueiredo-Pereira M.E., Tzinia A.K. Abeta(1-40)-induced secretion of matrix metalloproteinase-9 results in sAPPalpha release by association with cell surface APP. Neurobiol. Dis. 2007, 28:304-315.
    • (2007) Neurobiol. Dis. , vol.28 , pp. 304-315
    • Talamagas, A.A.1    Efthimiopoulos, S.2    Tsilibary, E.C.3    Figueiredo-Pereira, M.E.4    Tzinia, A.K.5
  • 199
    • 67149115144 scopus 로고    scopus 로고
    • DFT studies of the ring-opening mechanism of SB-3CT, a potent inhibitor of matrix metalloproteinase 2
    • Tao P., Fisher J.F., Mobashery S., Schlegel H.B. DFT studies of the ring-opening mechanism of SB-3CT, a potent inhibitor of matrix metalloproteinase 2. Org. Lett. 2009, 11:2559-2562.
    • (2009) Org. Lett. , vol.11 , pp. 2559-2562
    • Tao, P.1    Fisher, J.F.2    Mobashery, S.3    Schlegel, H.B.4
  • 203
    • 67349181321 scopus 로고    scopus 로고
    • Lack of TIMP-1 increases severity of experimental autoimmune encephalomyelitis: effects of darbepoetin alfa on TIMP-1 null and wild-type mice
    • Thorne M., Moore C.S., Robertson G.S. Lack of TIMP-1 increases severity of experimental autoimmune encephalomyelitis: effects of darbepoetin alfa on TIMP-1 null and wild-type mice. J. Neuroimmunol. 2009, 211:92-100.
    • (2009) J. Neuroimmunol. , vol.211 , pp. 92-100
    • Thorne, M.1    Moore, C.S.2    Robertson, G.S.3
  • 204
    • 6344252618 scopus 로고    scopus 로고
    • Key metalloproteinases are expressed by specific cell types in experimental autoimmune encephalomyelitis
    • Toft-Hansen H., Nuttall R.K., Edwards D.R., Owens T. Key metalloproteinases are expressed by specific cell types in experimental autoimmune encephalomyelitis. J. Immunol. 2004, 173:5209-5218.
    • (2004) J. Immunol. , vol.173 , pp. 5209-5218
    • Toft-Hansen, H.1    Nuttall, R.K.2    Edwards, D.R.3    Owens, T.4
  • 206
    • 0029849195 scopus 로고    scopus 로고
    • Roles of proinflammatory and anti-inflammatory cytokines in pathophysiology of bacterial meningitis and effect of adjunctive therapy
    • Van Furth A.M., Roord J.J., Van Furth R. Roles of proinflammatory and anti-inflammatory cytokines in pathophysiology of bacterial meningitis and effect of adjunctive therapy. Infect. Immun. 1996, 64:4883-4890.
    • (1996) Infect. Immun. , vol.64 , pp. 4883-4890
    • Van Furth, A.M.1    Roord, J.J.2    Van Furth, R.3
  • 208
    • 79954484426 scopus 로고    scopus 로고
    • Peptide-based vectors for blood-brain barrier targeting and delivery of drugs to the central nervous system
    • Vlieghe P., Khrestchatisky M. Peptide-based vectors for blood-brain barrier targeting and delivery of drugs to the central nervous system. Ther. Deliv. 2010, 1:489-494.
    • (2010) Ther. Deliv. , vol.1 , pp. 489-494
    • Vlieghe, P.1    Khrestchatisky, M.2
  • 209
    • 84876083067 scopus 로고    scopus 로고
    • Medicinal chemistry based approaches and nanotechnology-based systems to improve CNS drug targeting and delivery
    • Vlieghe P., Khrestchatisky M. Medicinal chemistry based approaches and nanotechnology-based systems to improve CNS drug targeting and delivery. Med. Res. Rev. 2013, 33:457-516.
    • (2013) Med. Res. Rev. , vol.33 , pp. 457-516
    • Vlieghe, P.1    Khrestchatisky, M.2
  • 210
    • 59749083104 scopus 로고    scopus 로고
    • TIMP-3 and MMP-3 contribute to delayed inflammation and hippocampal neuronal death following global ischemia
    • Walker E.J., Rosenberg G.A. TIMP-3 and MMP-3 contribute to delayed inflammation and hippocampal neuronal death following global ischemia. Exp. Neurol. 2009, 216:122-131.
    • (2009) Exp. Neurol. , vol.216 , pp. 122-131
    • Walker, E.J.1    Rosenberg, G.A.2
  • 211
    • 0032693982 scopus 로고    scopus 로고
    • Serum MMP-9 and TIMP-1 levels are related to MRI activity in relapsing multiple sclerosis
    • Waubant E., Goodkin D.E., Gee L., Bacchetti P., Sloan R., Stewart T., et al. Serum MMP-9 and TIMP-1 levels are related to MRI activity in relapsing multiple sclerosis. Neurology 1999, 53:1397-1401.
    • (1999) Neurology , vol.53 , pp. 1397-1401
    • Waubant, E.1    Goodkin, D.E.2    Gee, L.3    Bacchetti, P.4    Sloan, R.5    Stewart, T.6
  • 212
    • 0034742686 scopus 로고    scopus 로고
    • IFN-beta1a may increase serum levels of TIMP-1 in patients with relapsing-remitting multiple sclerosis
    • Waubant E., Gee L., Miller K., Stabler G., Goodkin D. IFN-beta1a may increase serum levels of TIMP-1 in patients with relapsing-remitting multiple sclerosis. J. Interferon Cytokine Res. 2001, 21:181-185.
    • (2001) J. Interferon Cytokine Res. , vol.21 , pp. 181-185
    • Waubant, E.1    Gee, L.2    Miller, K.3    Stabler, G.4    Goodkin, D.5
  • 213
    • 26444447974 scopus 로고    scopus 로고
    • An elevated matrix metalloproteinase (MMP) in an animal model of multiple sclerosis is protective by affecting Th1/Th2 polarization
    • Weaver A., Goncalves Da Silva A., Nuttall R.K., Edwards D.R., Shapiro S.D., Rivest S., Yong V.W. An elevated matrix metalloproteinase (MMP) in an animal model of multiple sclerosis is protective by affecting Th1/Th2 polarization. FASEB J. 2005, 19:1668-1670.
    • (2005) FASEB J. , vol.19 , pp. 1668-1670
    • Weaver, A.1    Goncalves Da Silva, A.2    Nuttall, R.K.3    Edwards, D.R.4    Shapiro, S.D.5    Rivest, S.6    Yong, V.W.7
  • 214
    • 0141502228 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-3 and matrix metalloproteinase-3 regulate neuronal sensitivity to doxorubicin-induced apoptosis
    • Wetzel M., Rosenberg G.A., Cunningham L.A. Tissue inhibitor of metalloproteinases-3 and matrix metalloproteinase-3 regulate neuronal sensitivity to doxorubicin-induced apoptosis. Eur. J. Neurosci. 2003, 18:1050-1060.
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 1050-1060
    • Wetzel, M.1    Rosenberg, G.A.2    Cunningham, L.A.3
  • 217
    • 33747680357 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 degrades amyloid-beta fibrils in vitro and compact plaques in situ
    • Yan P., Hu X., Song H., Yin K., Bateman R.J., Cirrito J.R., et al. Matrix metalloproteinase-9 degrades amyloid-beta fibrils in vitro and compact plaques in situ. J. Biol. Chem. 2006, 281:24566-24574.
    • (2006) J. Biol. Chem. , vol.281 , pp. 24566-24574
    • Yan, P.1    Hu, X.2    Song, H.3    Yin, K.4    Bateman, R.J.5    Cirrito, J.R.6
  • 218
    • 33751112725 scopus 로고    scopus 로고
    • Matrix metalloproteinases expressed by astrocytes mediate extracellular amyloid-beta peptide catabolism
    • Yin K.-J., Cirrito J.R., Yan P., Hu X., Xiao Q., Pan X., et al. Matrix metalloproteinases expressed by astrocytes mediate extracellular amyloid-beta peptide catabolism. J. Neurosci. 2006, 26:10939-10948.
    • (2006) J. Neurosci. , vol.26 , pp. 10939-10948
    • Yin, K.-J.1    Cirrito, J.R.2    Yan, P.3    Hu, X.4    Xiao, Q.5    Pan, X.6
  • 220
    • 34249809137 scopus 로고    scopus 로고
    • Experimental models of neuroprotection relevant to multiple sclerosis
    • discussion S43-S54
    • Yong V.W., Giuliani F., Xue M., Bar-Or A., Metz L.M. Experimental models of neuroprotection relevant to multiple sclerosis. Neurology 2007, 68:S32-S37. discussion S43-S54.
    • (2007) Neurology , vol.68 , pp. S32-S37
    • Yong, V.W.1    Giuliani, F.2    Xue, M.3    Bar-Or, A.4    Metz, L.M.5
  • 221
    • 0034597152 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) in human cerebrospinal fluid (CSF): elevated levels are primarily related to CSF cell count
    • Yushchenko M., Weber F., Mader M., Scholl U., Maliszewska M., Tumani H., et al. Matrix metalloproteinase-9 (MMP-9) in human cerebrospinal fluid (CSF): elevated levels are primarily related to CSF cell count. J. Neuroimmunol. 2000, 110:244-251.
    • (2000) J. Neuroimmunol. , vol.110 , pp. 244-251
    • Yushchenko, M.1    Weber, F.2    Mader, M.3    Scholl, U.4    Maliszewska, M.5    Tumani, H.6
  • 222
    • 0034577933 scopus 로고    scopus 로고
    • Regional and age-related expression of gelatinases in the brains of young and old rats after treatment with kainic acid
    • Zhang J.W., Deb S., Gottschall P.E. Regional and age-related expression of gelatinases in the brains of young and old rats after treatment with kainic acid. Neurosci. Lett. 2000, 295:9-12.
    • (2000) Neurosci. Lett. , vol.295 , pp. 9-12
    • Zhang, J.W.1    Deb, S.2    Gottschall, P.E.3
  • 223
    • 63849319352 scopus 로고    scopus 로고
    • Macrophage-mediated degradation of beta-amyloid via an apolipoprotein E isoform-dependent mechanism
    • Zhao L., Lin S., Bales K.R., Gelfanova V., Koger D., Delong C., et al. Macrophage-mediated degradation of beta-amyloid via an apolipoprotein E isoform-dependent mechanism. J. Neurosci. 2009, 29:3603-3612.
    • (2009) J. Neurosci. , vol.29 , pp. 3603-3612
    • Zhao, L.1    Lin, S.2    Bales, K.R.3    Gelfanova, V.4    Koger, D.5    Delong, C.6
  • 224
    • 0036314877 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression correlates with virulence following neurotropic mouse hepatitis virus infection
    • Zhou J., Stohlman S.A., Atkinson R., Hinton D.R., Marten N.W. Matrix metalloproteinase expression correlates with virulence following neurotropic mouse hepatitis virus infection. J. Virol. 2002, 76:7374-7384.
    • (2002) J. Virol. , vol.76 , pp. 7374-7384
    • Zhou, J.1    Stohlman, S.A.2    Atkinson, R.3    Hinton, D.R.4    Marten, N.W.5
  • 225
    • 16244409276 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and their tissue inhibitor during viral encephalitis
    • Zhou J., Marten N.W., Bergmann C.C., Macklin W.B., Hinton D.R., Stohlman S.A. Expression of matrix metalloproteinases and their tissue inhibitor during viral encephalitis. J. Virol. 2005, 79:4764-4773.
    • (2005) J. Virol. , vol.79 , pp. 4764-4773
    • Zhou, J.1    Marten, N.W.2    Bergmann, C.C.3    Macklin, W.B.4    Hinton, D.R.5    Stohlman, S.A.6
  • 226
    • 0032527889 scopus 로고    scopus 로고
    • Neuronal matrix metalloproteinase-2 degrades and inactivates a neurite-inhibiting chondroitin sulfate proteoglycan
    • Zuo J., Ferguson T.A., Hernandez Y.J., Stetler-Stevenson W.G., Muir D. Neuronal matrix metalloproteinase-2 degrades and inactivates a neurite-inhibiting chondroitin sulfate proteoglycan. J. Neurosci. 1998, 18:5203-5211.
    • (1998) J. Neurosci. , vol.18 , pp. 5203-5211
    • Zuo, J.1    Ferguson, T.A.2    Hernandez, Y.J.3    Stetler-Stevenson, W.G.4    Muir, D.5
  • 227
    • 0020084070 scopus 로고
    • Complement-mediated opsonic activity in normal and infected human cerebrospinal fluid: early response during bacterial meningitis
    • Zwahlen A., Nydegger U.E., Vaudaux P., Lambert P.H., Waldvogel F.A. Complement-mediated opsonic activity in normal and infected human cerebrospinal fluid: early response during bacterial meningitis. J. Infect. Dis. 1982, 145:635-646.
    • (1982) J. Infect. Dis. , vol.145 , pp. 635-646
    • Zwahlen, A.1    Nydegger, U.E.2    Vaudaux, P.3    Lambert, P.H.4    Waldvogel, F.A.5


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