메뉴 건너뛰기




Volumn 38, Issue 6, 2013, Pages 1113-1121

Proteolytic remodeling of the synaptic cell adhesion molecules (CAMs) by metzincins in synaptic plasticity

Author keywords

Cadherin; Dendritic spines; MMP; Proteolysis; Synapse; SynCAM

Indexed keywords

ADAM10 ENDOPEPTIDASE; BETA DYSTROGLYCAN; CADHERIN; CELL PROTEIN; GAMMA SECRETASE; GELATINASE A; GELATINASE B; INTERCELLULAR ADHESION MOLECULE 5; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; METZINCIN; MITOGEN ACTIVATED PROTEIN KINASE; NECTIN 2; NERVE CELL ADHESION MOLECULE; NERVE CELL ADHESION MOLECULE L1; NEUREXIN; PHOSPHATIDYLINOSITOL 3 KINASE; PRESENILIN 1; PROTEIN KINASE C; SYNDECAN; THROMBOSPONDIN; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; UNCLASSIFIED DRUG;

EID: 84878017554     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-012-0919-6     Document Type: Review
Times cited : (25)

References (79)
  • 1
    • 84859730415 scopus 로고    scopus 로고
    • Building and remodeling synapses
    • 20882551 10.1002/hipo.20872
    • Benson DL, Huntley GW (2012) Building and remodeling synapses. Hippocampus 22(5):954-968
    • (2012) Hippocampus , vol.22 , Issue.5 , pp. 954-968
    • Benson, D.L.1    Huntley, G.W.2
  • 2
    • 78449239604 scopus 로고    scopus 로고
    • Metzincin proteases and their inhibitors: Foes or friends in nervous system physiology?
    • 21084591 10.1523/JNEUROSCI.3467-10.2010 1:CAS:528:DC%2BC3cXhsFWitbzN
    • Rivera S, Khrestchatisky M, Kaczmarek L, Rosenberg GA, Jaworski DM (2010) Metzincin proteases and their inhibitors: foes or friends in nervous system physiology? J Neurosci 30(46):15337-15357
    • (2010) J Neurosci , vol.30 , Issue.46 , pp. 15337-15357
    • Rivera, S.1    Khrestchatisky, M.2    Kaczmarek, L.3    Rosenberg, G.A.4    Jaworski, D.M.5
  • 3
    • 77954526026 scopus 로고    scopus 로고
    • Remodeling of extracellular matrix and epileptogenesis
    • 20618403 10.1111/j.1528-1167.2010.02612.x 1:CAS:528:DC%2BC3cXhtVegs7fP
    • Dityatev A (2010) Remodeling of extracellular matrix and epileptogenesis. Epilepsia 51(Suppl 3):61-65
    • (2010) Epilepsia , vol.51 , Issue.SUPPL. 3 , pp. 61-65
    • Dityatev, A.1
  • 4
    • 2542436756 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain
    • 15165905 10.1016/j.febslet.2004.03.070 1:CAS:528:DC%2BD2cXksVGhtL8%3D
    • Dzwonek J, Rylski M, Kaczmarek L (2004) Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain. FEBS Lett 567(1):129-135
    • (2004) FEBS Lett , vol.567 , Issue.1 , pp. 129-135
    • Dzwonek, J.1    Rylski, M.2    Kaczmarek, L.3
  • 5
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • 10.1038/nrm2125 1:CAS:528:DC%2BD2sXitVGrs74%3D
    • Page-McCaw A, Ewald AJ, Werb Z (2007) Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev 8(3):221-233
    • (2007) Nat Rev , vol.8 , Issue.3 , pp. 221-233
    • Page-Mccaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 6
    • 0033636556 scopus 로고    scopus 로고
    • Increasing numbers of synaptic puncta during late-phase LTP: N-cadherin is synthesized, recruited to synaptic sites, and required for potentiation
    • 11086998 10.1016/S0896-6273(00)00100-8 1:CAS:528:DC%2BD3cXnvVGltLY%3D
    • Bozdagi O, Shan W, Tanaka H, Benson DL, Huntley GW (2000) Increasing numbers of synaptic puncta during late-phase LTP: N-cadherin is synthesized, recruited to synaptic sites, and required for potentiation. Neuron 28(1):245-259
    • (2000) Neuron , vol.28 , Issue.1 , pp. 245-259
    • Bozdagi, O.1    Shan, W.2    Tanaka, H.3    Benson, D.L.4    Huntley, G.W.5
  • 7
    • 78649747630 scopus 로고    scopus 로고
    • Synaptic localization and activity of ADAM10 regulate excitatory synapses through N-cadherin cleavage
    • 21123580 10.1523/JNEUROSCI.1984-10.2010 1:CAS:528:DC%2BC3cXhs1SlurnI
    • Malinverno M, Carta M, Epis R, Marcello E, Verpelli C, Cattabeni F, Sala C, Mulle C, Di Luca M, Gardoni F (2010) Synaptic localization and activity of ADAM10 regulate excitatory synapses through N-cadherin cleavage. J Neurosci 30(48):16343-16355
    • (2010) J Neurosci , vol.30 , Issue.48 , pp. 16343-16355
    • Malinverno, M.1    Carta, M.2    Epis, R.3    Marcello, E.4    Verpelli, C.5    Cattabeni, F.6    Sala, C.7    Mulle, C.8    Di Luca, M.9    Gardoni, F.10
  • 8
    • 15444371289 scopus 로고    scopus 로고
    • ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling
    • 15692570 10.1038/sj.emboj.7600548 1:CAS:528:DC%2BD2MXhsFWlsbo%3D
    • Reiss K, Maretzky T, Ludwig A, Tousseyn T, de Strooper B, Hartmann D, Saftig P (2005) ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-catenin nuclear signalling. EMBO J 24(4):742-752
    • (2005) EMBO J , vol.24 , Issue.4 , pp. 742-752
    • Reiss, K.1    Maretzky, T.2    Ludwig, A.3    Tousseyn, T.4    De Strooper, B.5    Hartmann, D.6    Saftig, P.7
  • 11
    • 0037118248 scopus 로고    scopus 로고
    • A RIP tide in neuronal signal transduction
    • 12062033 10.1016/S0896-6273(02)00704-3 1:CAS:528:DC%2BD38XktFSmurg%3D
    • Ebinu JO, Yankner BA (2002) A RIP tide in neuronal signal transduction. Neuron 34(4):499-502
    • (2002) Neuron , vol.34 , Issue.4 , pp. 499-502
    • Ebinu, J.O.1    Yankner, B.A.2
  • 12
    • 84861218961 scopus 로고    scopus 로고
    • The neuropeptide PACAP38 induces dendritic spine remodeling through ADAM10-N-cadherin signaling pathway
    • 10.1242/jcs.097576
    • Gardoni F, Saraceno C, Malinverno M, Marcello E, Verpelli C, Sala C, Di Luca M (2011) The neuropeptide PACAP38 induces dendritic spine remodeling through ADAM10-N-cadherin signaling pathway. J Cell Sci 125(6):1401-1406
    • (2011) J Cell Sci , vol.125 , Issue.6 , pp. 1401-1406
    • Gardoni, F.1    Saraceno, C.2    Malinverno, M.3    Marcello, E.4    Verpelli, C.5    Sala, C.6    Di Luca, M.7
  • 13
    • 0031014623 scopus 로고    scopus 로고
    • Differential alteration of hippocampal synaptic strength induced by pituitary adenylate cyclase activating polypeptide-38 (PACAP-38)
    • 9121696 10.1016/S0304-3940(96)13323-1 1:CAS:528:DyaK2sXns1egsA%3D%3D
    • Kondo T, Tominaga T, Ichikawa M, Iijima T (1997) Differential alteration of hippocampal synaptic strength induced by pituitary adenylate cyclase activating polypeptide-38 (PACAP-38). Neurosci Lett 221(2-3):189-192
    • (1997) Neurosci Lett , vol.221 , Issue.2-3 , pp. 189-192
    • Kondo, T.1    Tominaga, T.2    Ichikawa, M.3    Iijima, T.4
  • 14
    • 0034798901 scopus 로고    scopus 로고
    • Differential effects of PACAP-38 on synaptic responses in rat hippocampal CA1 region
    • Roberto M, Scuri R, Brunelli M (2001) Differential effects of PACAP-38 on synaptic responses in rat hippocampal CA1 region. Learning & memory (Cold Spring Harbor, NY) 8 (5):265-271
    • (2001) Learning & Memory (Cold Spring Harbor, NY) , vol.8 , Issue.5 , pp. 265-271
    • Roberto, M.1    Scuri, R.2    Brunelli, M.3
  • 15
    • 58149295113 scopus 로고    scopus 로고
    • Epac mediates PACAP-dependent long-term depression in the hippocampus
    • 19001039 10.1113/jphysiol.2008.157461 1:CAS:528:DC%2BD1MXhtVKls7k%3D
    • Ster J, de Bock F, Bertaso F, Abitbol K, Daniel H, Bockaert J, Fagni L (2009) Epac mediates PACAP-dependent long-term depression in the hippocampus. J Physiol 587(1):101-113
    • (2009) J Physiol , vol.587 , Issue.1 , pp. 101-113
    • Ster, J.1    De Bock, F.2    Bertaso, F.3    Abitbol, K.4    Daniel, H.5    Bockaert, J.6    Fagni, L.7
  • 16
    • 78349305629 scopus 로고    scopus 로고
    • The involvement of PACAP/VIP system in the synaptic transmission in the hippocampus
    • 20414742 10.1007/s12031-010-9372-7 1:CAS:528:DC%2BC3cXht1yktb3J
    • Yang K, Lei G, Jackson MF, Macdonald JF (2010) The involvement of PACAP/VIP system in the synaptic transmission in the hippocampus. J Mol Neurosci 42(3):319-326
    • (2010) J Mol Neurosci , vol.42 , Issue.3 , pp. 319-326
    • Yang, K.1    Lei, G.2    Jackson, M.F.3    Macdonald, J.F.4
  • 17
    • 33645799439 scopus 로고    scopus 로고
    • The neuropeptide PACAP promotes the alpha-secretase pathway for processing the Alzheimer amyloid precursor protein
    • 16401644 1:CAS:528:DC%2BD28Xis1yntrY%3D
    • Kojro E, Postina R, Buro C, Meiringer C, Gehrig-Burger K, Fahrenholz F (2006) The neuropeptide PACAP promotes the alpha-secretase pathway for processing the Alzheimer amyloid precursor protein. Faseb J 20(3):512-514
    • (2006) Faseb J , vol.20 , Issue.3 , pp. 512-514
    • Kojro, E.1    Postina, R.2    Buro, C.3    Meiringer, C.4    Gehrig-Burger, K.5    Fahrenholz, F.6
  • 18
    • 84863808027 scopus 로고    scopus 로고
    • MT5-MMP, ADAM-10, and N-Cadherin Act in concert to facilitate synapse reorganization after traumatic brain injury
    • 22489706 10.1089/neu.2012.2383
    • Warren KM, Reeves TM, Phillips LL (2012) MT5-MMP, ADAM-10, and N-Cadherin Act in concert to facilitate synapse reorganization after traumatic brain injury. J Neurotrauma 29(10):1922-1940
    • (2012) J Neurotrauma , vol.29 , Issue.10 , pp. 1922-1940
    • Warren, K.M.1    Reeves, T.M.2    Phillips, L.L.3
  • 19
    • 50849102322 scopus 로고    scopus 로고
    • Effects of N-cadherin disruption on spine morphological dynamics
    • doi: 10.3389/neuro.03.001.2007
    • Mysore SP, Tai CY, Schuman EM (2007) Effects of N-cadherin disruption on spine morphological dynamics. Frontiers Cell Neurosci 1(1). doi: 10.3389/neuro.03.001.2007
    • (2007) Frontiers Cell Neurosci , vol.1 , Issue.1
    • Mysore, S.P.1    Tai, C.Y.2    Schuman, E.M.3
  • 20
    • 0032103412 scopus 로고    scopus 로고
    • A role for the cadherin family of cell adhesion molecules in hippocampal long-term potentiation
    • 9655504 10.1016/S0896-6273(00)80497-3 1:CAS:528:DyaK1cXktFOksbg%3D
    • Tang L, Hung CP, Schuman EM (1998) A role for the cadherin family of cell adhesion molecules in hippocampal long-term potentiation. Neuron 20(6):1165-1175
    • (1998) Neuron , vol.20 , Issue.6 , pp. 1165-1175
    • Tang, L.1    Hung, C.P.2    Schuman, E.M.3
  • 21
    • 84864584881 scopus 로고    scopus 로고
    • Cadherins and neuropsychiatric disorders
    • 22765916 10.1016/j.brainres.2012.06.020 1:CAS:528:DC%2BC38XhtFGlurfI
    • Redies C, Hertel N, Hubner CA (2012) Cadherins and neuropsychiatric disorders. Brain Res 1470:130-144
    • (2012) Brain Res , vol.1470 , pp. 130-144
    • Redies, C.1    Hertel, N.2    Hubner, C.A.3
  • 23
    • 45349091378 scopus 로고    scopus 로고
    • ADAM10-mediated E-cadherin release is regulated by proinflammatory cytokines and modulates keratinocyte cohesion in eczematous dermatitis
    • 18200054 10.1038/sj.jid.5701242 1:CAS:528:DC%2BD1cXntVersbs%3D
    • Maretzky T, Scholz F, Koten B, Proksch E, Saftig P, Reiss K (2008) ADAM10-mediated E-cadherin release is regulated by proinflammatory cytokines and modulates keratinocyte cohesion in eczematous dermatitis. J Invest Dermatol 128(7):1737-1746
    • (2008) J Invest Dermatol , vol.128 , Issue.7 , pp. 1737-1746
    • Maretzky, T.1    Scholz, F.2    Koten, B.3    Proksch, E.4    Saftig, P.5    Reiss, K.6
  • 24
    • 49649103585 scopus 로고    scopus 로고
    • The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation
    • 18434311 10.1074/jbc.M801329200 1:CAS:528:DC%2BD1cXnsVCnt7o%3D
    • Najy AJ, Day KC, Day ML (2008) The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation. J Biol Chem 283(26):18393-18401
    • (2008) J Biol Chem , vol.283 , Issue.26 , pp. 18393-18401
    • Najy, A.J.1    Day, K.C.2    Day, M.L.3
  • 25
    • 0033535040 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycan syndecan-2 induces the maturation of dendritic spines in rat hippocampal neurons
    • 9971750 10.1083/jcb.144.3.575 1:CAS:528:DyaK1MXhtFGqsr0%3D
    • Ethell IM, Yamaguchi Y (1999) Cell surface heparan sulfate proteoglycan syndecan-2 induces the maturation of dendritic spines in rat hippocampal neurons. J Cell Biol 144(3):575-586
    • (1999) J Cell Biol , vol.144 , Issue.3 , pp. 575-586
    • Ethell, I.M.1    Yamaguchi, Y.2
  • 26
    • 0028216755 scopus 로고
    • Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3)
    • 8175719 1:CAS:528:DyaK2cXivFSkurY%3D
    • Raulo E, Chernousov MA, Carey DJ, Nolo R, Rauvala H (1994) Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3). J Biol Chem 269(17):12999-13004
    • (1994) J Biol Chem , vol.269 , Issue.17 , pp. 12999-13004
    • Raulo, E.1    Chernousov, M.A.2    Carey, D.J.3    Nolo, R.4    Rauvala, H.5
  • 28
    • 33646863047 scopus 로고    scopus 로고
    • The shedding of syndecan-4 and syndecan-1 from HeLa cells and human primary macrophages is accelerated by SDF-1/CXCL12 and mediated by the matrix metalloproteinase-9
    • 16513763 10.1093/glycob/cwj098 1:CAS:528:DC%2BD28XkvVSrsL4%3D
    • Brule S, Charnaux N, Sutton A, Ledoux D, Chaigneau T, Saffar L, Gattegno L (2006) The shedding of syndecan-4 and syndecan-1 from HeLa cells and human primary macrophages is accelerated by SDF-1/CXCL12 and mediated by the matrix metalloproteinase-9. Glycobiology 16(6):488-501
    • (2006) Glycobiology , vol.16 , Issue.6 , pp. 488-501
    • Brule, S.1    Charnaux, N.2    Sutton, A.3    Ledoux, D.4    Chaigneau, T.5    Saffar, L.6    Gattegno, L.7
  • 29
    • 33744951974 scopus 로고    scopus 로고
    • Syndecan-2 is expressed in the microvasculature of gliomas and regulates angiogenic processes in microvascular endothelial cells
    • 16574663 10.1074/jbc.C600075200 1:CAS:528:DC%2BD28XkslGqsr0%3D
    • Fears CY, Gladson CL, Woods A (2006) Syndecan-2 is expressed in the microvasculature of gliomas and regulates angiogenic processes in microvascular endothelial cells. J Biol Chem 281(21):14533-14536
    • (2006) J Biol Chem , vol.281 , Issue.21 , pp. 14533-14536
    • Fears, C.Y.1    Gladson, C.L.2    Woods, A.3
  • 30
    • 18744383614 scopus 로고    scopus 로고
    • Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury
    • 12464176 10.1016/S0092-8674(02)01079-6 1:CAS:528:DC%2BD38XptlGrtbs%3D
    • Li Q, Park PW, Wilson CL, Parks WC (2002) Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury. Cell 111(5):635-646
    • (2002) Cell , vol.111 , Issue.5 , pp. 635-646
    • Li, Q.1    Park, P.W.2    Wilson, C.L.3    Parks, W.C.4
  • 31
    • 0142103466 scopus 로고    scopus 로고
    • Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration
    • 12904296 10.1074/jbc.M306736200 1:CAS:528:DC%2BD3sXotFWgsLo%3D
    • Endo K, Takino T, Miyamori H, Kinsen H, Yoshizaki T, Furukawa M, Sato H (2003) Cleavage of syndecan-1 by membrane type matrix metalloproteinase-1 stimulates cell migration. J Biol Chem 278(42):40764-40770
    • (2003) J Biol Chem , vol.278 , Issue.42 , pp. 40764-40770
    • Endo, K.1    Takino, T.2    Miyamori, H.3    Kinsen, H.4    Yoshizaki, T.5    Furukawa, M.6    Sato, H.7
  • 32
    • 73649109903 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 17 (ADAM17) mediates inflammation-induced shedding of syndecan-1 and -4 by lung epithelial cells
    • 19875451 10.1074/jbc.M109.059394 1:CAS:528:DC%2BD1MXhs1SqtrzO
    • Pruessmeyer J, Martin C, Hess FM, Schwarz N, Schmidt S, Kogel T, Hoettecke N, Schmidt B, Sechi A, Uhlig S, Ludwig A (2010) A disintegrin and metalloproteinase 17 (ADAM17) mediates inflammation-induced shedding of syndecan-1 and -4 by lung epithelial cells. J Biol Chem 285(1):555-564
    • (2010) J Biol Chem , vol.285 , Issue.1 , pp. 555-564
    • Pruessmeyer, J.1    Martin, C.2    Hess, F.M.3    Schwarz, N.4    Schmidt, S.5    Kogel, T.6    Hoettecke, N.7    Schmidt, B.8    Sechi, A.9    Uhlig, S.10    Ludwig, A.11
  • 34
    • 26444448409 scopus 로고    scopus 로고
    • L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth
    • 16199880 10.1128/MCB.25.20.9040-9053.2005 1:CAS:528:DC%2BD2MXhtFWis7%2FO
    • Maretzky T, Schulte M, Ludwig A, Rose-John S, Blobel C, Hartmann D, Altevogt P, Saftig P, Reiss K (2005) L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth. Mol Cell Biol 25(20):9040-9053
    • (2005) Mol Cell Biol , vol.25 , Issue.20 , pp. 9040-9053
    • Maretzky, T.1    Schulte, M.2    Ludwig, A.3    Rose-John, S.4    Blobel, C.5    Hartmann, D.6    Altevogt, P.7    Saftig, P.8    Reiss, K.9
  • 35
    • 0037266939 scopus 로고    scopus 로고
    • Intracellular signaling by the neural cell adhesion molecule
    • 12587671 10.1023/A:1021660531484 1:CAS:528:DC%2BD38XpsFCis70%3D
    • Povlsen GK, Ditlevsen DK, Berezin V, Bock E (2003) Intracellular signaling by the neural cell adhesion molecule. Neurochem Res 28(1):127-141
    • (2003) Neurochem Res , vol.28 , Issue.1 , pp. 127-141
    • Povlsen, G.K.1    Ditlevsen, D.K.2    Berezin, V.3    Bock, E.4
  • 36
    • 0035215303 scopus 로고    scopus 로고
    • Contribution of the neural cell adhesion molecule to neuronal and synaptic plasticity
    • 11783716 1:STN:280:DC%2BD38%2FlvVemsQ%3D%3D
    • Kiss JZ, Muller D (2001) Contribution of the neural cell adhesion molecule to neuronal and synaptic plasticity. Rev Neurosci 12(4):297-310
    • (2001) Rev Neurosci , vol.12 , Issue.4 , pp. 297-310
    • Kiss, J.Z.1    Muller, D.2
  • 37
    • 33749037455 scopus 로고    scopus 로고
    • NCAM promotes assembly and activity-dependent remodeling of the postsynaptic signaling complex
    • 17000882 10.1083/jcb.200604145 1:CAS:528:DC%2BD28Xht12ht7bI
    • Sytnyk V, Leshchyns'ka I, Nikonenko AG, Schachner M (2006) NCAM promotes assembly and activity-dependent remodeling of the postsynaptic signaling complex. J Cell Biol 174(7):1071-1085
    • (2006) J Cell Biol , vol.174 , Issue.7 , pp. 1071-1085
    • Sytnyk, V.1    Leshchyns'Ka, I.2    Nikonenko, A.G.3    Schachner, M.4
  • 38
    • 33750807736 scopus 로고    scopus 로고
    • Metalloprotease-induced ectodomain shedding of neural cell adhesion molecule (NCAM)
    • 16967505 10.1002/neu.20257 1:CAS:528:DC%2BD28Xht1WmsrjO
    • Hinkle CL, Diestel S, Lieberman J, Maness PF (2006) Metalloprotease- induced ectodomain shedding of neural cell adhesion molecule (NCAM). J Neurobiol 66(12):1378-1395
    • (2006) J Neurobiol , vol.66 , Issue.12 , pp. 1378-1395
    • Hinkle, C.L.1    Diestel, S.2    Lieberman, J.3    Maness, P.F.4
  • 39
    • 0035940469 scopus 로고    scopus 로고
    • A biophysical model of bidirectional synaptic plasticity: Dependence on AMPA and NMDA receptors
    • 11675507 10.1073/pnas.201404598 1:CAS:528:DC%2BD3MXotFahs7s%3D
    • Castellani GC, Quinlan EM, Cooper LN, Shouval HZ (2001) A biophysical model of bidirectional synaptic plasticity: dependence on AMPA and NMDA receptors. Proc Natl Acad Sci USA 98(22):12772-12777
    • (2001) Proc Natl Acad Sci USA , vol.98 , Issue.22 , pp. 12772-12777
    • Castellani, G.C.1    Quinlan, E.M.2    Cooper, L.N.3    Shouval, H.Z.4
  • 40
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: A control mechanism conserved from bacteria to humans
    • 10693756 10.1016/S0092-8674(00)80675-3 1:CAS:528:DC%2BD3cXhsVOltbg%3D
    • Brown MS, Ye J, Rawson RB, Goldstein JL (2000) Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100(4):391-398
    • (2000) Cell , vol.100 , Issue.4 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 41
    • 0042821897 scopus 로고    scopus 로고
    • NMDA-dependent proteolysis of presynaptic adhesion molecule L1 in the hippocampus by neuropsin
    • 12944500 1:CAS:528:DC%2BD3sXmvFGhtLY%3D
    • Matsumoto-Miyai K, Ninomiya A, Yamasaki H, Tamura H, Nakamura Y, Shiosaka S (2003) NMDA-dependent proteolysis of presynaptic adhesion molecule L1 in the hippocampus by neuropsin. J Neurosci 23(21):7727-7736
    • (2003) J Neurosci , vol.23 , Issue.21 , pp. 7727-7736
    • Matsumoto-Miyai, K.1    Ninomiya, A.2    Yamasaki, H.3    Tamura, H.4    Nakamura, Y.5    Shiosaka, S.6
  • 42
    • 2442456895 scopus 로고    scopus 로고
    • A synthetic neural cell adhesion molecule mimetic peptide promotes synaptogenesis, enhances presynaptic function, and facilitates memory consolidation
    • 15115815 10.1523/JNEUROSCI.0436-04.2004 1:CAS:528:DC%2BD2cXjvFemsL0%3D
    • Cambon K, Hansen SM, Venero C, Herrero AI, Skibo G, Berezin V, Bock E, Sandi C (2004) A synthetic neural cell adhesion molecule mimetic peptide promotes synaptogenesis, enhances presynaptic function, and facilitates memory consolidation. J Neurosci 24(17):4197-4204
    • (2004) J Neurosci , vol.24 , Issue.17 , pp. 4197-4204
    • Cambon, K.1    Hansen, S.M.2    Venero, C.3    Herrero, A.I.4    Skibo, G.5    Berezin, V.6    Bock, E.7    Sandi, C.8
  • 43
    • 1442275737 scopus 로고    scopus 로고
    • Distinct roles of different neural cell adhesion molecule (NCAM) isoforms in synaptic maturation revealed by analysis of NCAM 180 kDa isoform-deficient mice
    • 14985425 10.1523/JNEUROSCI.4406-03.2004 1:CAS:528:DC%2BD2cXitVWktrs%3D
    • Polo-Parada L, Bose CM, Plattner F, Landmesser LT (2004) Distinct roles of different neural cell adhesion molecule (NCAM) isoforms in synaptic maturation revealed by analysis of NCAM 180 kDa isoform-deficient mice. J Neurosci 24(8):1852-1864
    • (2004) J Neurosci , vol.24 , Issue.8 , pp. 1852-1864
    • Polo-Parada, L.1    Bose, C.M.2    Plattner, F.3    Landmesser, L.T.4
  • 44
    • 0028230594 scopus 로고
    • Increase in extracellular NCAM and amyloid precursor protein following induction of long-term potentiation in the dentate gyrus of anaesthetized rats
    • 8047297 10.1016/0304-3940(94)90360-3 1:CAS:528:DyaK2cXksFCmt7k%3D
    • Fazeli MS, Breen K, Errington ML, Bliss TV (1994) Increase in extracellular NCAM and amyloid precursor protein following induction of long-term potentiation in the dentate gyrus of anaesthetized rats. Neurosci Lett 169(1-2):77-80
    • (1994) Neurosci Lett , vol.169 , Issue.1-2 , pp. 77-80
    • Fazeli, M.S.1    Breen, K.2    Errington, M.L.3    Bliss, T.V.4
  • 45
    • 0032539086 scopus 로고    scopus 로고
    • Activation of NMDA receptors stimulates extracellular proteolysis of cell adhesion molecules in hippocampus
    • 9804935 10.1016/S0006-8993(98)00907-X 1:CAS:528:DyaK1cXmvFWht78%3D
    • Hoffman KB, Larson J, Bahr BA, Lynch G (1998) Activation of NMDA receptors stimulates extracellular proteolysis of cell adhesion molecules in hippocampus. Brain Res 811(1-2):152-155
    • (1998) Brain Res , vol.811 , Issue.1-2 , pp. 152-155
    • Hoffman, K.B.1    Larson, J.2    Bahr, B.A.3    Lynch, G.4
  • 46
    • 21844474852 scopus 로고    scopus 로고
    • Neural cell adhesion molecule function is regulated by metalloproteinase-mediated ectodomain release
    • 15884014 10.1002/jnr.20530
    • Hubschmann MV, Skladchikova G, Bock E, Berezin V (2005) Neural cell adhesion molecule function is regulated by metalloproteinase-mediated ectodomain release. J Neurosci Res 80(6):826-837
    • (2005) J Neurosci Res , vol.80 , Issue.6 , pp. 826-837
    • Hubschmann, M.V.1    Skladchikova, G.2    Bock, E.3    Berezin, V.4
  • 47
    • 33751541414 scopus 로고    scopus 로고
    • MMP-2, VCAM-1 and NCAM-1 expression in the brain of rats with experimental autoimmune encephalomyelitis as a trigger mechanism for synaptic plasticity and pathology
    • 17064783 10.1016/j.jneuroim.2006.08.013 1:CAS:528:DC%2BD28Xht1Krs7nP
    • Jovanova-Nesic K, Shoenfeld Y (2006) MMP-2, VCAM-1 and NCAM-1 expression in the brain of rats with experimental autoimmune encephalomyelitis as a trigger mechanism for synaptic plasticity and pathology. J Neuroimmunol 181(1-2):112-121
    • (2006) J Neuroimmunol , vol.181 , Issue.1-2 , pp. 112-121
    • Jovanova-Nesic, K.1    Shoenfeld, Y.2
  • 48
    • 84857233056 scopus 로고    scopus 로고
    • NCAM2/OCAM/RNCAM: Cell adhesion molecule with a role in neuronal compartmentalization
    • 22155300 10.1016/j.biocel.2011.11.020 1:CAS:528:DC%2BC38XjtFSntrc%3D
    • Winther M, Berezin V, Walmod PS (2012) NCAM2/OCAM/RNCAM: cell adhesion molecule with a role in neuronal compartmentalization. Int J Biochem Cell Biol 44(3):441-446
    • (2012) Int J Biochem Cell Biol , vol.44 , Issue.3 , pp. 441-446
    • Winther, M.1    Berezin, V.2    Walmod, P.S.3
  • 49
    • 81255157685 scopus 로고    scopus 로고
    • Characterization of nectin processing mediated by presenilin-dependent gamma-secretase
    • 21910732 10.1111/j.1471-4159.2011.07479.x 1:CAS:528:DC%2BC3MXhs1Gqtb7L
    • Kim J, Chang A, Dudak A, Federoff HJ, Lim ST (2011) Characterization of nectin processing mediated by presenilin-dependent gamma-secretase. J Neurochem 119(5):945-956
    • (2011) J Neurochem , vol.119 , Issue.5 , pp. 945-956
    • Kim, J.1    Chang, A.2    Dudak, A.3    Federoff, H.J.4    Lim, S.T.5
  • 50
    • 84857192747 scopus 로고    scopus 로고
    • Ectodomain shedding of nectin-1 regulates the maintenance of dendritic spine density
    • 22118475 10.1111/j.1471-4159.2011.07592.x 1:CAS:528:DC%2BC38XksFCntrY%3D
    • Lim ST, Chang A, Giuliano RE, Federoff HJ (2012) Ectodomain shedding of nectin-1 regulates the maintenance of dendritic spine density. J Neurochem 120(5):741-751
    • (2012) J Neurochem , vol.120 , Issue.5 , pp. 741-751
    • Lim, S.T.1    Chang, A.2    Giuliano, R.E.3    Federoff, H.J.4
  • 51
    • 77954917968 scopus 로고    scopus 로고
    • Activity-dependent alpha-cleavage of nectin-1 is mediated by a disintegrin and metalloprotease 10 (ADAM10)
    • 20501653 10.1074/jbc.M110.126649 1:CAS:528:DC%2BC3cXovFemtrg%3D
    • Kim J, Lilliehook C, Dudak A, Prox J, Saftig P, Federoff HJ, Lim ST (2010) Activity-dependent alpha-cleavage of nectin-1 is mediated by a disintegrin and metalloprotease 10 (ADAM10). J Biol Chem 285(30):22919-22926
    • (2010) J Biol Chem , vol.285 , Issue.30 , pp. 22919-22926
    • Kim, J.1    Lilliehook, C.2    Dudak, A.3    Prox, J.4    Saftig, P.5    Federoff, H.J.6    Lim, S.T.7
  • 52
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • 13678586 10.1016/j.cell.2003.08.008 1:CAS:528:DC%2BD3sXntlaltL0%3D
    • Marambaud P, Wen PH, Dutt A, Shioi J, Takashima A, Siman R, Robakis NK (2003) A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell 114(5):635-645
    • (2003) Cell , vol.114 , Issue.5 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5    Siman, R.6    Robakis, N.K.7
  • 53
    • 33845422266 scopus 로고    scopus 로고
    • AF6/s-afadin is a dual residency protein and localizes to a novel subnuclear compartment
    • 17013812 10.1002/jcp.20853 1:CAS:528:DC%2BD28XhtlWktrnL
    • Buchert M, Poon C, King JA, Baechi T, D'Abaco G, Hollande F, Hovens CM (2007) AF6/s-afadin is a dual residency protein and localizes to a novel subnuclear compartment. J Cell Physiol 210(1):212-223
    • (2007) J Cell Physiol , vol.210 , Issue.1 , pp. 212-223
    • Buchert, M.1    Poon, C.2    King, J.A.3    Baechi, T.4    D'Abaco, G.5    Hollande, F.6    Hovens, C.M.7
  • 54
    • 36248987849 scopus 로고    scopus 로고
    • SynCAMs organize synapses through heterophilic adhesion
    • 18003830 10.1523/JNEUROSCI.2739-07.2007 1:CAS:528:DC%2BD2sXhsVSgs7bE
    • Fogel AI, Akins MR, Krupp AJ, Stagi M, Stein V, Biederer T (2007) SynCAMs organize synapses through heterophilic adhesion. J Neurosci 27(46):12516-12530
    • (2007) J Neurosci , vol.27 , Issue.46 , pp. 12516-12530
    • Fogel, A.I.1    Akins, M.R.2    Krupp, A.J.3    Stagi, M.4    Stein, V.5    Biederer, T.6
  • 55
    • 50849110507 scopus 로고    scopus 로고
    • Neuronal RA175/SynCAM1 isoforms are processed by tumor necrosis factor-alpha-converting enzyme (TACE)/ADAM17-like proteases
    • 18718504 10.1016/j.neulet.2008.08.023 1:CAS:528:DC%2BD1cXhtV2jsL3F
    • Tanabe Y, Kasahara T, Momoi T, Fujita E (2008) Neuronal RA175/SynCAM1 isoforms are processed by tumor necrosis factor-alpha-converting enzyme (TACE)/ADAM17-like proteases. Neurosci Lett 444(1):16-21
    • (2008) Neurosci Lett , vol.444 , Issue.1 , pp. 16-21
    • Tanabe, Y.1    Kasahara, T.2    Momoi, T.3    Fujita, E.4
  • 56
    • 84864137954 scopus 로고    scopus 로고
    • Synaptic cell adhesion molecule-2 and collapsin response mediator protein-2 are novel members of the matrix metalloproteinase-9 degradome
    • 22694054 10.1111/j.1471-4159.2012.07829.x 1:CAS:528:DC%2BC38XhtFeit77L
    • Bajor M, Michaluk P, Gulyassy P, Kekesi AK, Juhasz G, Kaczmarek L (2012) Synaptic cell adhesion molecule-2 and collapsin response mediator protein-2 are novel members of the matrix metalloproteinase-9 degradome. J Neurochem 122(4):775-788
    • (2012) J Neurochem , vol.122 , Issue.4 , pp. 775-788
    • Bajor, M.1    Michaluk, P.2    Gulyassy, P.3    Kekesi, A.K.4    Juhasz, G.5    Kaczmarek, L.6
  • 58
    • 0032054657 scopus 로고    scopus 로고
    • Polarized distribution and cell type-specific localization of telencephalin, an intercellular adhesion molecule
    • 9556028 10.1002/(SICI)1097-4547(19980401)52:1<43: AID-JNR5>3.0. CO;2-K 1:CAS:528:DyaK1cXisVSrtLs%3D
    • Benson DL, Yoshihara Y, Mori K (1998) Polarized distribution and cell type-specific localization of telencephalin, an intercellular adhesion molecule. J Neurosci Res 52(1):43-53
    • (1998) J Neurosci Res , vol.52 , Issue.1 , pp. 43-53
    • Benson, D.L.1    Yoshihara, Y.2    Mori, K.3
  • 59
    • 13944251668 scopus 로고    scopus 로고
    • A novel phenylalanine-based targeting signal directs telencephalin to neuronal dendrites
    • 15689548 10.1523/JNEUROSCI.3853-04.2005 1:CAS:528:DC%2BD2MXhsVahs78%3D
    • Mitsui S, Saito M, Hayashi K, Mori K, Yoshihara Y (2005) A novel phenylalanine-based targeting signal directs telencephalin to neuronal dendrites. J Neurosci 25(5):1122-1131
    • (2005) J Neurosci , vol.25 , Issue.5 , pp. 1122-1131
    • Mitsui, S.1    Saito, M.2    Hayashi, K.3    Mori, K.4    Yoshihara, Y.5
  • 61
    • 32544436404 scopus 로고    scopus 로고
    • Telencephalin slows spine maturation
    • 16467526 10.1523/JNEUROSCI.2651-05.2006 1:CAS:528:DC%2BD28XhslChtrk%3D
    • Matsuno H, Okabe S, Mishina M, Yanagida T, Mori K, Yoshihara Y (2006) Telencephalin slows spine maturation. J Neurosci 26(6):1776-1786
    • (2006) J Neurosci , vol.26 , Issue.6 , pp. 1776-1786
    • Matsuno, H.1    Okabe, S.2    Mishina, M.3    Yanagida, T.4    Mori, K.5    Yoshihara, Y.6
  • 62
    • 77951881501 scopus 로고    scopus 로고
    • Matrix metalloproteinase-dependent shedding of intercellular adhesion molecule-5 occurs with long-term potentiation
    • 20045450 10.1016/j.neuroscience.2009.12.061 1:CAS:528: DC%2BC3cXitVejsL8%3D
    • Conant K, Wang Y, Szklarczyk A, Dudak A, Mattson MP, Lim ST (2010) Matrix metalloproteinase-dependent shedding of intercellular adhesion molecule-5 occurs with long-term potentiation. Neuroscience 166(2):508-521
    • (2010) Neuroscience , vol.166 , Issue.2 , pp. 508-521
    • Conant, K.1    Wang, Y.2    Szklarczyk, A.3    Dudak, A.4    Mattson, M.P.5    Lim, S.T.6
  • 63
    • 84865054321 scopus 로고    scopus 로고
    • MMPs and Soluble ICAM-5 increase neuronal excitability within in vitro networks of hippocampal neurons
    • 22912716 10.1371/journal.pone.0042631 1:CAS:528:DC%2BC38Xht1amsrrN
    • Niedringhaus M, Chen X, Dzakpasu R, Conant K (2012) MMPs and Soluble ICAM-5 increase neuronal excitability within in vitro networks of hippocampal neurons. PLoS ONE 7(8):e42631
    • (2012) PLoS ONE , vol.7 , Issue.8 , pp. 42631
    • Niedringhaus, M.1    Chen, X.2    Dzakpasu, R.3    Conant, K.4
  • 64
    • 0026543686 scopus 로고
    • Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
    • 1741056 10.1038/355696a0 1:CAS:528:DyaK3sXitFSlu78%3D
    • Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, Slaughter CA, Sernett SW, Campbell KP (1992) Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 355(6362):696-702
    • (1992) Nature , vol.355 , Issue.6362 , pp. 696-702
    • Ibraghimov-Beskrovnaya, O.1    Ervasti, J.M.2    Leveille, C.J.3    Slaughter, C.A.4    Sernett, S.W.5    Campbell, K.P.6
  • 67
    • 0345515991 scopus 로고    scopus 로고
    • Kainate-evoked changes in dystrophin messenger RNA levels in the rat hippocampus
    • 9539217 10.1016/S0306-4522(97)00562-9 1:CAS:528:DyaK1cXhvV2ksb4%3D
    • Gorecki DC, Lukasiuk K, Szklarczyk A, Kaczmarek L (1998) Kainate-evoked changes in dystrophin messenger RNA levels in the rat hippocampus. Neuroscience 84(2):467-477
    • (1998) Neuroscience , vol.84 , Issue.2 , pp. 467-477
    • Gorecki, D.C.1    Lukasiuk, K.2    Szklarczyk, A.3    Kaczmarek, L.4
  • 68
    • 0344731376 scopus 로고    scopus 로고
    • Differential seizure-induced and developmental changes of neurexin expression
    • 10408888 10.1006/mcne.1999.0740 1:CAS:528:DyaK1MXivFOktL8%3D
    • Gorecki DC, Szklarczyk A, Lukasiuk K, Kaczmarek L, Simons JP (1999) Differential seizure-induced and developmental changes of neurexin expression. Mol Cell Neurosci 13(3):218-227
    • (1999) Mol Cell Neurosci , vol.13 , Issue.3 , pp. 218-227
    • Gorecki, D.C.1    Szklarczyk, A.2    Lukasiuk, K.3    Kaczmarek, L.4    Simons, J.P.5
  • 69
    • 79955761820 scopus 로고    scopus 로고
    • Presenilin/gamma-secretase regulates neurexin processing at synapses
    • 21559374 10.1371/journal.pone.0019430 1:CAS:528:DC%2BC3MXlslGgtbc%3D
    • Saura CA, Servian-Morilla E, Scholl FG (2011) Presenilin/gamma-secretase regulates neurexin processing at synapses. PLoS ONE 6(4):e19430
    • (2011) PLoS ONE , vol.6 , Issue.4 , pp. 19430
    • Saura, C.A.1    Servian-Morilla, E.2    Scholl, F.G.3
  • 70
    • 78951488794 scopus 로고    scopus 로고
    • Processing of the synaptic cell adhesion molecule neurexin-3beta by Alzheimer disease alpha- and gamma-secretases
    • 21084300 10.1074/jbc.M110.142521 1:CAS:528:DC%2BC3MXosValsw%3D%3D
    • Bot N, Schweizer C, Ben Halima S, Fraering PC (2011) Processing of the synaptic cell adhesion molecule neurexin-3beta by Alzheimer disease alpha- and gamma-secretases. J Biol Chem 286(4):2762-2773
    • (2011) J Biol Chem , vol.286 , Issue.4 , pp. 2762-2773
    • Bot, N.1    Schweizer, C.2    Ben Halima, S.3    Fraering, P.C.4
  • 73
    • 70349658097 scopus 로고    scopus 로고
    • Thrombospondin-1 modulates vascular endothelial growth factor activity at the receptor level
    • 19528255 10.1096/fj.09-131649 1:CAS:528:DC%2BD1MXht1GjtLbO
    • Zhang X, Kazerounian S, Duquette M, Perruzzi C, Nagy JA, Dvorak HF, Parangi S, Lawler J (2009) Thrombospondin-1 modulates vascular endothelial growth factor activity at the receptor level. Faseb J 23(10):3368-3376
    • (2009) Faseb J , vol.23 , Issue.10 , pp. 3368-3376
    • Zhang, X.1    Kazerounian, S.2    Duquette, M.3    Perruzzi, C.4    Nagy, J.A.5    Dvorak, H.F.6    Parangi, S.7    Lawler, J.8
  • 74
    • 33751073396 scopus 로고    scopus 로고
    • ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2
    • 17082774 10.1038/sj.emboj.7601400 1:CAS:528:DC%2BD28Xht1Sgt7zN
    • Lee NV, Sato M, Annis DS, Loo JA, Wu L, Mosher DF, Iruela-Arispe ML (2006) ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2. EMBO J 25(22):5270-5283
    • (2006) EMBO J , vol.25 , Issue.22 , pp. 5270-5283
    • Lee, N.V.1    Sato, M.2    Annis, D.S.3    Loo, J.A.4    Wu, L.5    Mosher, D.F.6    Iruela-Arispe, M.L.7
  • 75
    • 0028157338 scopus 로고
    • Matrix-bound thrombospondin promotes angiogenesis in vitro
    • 7507491 10.1083/jcb.124.1.183 1:CAS:528:DyaK2cXnsVantQ%3D%3D
    • Nicosia RF, Tuszynski GP (1994) Matrix-bound thrombospondin promotes angiogenesis in vitro. J Cell Biol 124(1-2):183-193
    • (1994) J Cell Biol , vol.124 , Issue.1-2 , pp. 183-193
    • Nicosia, R.F.1    Tuszynski, G.P.2
  • 76
    • 34247341829 scopus 로고    scopus 로고
    • Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome
    • 17200105 10.1074/mcp.M600341-MCP200 1:CAS:528:DC%2BD2sXksVKgtbg%3D
    • Dean RA, Overall CM (2007) Proteomics discovery of metalloproteinase substrates in the cellular context by iTRAQ labeling reveals a diverse MMP-2 substrate degradome. Mol Cell Proteomics 6(4):611-623
    • (2007) Mol Cell Proteomics , vol.6 , Issue.4 , pp. 611-623
    • Dean, R.A.1    Overall, C.M.2
  • 77
    • 47949123468 scopus 로고    scopus 로고
    • Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: Dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding
    • 18505826 10.1128/MCB.01775-07 1:CAS:528:DC%2BD1cXptF2luro%3D
    • Butler GS, Dean RA, Tam EM, Overall CM (2008) Pharmacoproteomics of a metalloproteinase hydroxamate inhibitor in breast cancer cells: dynamics of membrane type 1 matrix metalloproteinase-mediated membrane protein shedding. Mol Cell Biol 28(15):4896-4914
    • (2008) Mol Cell Biol , vol.28 , Issue.15 , pp. 4896-4914
    • Butler, G.S.1    Dean, R.A.2    Tam, E.M.3    Overall, C.M.4
  • 78
    • 77951134556 scopus 로고    scopus 로고
    • Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics
    • 20305284 10.1074/mcp.M000050-MCP201 1:CAS:528:DC%2BC3cXpslyrsLY%3D
    • Prudova A, Auf Dem Keller U, Butler GS, Overall CM (2010) Multiplex N-terminome analysis of MMP-2 and MMP-9 substrate degradomes by iTRAQ-TAILS quantitative proteomics. Mol Cell Proteomics 9(5):894-911
    • (2010) Mol Cell Proteomics , vol.9 , Issue.5 , pp. 894-911
    • Prudova, A.1    Auf Dem Keller, U.2    Butler, G.S.3    Overall, C.M.4
  • 79
    • 0038349637 scopus 로고    scopus 로고
    • Cleavage of cartilage oligomeric matrix protein (thrombospondin-5) by matrix metalloproteinases and a disintegrin and metalloproteinase with thrombospondin motifs
    • 12853037 10.1016/S0945-053X(03)00034-9 1:CAS:528:DC%2BD3sXlt1enur0%3D
    • Dickinson SC, Vankemmelbeke MN, Buttle DJ, Rosenberg K, Heinegard D, Hollander AP (2003) Cleavage of cartilage oligomeric matrix protein (thrombospondin-5) by matrix metalloproteinases and a disintegrin and metalloproteinase with thrombospondin motifs. Matrix Biol 22(3):267-278
    • (2003) Matrix Biol , vol.22 , Issue.3 , pp. 267-278
    • Dickinson, S.C.1    Vankemmelbeke, M.N.2    Buttle, D.J.3    Rosenberg, K.4    Heinegard, D.5    Hollander, A.P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.