메뉴 건너뛰기




Volumn 23, Issue 6, 2012, Pages 1068-1079

A secreted MMP is required for reepithelialization during wound healing

Author keywords

[No Author keywords available]

Indexed keywords

GELATINASE A; INTERSTITIAL COLLAGENASE; MITOGEN ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE;

EID: 84858388258     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E11-09-0745     Document Type: Article
Times cited : (125)

References (64)
  • 1
    • 33847351560 scopus 로고    scopus 로고
    • Metastatic ability of Drosophila tumors depends on MMP activity
    • DOI 10.1016/j.ydbio.2006.12.001, PII S0012160606014011
    • Beaucher M, Hersperger E, Page-McCaw A, Shearn A (2007). Metastatic ability of Drosophila tumors depends on MMP activity. Dev Biol 303, 625-634. (Pubitemid 46341291)
    • (2007) Developmental Biology , vol.303 , Issue.2 , pp. 625-634
    • Beaucher, M.1    Hersperger, E.2    Page-McCaw, A.3    Shearn, A.4
  • 2
    • 0000391746 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
    • Bergers G et al. (2000). Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nat Cell Biol 2, 737-744.
    • (2000) Nat Cell Biol , vol.2 , pp. 737-744
    • Bergers, G.1
  • 3
    • 0024503589 scopus 로고
    • Prolonged activation of jun and collagenase genes by tumour necrosis factor-alpha
    • DOI 10.1038/337661a0
    • Brenner DA, O'Hara M, Angel P, Chojkier M, Karin M (1989). Prolonged activation of jun and collagenase genes by tumour necrosis factor-alpha. Nature 337, 661-663. (Pubitemid 19054296)
    • (1989) Nature , vol.337 , Issue.6208 , pp. 661-663
    • Brenner, D.A.1    O'Hara, M.2    Angel, P.3    Chojkier, M.4    Karin, M.5
  • 5
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • DOI 10.1126/science.1116995
    • Discher DE, Janmey P, Wang Y-L (2005). Tissue cells feel and respond to the stiffness of their substrate. Science 310, 1139-1143. (Pubitemid 41681732)
    • (2005) Science , vol.310 , Issue.5751 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.-L.3
  • 6
    • 68949210380 scopus 로고    scopus 로고
    • RSK is a principal effector of the RAS-ERK pathway for eliciting a coordinate promotile/invasive gene program and phenotype in epithelial cells
    • Doehn U et al. (2009). RSK is a principal effector of the RAS-ERK pathway for eliciting a coordinate promotile/invasive gene program and phenotype in epithelial cells. Mol Cell 35, 511-522.
    • (2009) Mol Cell , vol.35 , pp. 511-522
    • Doehn, U.1
  • 7
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z (2002). New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2, 161-174. (Pubitemid 37328786)
    • (2002) Nature Reviews Cancer , vol.2 , Issue.3 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 8
    • 0030866482 scopus 로고    scopus 로고
    • In situ activation pattern of Drosophila EGF receptor pathway during development
    • DOI 10.1126/science.277.5329.1103
    • Gabay L, Seger R, Shilo BZ (1997). In situ activation pattern of Drosophila EGF receptor pathway during development. Science 277, 1103-1106. (Pubitemid 27371633)
    • (1997) Science , vol.277 , Issue.5329 , pp. 1103-1106
    • Gabay, L.1    Seger, R.2    Shilo, B.-Z.3
  • 9
    • 19344365657 scopus 로고    scopus 로고
    • Cellular and genetic analysis of wound healing in Drosophila larvae
    • Galko MJ, Krasnow MA (2004). Cellular and genetic analysis of wound healing in Drosophila larvae. PLoS Biol 2, E239.
    • (2004) PLoS Biol , vol.2
    • Galko, M.J.1    Krasnow, M.A.2
  • 10
    • 0029069565 scopus 로고
    • Matrix metalloproteinases and processing of pro-TNF-alpha
    • Gearing A et al. (1995). Matrix metalloproteinases and processing of pro-TNF-alpha. J Leukocyte Biol 57, 774-777.
    • (1995) J Leukocyte Biol , vol.57 , pp. 774-777
    • Gearing, A.1
  • 11
    • 43049092274 scopus 로고    scopus 로고
    • Metalloproteinases and their inhibitors: Regulators of wound healing
    • Gill SE, Parks WC (2008). Metalloproteinases and their inhibitors: regulators of wound healing. Int J Biochem Cell Biol 40, 1334-1347.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1334-1347
    • Gill, S.E.1    Parks, W.C.2
  • 12
    • 62449085119 scopus 로고    scopus 로고
    • Distinct functions for the catalytic and hemopexin domains of a Drosophila matrix metalloproteinase
    • Glasheen BM, Kabra AT, Page-McCaw A (2009). Distinct functions for the catalytic and hemopexin domains of a Drosophila matrix metalloproteinase. Proc Natl Acad Sci USA 106, 2659-2664.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 2659-2664
    • Glasheen, B.M.1    Kabra, A.T.2    Page-McCaw, A.3
  • 14
    • 0033861140 scopus 로고    scopus 로고
    • Inflated wings, tissue autolysis and early death in tissue inhibitor of metalloproteinases mutants of Drosophila
    • Godenschwege TA, Pohar N, Buchner S, Buchner E (2000). Inflated wings, tissue autolysis and early death in tissue inhibitor of metalloproteinases mutants of Drosophila. Eur J Cell Biol 79, 495-501. (Pubitemid 30612204)
    • (2000) European Journal of Cell Biology , vol.79 , Issue.7 , pp. 495-501
    • Godenschwege, T.A.1    Pohar, N.2    Buchner, S.3    Buchner, E.4
  • 16
    • 1842377505 scopus 로고    scopus 로고
    • Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1
    • Gomis-Ruth FX et al. (1997). Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 389, 77-81.
    • (1997) Nature , vol.389 , pp. 77-81
    • Gomis-Ruth, F.X.1
  • 17
    • 0030935859 scopus 로고    scopus 로고
    • Regulation of 92 kDa type IV collagenase expression by the jun aminoterminal kinase- and the extracellular signal-regulated kinase-dependent signaling cascades
    • Gum R, Wang H, Lengyel E, Juarez J, Boyd D (1997). Regulation of 92 kDa type IV collagenase expression by the jun aminoterminal kinase- and the extracellular signal-regulated kinase-dependent signaling cascades. Oncogene 14, 1481-1493. (Pubitemid 27182438)
    • (1997) Oncogene , vol.14 , Issue.12 , pp. 1481-1493
    • Gum, R.1    Wang, H.2    Lengyel, E.3    Juarez, J.4    Boyd, D.5
  • 18
    • 43749088730 scopus 로고    scopus 로고
    • Wound repair and regeneration
    • DOI 10.1038/nature07039, PII NATURE07039
    • Gurtner GC, Werner S, Barrandon Y, Longaker MT (2008). Wound repair and regeneration. Nature 453, 314-321. (Pubitemid 351693137)
    • (2008) Nature , vol.453 , Issue.7193 , pp. 314-321
    • Gurtner, G.C.1    Werner, S.2    Barrandon, Y.3    Longaker, M.T.4
  • 20
    • 68449099008 scopus 로고    scopus 로고
    • MMP-13 plays a role in keratinocyte migration, angiogenesis, and contraction in mouse skin wound healing
    • Hattori N, Mochizuki S, Kishi K, Nakajima T, Takaishi H, D'Armiento J, Okada Y (2009). MMP-13 plays a role in keratinocyte migration, angiogenesis, and contraction in mouse skin wound healing. Am J Pathol 175, 533-546.
    • (2009) Am J Pathol , vol.175 , pp. 533-546
    • Hattori, N.1    Mochizuki, S.2    Kishi, K.3    Nakajima, T.4    Takaishi, H.5    D'Armiento, J.6    Okada, Y.7
  • 21
    • 79952111781 scopus 로고    scopus 로고
    • Detection of RTK pathway activation in Drosophila using anti-dpERK immunofluorescence staining
    • Helman A, Paroush Z (2010). Detection of RTK pathway activation in Drosophila using anti-dpERK immunofluorescence staining. Methods Mol Biol 661, 401-408.
    • (2010) Methods Mol Biol , vol.661 , pp. 401-408
    • Helman, A.1    Paroush, Z.2
  • 23
    • 0034710157 scopus 로고    scopus 로고
    • The evolution of cell adhesion
    • Hynes RO, Zhao Q (2000). The evolution of cell adhesion. J Cell Biol 150, F89-F96.
    • (2000) J Cell Biol , vol.150
    • Hynes, R.O.1    Zhao, Q.2
  • 24
    • 0037124314 scopus 로고    scopus 로고
    • Eiger, a TNF superfamily ligand that triggers the Drosophila JNK pathway
    • DOI 10.1093/emboj/cdf306
    • Igaki T, Kanda H, Yamamoto-Goto Y, Kanuka H, Kuranaga E, Aigaki T, Miura M (2002). Eiger, a TNF superfamily ligand that triggers the Drosophila JNK pathway. EMBO J 21, 3009-3018. (Pubitemid 34670385)
    • (2002) EMBO Journal , vol.21 , Issue.12 , pp. 3009-3018
    • Igaki, T.1    Kanda, H.2    Yamamoto-Goto, Y.3    Kanuka, H.4    Kuranaga, E.5    Aigaki, T.6    Miura, M.7
  • 25
    • 61749087213 scopus 로고    scopus 로고
    • Intrinsic tumor suppression and epithelial maintenance by endocytic activation of Eiger/TNF signaling in Drosophila
    • Igaki T, Pastor-Pareja JC, Aonuma H, Miura M, Xu T (2009). Intrinsic tumor suppression and epithelial maintenance by endocytic activation of Eiger/TNF signaling in Drosophila. Dev Cell 16, 458-465.
    • (2009) Dev Cell , vol.16 , pp. 458-465
    • Igaki, T.1    Pastor-Pareja, J.C.2    Aonuma, H.3    Miura, M.4    Xu, T.5
  • 26
    • 79957646416 scopus 로고    scopus 로고
    • Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling
    • Kirmse R, Otto H, Ludwig T (2011). Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling. J Cell Sci 124, 1857-1866.
    • (2011) J Cell Sci , vol.124 , pp. 1857-1866
    • Kirmse, R.1    Otto, H.2    Ludwig, T.3
  • 28
    • 62749193153 scopus 로고    scopus 로고
    • Mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis
    • Kyriakides TR, Wulsin D, Skokos EA, Fleckman P, Pirrone A, Shipley JM, Senior RM, Bornstein P (2009). Mice that lack matrix metalloproteinase-9 display delayed wound healing associated with delayed reepithelization and disordered collagen fibrillogenesis. Matrix Biol 28, 65-73.
    • (2009) Matrix Biol , vol.28 , pp. 65-73
    • Kyriakides, T.R.1    Wulsin, D.2    Skokos, E.A.3    Fleckman, P.4    Pirrone, A.5    Shipley, J.M.6    Senior, R.M.7    Bornstein, P.8
  • 30
    • 18744383614 scopus 로고    scopus 로고
    • Matrilysin shedding of syndecan-1 regulates chemokine mobilization and transepithelial efflux of neutrophils in acute lung injury
    • DOI 10.1016/S0092-8674(02)01079-6
    • 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, 635-646. (Pubitemid 35441246)
    • (2002) Cell , vol.111 , Issue.5 , pp. 635-646
    • Li, Q.1    Park, P.W.2    Wilson, C.L.3    Parks, W.C.4
  • 32
    • 0034680919 scopus 로고    scopus 로고
    • Dm1-MMP, a matrix metalloproteinase from Drosophila with a potential role in extracellular matrix remodeling during neural development
    • Llano E, Pendas AM, Aza-Blanc P, Kornberg TB, Lopez-Otin C (2000). Dm1-MMP, a matrix metalloproteinase from Drosophila with a potential role in extracellular matrix remodeling during neural development. J Biol Chem 275, 35978-35985.
    • (2000) J Biol Chem , vol.275 , pp. 35978-35985
    • Llano, E.1    Pendas, A.M.2    Aza-Blanc, P.3    Kornberg, T.B.4    Lopez-Otin, C.5
  • 33
    • 0000480639 scopus 로고
    • Development and patterning of the larval epidermis of Drosophila
    • Martinez Arias A (1993). Plainview, NY: Cold Spring Harbor Laboratory Press
    • Martinez Arias A (1993). Bate M, Martinez Arias A (1993). Development and patterning of the larval epidermis of Drosophila. The Development of Drosophila melanogaster 1, Plainview, NY: Cold Spring Harbor Laboratory Press, 517-608.
    • (1993) The Development of Drosophila Melanogaster , vol.1 , pp. 517-608
    • Martinez Arias, A.1    Bate, M.2
  • 34
    • 1942540793 scopus 로고    scopus 로고
    • ERK Activation Propagates in Epithelial Cell Sheets and Regulates Their Migration during Wound Healing
    • DOI 10.1016/j.cub.2004.03.060, PII S0960982204002532
    • Matsubayashi Y, Ebisuya M, Honjoh S, Nishida E (2004). ERK activation propagates in epithelial cell sheets and regulates their migration during wound healing. Curr Biol 14, 731-735. (Pubitemid 38503612)
    • (2004) Current Biology , vol.14 , Issue.8 , pp. 731-735
    • Matsubayashi, Y.1    Ebisuya, M.2    Honjoh, S.3    Nishida, E.4
  • 36
    • 69949156933 scopus 로고    scopus 로고
    • The shape of motile cells
    • Mogilner A, Keren K (2009). The shape of motile cells. Curr Biol 19, R762-R771.
    • (2009) Curr Biol , vol.19
    • Mogilner, A.1    Keren, K.2
  • 38
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • DOI 10.1016/j.ceb.2004.07.010, PII S0955067404001097
    • Mott JD, Werb Z (2004). Regulation of matrix biology by matrix metalloproteinases. Curr Opin Cell Biol 16, 558-564. (Pubitemid 39201241)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.5 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 39
    • 0028934970 scopus 로고
    • Changing distributions of extracellular matrix components during early wing morphogenesis in Drosophila
    • Murray MJ, Fessler LI, Palka J (1995). Changing distributions of extracellular matrix components during early wing morphogenesis in Drosophila. Dev Biol 168, 150-165.
    • (1995) Dev Biol , vol.168 , pp. 150-165
    • Murray, M.J.1    Fessler, L.I.2    Palka, J.3
  • 40
    • 0031983514 scopus 로고    scopus 로고
    • JNK signaling and morphogenesis in Drosophila
    • Noselli S (1998). JNK signaling and morphogenesis in Drosophila. Trends Genet 14, 33-38.
    • (1998) Trends Genet , vol.14 , pp. 33-38
    • Noselli, S.1
  • 41
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A, Ewald AJ, Werb Z (2007). Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 8, 221-233.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 42
    • 0037239819 scopus 로고    scopus 로고
    • Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development
    • DOI 10.1016/S1534-5807(02)00400-8, PII S1534580702004008
    • Page-McCaw A, Serano J, Sante JM, Rubin GM (2003). Drosophila matrix metalloproteinases are required for tissue remodeling, but not embryonic development. Dev Cell 4, 95-106. (Pubitemid 36105336)
    • (2003) Developmental Cell , vol.4 , Issue.1 , pp. 95-106
    • Page-McCaw, A.1    Serano, J.2    Sante, J.M.3    Rubin, G.M.4
  • 44
    • 3543134126 scopus 로고    scopus 로고
    • Matrix metalloproteinases as modulators of inflammation and innate immunity
    • Parks WC, Wilson CL, Lopez-Boado YS (2004). Matrix metalloproteinases as modulators of inflammation and innate immunity. Nat Rev Immunol 4, 617-629. (Pubitemid 39025047)
    • (2004) Nature Reviews Immunology , vol.4 , Issue.8 , pp. 617-629
    • Parks, W.C.1    Wilson, C.L.2    Lopez-Boado, Y.S.3
  • 45
    • 79961238713 scopus 로고    scopus 로고
    • Shaping cells and organs in Drosophila by opposing roles of fat body-secreted collagen iv and perlecan
    • Pastor-Pareja JC, Xu T (2011). Shaping cells and organs in Drosophila by opposing roles of fat body-secreted collagen iv and perlecan. Dev Cell 21, 245-256.
    • (2011) Dev Cell , vol.21 , pp. 245-256
    • Pastor-Pareja, J.C.1    Xu, T.2
  • 46
    • 0036149337 scopus 로고    scopus 로고
    • JNK signaling pathway is required for efficient wound healing in Drosophila
    • DOI 10.1006/dbio.2001.0502
    • Ramet M, Lanot R, Zachary D, Manfruelli P (2002). JNK signaling pathway is required for efficient wound healing in Drosophila. Dev Biol 241, 145-156. (Pubitemid 34066768)
    • (2002) Developmental Biology , vol.241 , Issue.1 , pp. 145-156
    • Ramet, M.1    Lanot, R.2    Zachary, D.3    Manfruelli, P.4
  • 48
    • 62449175839 scopus 로고    scopus 로고
    • Interactions between extracellular matrix and growth factors in wound healing
    • Schultz GS, Wysocki A (2009). Interactions between extracellular matrix and growth factors in wound healing. Wound Repair Regen 17, 153-162.
    • (2009) Wound Repair Regen , vol.17 , pp. 153-162
    • Schultz, G.S.1    Wysocki, A.2
  • 49
    • 70350376721 scopus 로고    scopus 로고
    • Wound repair at a glance
    • Shaw TJ, Martin P (2009). Wound repair at a glance. J Cell Sci 122, 3209-3213.
    • (2009) J Cell Sci , vol.122 , pp. 3209-3213
    • Shaw, T.J.1    Martin, P.2
  • 51
    • 0025874499 scopus 로고
    • The regulation of the cell cycle during Drosophila embryogenesis: The transition to polyteny
    • Smith AV, Orr-Weaver TL (1991). The regulation of the cell cycle during Drosophila embryogenesis: the transition to polyteny. Development 112, 997-1008. (Pubitemid 21900301)
    • (1991) Development , vol.112 , Issue.4 , pp. 997-1008
    • Smith, A.V.1    Orr-Weaver, T.L.2
  • 53
    • 0031467314 scopus 로고    scopus 로고
    • Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site
    • DOI 10.1074/jbc.272.50.31730
    • Suzuki M, Raab G, Moses MA, Fernandez CA, Klagsbrun M (1997). Matrix metalloproteinase-3 releases active heparin-binding EGF-like growth factor by cleavage at a specific juxtamembrane site. J Biol Chem 272, 31730-31737. (Pubitemid 28013322)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.50 , pp. 31730-31737
    • Suzuki, M.1    Raab, G.2    Moses, M.A.3    Fernandez, C.A.4    Klagsbrun, M.5
  • 55
    • 33751111927 scopus 로고    scopus 로고
    • JNK- and Fos-regulated Mmp1 expression cooperates with Ras to induce invasive tumors in Drosophila
    • DOI 10.1038/sj.emboj.7601401, PII 7601401
    • Uhlirova M, Bohmann D (2006). JNK- and Fos-regulated Mmp1 expression cooperates with Ras to induce invasive tumors in Drosophila. EMBO J 25, 5294-5304. (Pubitemid 44764139)
    • (2006) EMBO Journal , vol.25 , Issue.22 , pp. 5294-5304
    • Uhlirova, M.1    Bohmann, D.2
  • 57
    • 0033052254 scopus 로고    scopus 로고
    • Actin dynamics in lamellipodia of migrating border cells in the Drosophila ovary revealed by a GFP-actin fusion protein
    • DOI 10.1016/S0014-5793(99)00124-6, PII S0014579399001246
    • Verkhusha VV, Tsukita S, Oda H (1999). Actin dynamics in lamellipodia of migrating border cells in the Drosophila ovary revealed by a GFP-actin fusion protein. FEBS Lett 445, 395-401. (Pubitemid 29117251)
    • (1999) FEBS Letters , vol.445 , Issue.2-3 , pp. 395-401
    • Verkhusha, V.V.1    Tsukita, S.2    Oda, H.3
  • 58
    • 0142095071 scopus 로고    scopus 로고
    • Drosophila TIMP Is a Potent Inhibitor of MMPs and TACE: Similarities in Structure and Function to TIMP-3
    • DOI 10.1021/bi035358x
    • Wei S, Xie Z, Filenova E, Brew K (2003). Drosophila TIMP is a potent inhibitor of MMPs and TACE: similarities in structure and function to TIMP-3. Biochemistry 42, 12200-12207. (Pubitemid 37296496)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12200-12207
    • Wei, S.1    Xie, Z.2    Filenova, E.3    Brew, K.4
  • 60
    • 69949142002 scopus 로고    scopus 로고
    • A bloodborne PDGF/VEGF-like ligand initiates wound-induced epidermal cell migration in Drosophila larvae
    • Wu Y, Brock AR, Wang Y, Fujitani K, Ueda R, Galko MJ (2009). A bloodborne PDGF/VEGF-like ligand initiates wound-induced epidermal cell migration in Drosophila larvae. Curr Biol 19, 1473-1477.
    • (2009) Curr Biol , vol.19 , pp. 1473-1477
    • Wu, Y.1    Brock, A.R.2    Wang, Y.3    Fujitani, K.4    Ueda, R.5    Galko, M.J.6
  • 61
    • 0030720096 scopus 로고    scopus 로고
    • Viking: Identification and characterization of a second type IV collagen in Drosophila
    • Yasothornsrikul S, Davis WJ, Cramer G, Kimbrell DA, Dearolf CR (1997). viking: identification and characterization of a second type IV collagen in Drosophila. Gene 198, 17-25.
    • (1997) Gene , vol.198 , pp. 17-25
    • Yasothornsrikul, S.1    Davis, W.J.2    Cramer, G.3    Kimbrell, D.A.4    Dearolf, C.R.5
  • 62
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q, Stamenkovic I (2000). Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev 14, 163-176. (Pubitemid 30070982)
    • (2000) Genes and Development , vol.14 , Issue.2 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 63
    • 33746062418 scopus 로고    scopus 로고
    • An MMP liberates the Ninjurin A ectodomain to signal a loss of cell adhesion
    • DOI 10.1101/gad.1426906
    • Zhang S, Dailey GM, Kwan E, Glasheen BM, Sroga GE, Page-McCaw A (2006). An MMP liberates the Ninjurin A ectodomain to signal a loss of cell adhesion. Genes Dev 20, 1899-1910. (Pubitemid 44079327)
    • (2006) Genes and Development , vol.20 , Issue.14 , pp. 1899-1910
    • Zhang, S.1    Dailey, G.M.2    Kwan, E.3    Glasheen, B.M.4    Sroga, G.E.5    Page-McCaw, A.6
  • 64
    • 49649101876 scopus 로고    scopus 로고
    • In vivo interstitial migration of primitive macrophages mediated by JNK-matrix metalloproteinase 13 signaling in response to acute injury
    • Zhang Y et al. (2008). In vivo interstitial migration of primitive macrophages mediated by JNK-matrix metalloproteinase 13 signaling in response to acute injury. J Immunol 181, 2155-2164.
    • (2008) J Immunol , vol.181 , pp. 2155-2164
    • Zhang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.