메뉴 건너뛰기




Volumn 34, Issue 8, 2014, Pages 1500-1511

ANKRD1 acts as a transcriptional repressor of MMP13 via the AP-1 site

Author keywords

[No Author keywords available]

Indexed keywords

ANKRD1 PROTEIN; COLLAGENASE 3; CYCLOPHILIN B; MESSENGER RNA; NUCLEAR PROTEIN; NUCLEOLIN; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN C JUN; SMALL INTERFERING RNA; STROMELYSIN 2; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1; UNCLASSIFIED DRUG; ANKRD1 PROTEIN, MOUSE; MMP13 PROTEIN, MOUSE; MUSCLE PROTEIN; PHOSPHOPROTEIN; REPRESSOR PROTEIN; RNA BINDING PROTEIN;

EID: 84896498196     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01357-13     Document Type: Article
Times cited : (34)

References (51)
  • 1
    • 9444234506 scopus 로고    scopus 로고
    • Tissue repair and the dynamics of the extracellular matrix
    • Midwood KS, Williams LV, Schwarzbauer JE. 2004. Tissue repair and the dynamics of the extracellular matrix. Int. J. Biochem. Cell Biol. 36: 1031-1037. http://dx.doi.org/10.1016/j.biocel.2003.12.003.
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 1031-1037
    • Midwood, K.S.1    Williams, L.V.2    Schwarzbauer, J.E.3
  • 2
    • 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. http://dx.doi.org/10.1111/j.1524-475X.2009.00466.x.
    • (2009) Wound Repair Regen. , vol.17 , pp. 153-162
    • Schultz, G.S.1    Wysocki, A.2
  • 4
    • 11144248394 scopus 로고    scopus 로고
    • CARP, a cardiac ankyrin repeat protein, is upregulated during wound healing and induces angiogenesis in experimental granulation tissue
    • Shi Y, Reitmaier B, Regenbogen J, Slowey RM, Opalenik SR, Wolf E, Goppelt A, Davidson JM. 2005. CARP, a cardiac ankyrin repeat protein, is upregulated during wound healing and induces angiogenesis in experimental granulation tissue. Am. J. Pathol. 166:303-312. http://dx.doi.org/10.1016/S0002-9440(10)62254-7.
    • (2005) Am. J. Pathol. , vol.166 , pp. 303-312
    • Shi, Y.1    Reitmaier, B.2    Regenbogen, J.3    Slowey, R.M.4    Opalenik, S.R.5    Wolf, E.6    Goppelt, A.7    Davidson, J.M.8
  • 5
    • 33748785438 scopus 로고    scopus 로고
    • CARP: fishing for novel mechanisms of neovascularization
    • Samaras SE, Shi Y, Davidson JM. 2006. CARP: fishing for novel mechanisms of neovascularization. J. Invest. Dermatol. Symp. Proc. 11:124-131. http://dx.doi.org/10.1038/sj.jidsymp.5650014.
    • (2006) J. Invest. Dermatol. Symp. Proc. , vol.11 , pp. 124-131
    • Samaras, S.E.1    Shi, Y.2    Davidson, J.M.3
  • 6
    • 0028944298 scopus 로고
    • Identification and characterization of a novel cytokine-inducible nuclear protein from human endothelial cells
    • Chu W, Burns DK, Swerlick RA, Presky DH. 1995. Identification and characterization of a novel cytokine-inducible nuclear protein from human endothelial cells. J. Biol. Chem. 270:10236-10245. http://dx.doi.org/10.1074/jbc.270.17.10236.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10236-10245
    • Chu, W.1    Burns, D.K.2    Swerlick, R.A.3    Presky, D.H.4
  • 7
    • 0030931797 scopus 로고    scopus 로고
    • A novel cardiac-restricted target for doxorubicin. CARP, a nuclear modulator of gene expression in cardiac progenitor cells and cardiomyocytes.
    • Jeyaseelan R, Poizat C, Baker RK, Abdishoo S, Isterabadi LB, Lyons GE, Kedes L. 1997. A novel cardiac-restricted target for doxorubicin. CARP, a nuclear modulator of gene expression in cardiac progenitor cells and cardiomyocytes. J. Biol. Chem. 272:22800-22808.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22800-22808
    • Jeyaseelan, R.1    Poizat, C.2    Baker, R.K.3    Abdishoo, S.4    Isterabadi, L.B.5    Lyons, G.E.6    Kedes, L.7
  • 9
    • 33745700311 scopus 로고    scopus 로고
    • The cardiac ankyrin repeat domain 1 protein: do you know enough about its dimerization properties?
    • author reply 251-252
    • Mikhailov AT, Torrado M. 2006. The cardiac ankyrin repeat domain 1 protein: do you know enough about its dimerization properties? J. Muscle Res. Cell Motil. 27:203-204; author reply, 251-252. http://dx.doi.org/10.1007/s10974-006-9061-x.
    • (2006) J. Muscle Res. Cell Motil. , vol.27 , pp. 203-204
    • Mikhailov, A.T.1    Torrado, M.2
  • 10
    • 0031029447 scopus 로고    scopus 로고
    • CARP, a cardiac ankyrin repeat protein, is downstream in the Nkx2-5 homeobox gene pathway
    • Zou Y, Evans S, Chen J, Kuo HC, Harvey RP, Chien KR. 1997. CARP, a cardiac ankyrin repeat protein, is downstream in the Nkx2-5 homeobox gene pathway. Development 124:793-804.
    • (1997) Development , vol.124 , pp. 793-804
    • Zou, Y.1    Evans, S.2    Chen, J.3    Kuo, H.C.4    Harvey, R.P.5    Chien, K.R.6
  • 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. http://dx.doi.org/10.1016/j.biocel.2007.10.024.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1334-1347
    • Gill, S.E.1    Parks, W.C.2
  • 12
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing: aiming for perfect skin regeneration
    • Martin P. 1997. Wound healing: aiming for perfect skin regeneration. Science 276:75-81. http://dx.doi.org/10.1126/science.276.5309.75.
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 13
    • 0034297101 scopus 로고    scopus 로고
    • Matrix metalloproteinases in wound repair (review)
    • Ravanti L, Kahari VM. 2000. Matrix metalloproteinases in wound repair (review). Int. J. Mol. Med. 6:391-407.
    • (2000) Int. J. Mol. Med. , vol.6 , pp. 391-407
    • Ravanti, L.1    Kahari, V.M.2
  • 14
    • 0036358207 scopus 로고    scopus 로고
    • The role of matrix metalloproteinases in wound healing
    • Armstrong DG, Jude EB. 2002. The role of matrix metalloproteinases in wound healing. J. Am. Podiatr. Med. Assoc. 92:12-18.
    • (2002) J. Am. Podiatr. Med. Assoc. , vol.92 , pp. 12-18
    • Armstrong, D.G.1    Jude, E.B.2
  • 15
    • 0032815514 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases and their inhibition in cutaneous wound healing and allergic contact hypersensitivity
    • Pilcher BK, Wang M, Qin XJ, Parks WC, Senior RM, Welgus HG. 1999. Role of matrix metalloproteinases and their inhibition in cutaneous wound healing and allergic contact hypersensitivity. Ann. N. Y. Acad. Sci. 878:12-24. http://dx.doi.org/10.1111/j.1749-6632.1999.tb07671.x.
    • (1999) Ann. N. Y. Acad. Sci. , vol.878 , pp. 12-24
    • Pilcher, B.K.1    Wang, M.2    Qin, X.J.3    Parks, W.C.4    Senior, R.M.5    Welgus, H.G.6
  • 17
    • 0031816247 scopus 로고    scopus 로고
    • Collagenase-3 induction in rat lung fibroblasts requires the combined effects of tumor necrosis factor-alpha and 12-lipoxygenase metabolites: a model of macrophage- induced, fibroblast-driven extracellular matrix remodeling during inflammatory lung injury
    • Mariani TJ, Sandefur S, Roby JD, Pierce RA. 1998. Collagenase-3 induction in rat lung fibroblasts requires the combined effects of tumor necrosis factor-alpha and 12-lipoxygenase metabolites: a model of macrophage- induced, fibroblast-driven extracellular matrix remodeling during inflammatory lung injury. Mol. Biol. Cell 9:1411-1424. http://dx.doi.org/10.1091/mbc.9.6.1411.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1411-1424
    • Mariani, T.J.1    Sandefur, S.2    Roby, J.D.3    Pierce, R.A.4
  • 18
    • 0036167349 scopus 로고    scopus 로고
    • Real-time visualization of MMP-13 promoter activity in transgenic mice
    • Wu N, Opalenik S, Liu J, Jansen ED, Giro MG, Davidson JM. 2002. Real-time visualization of MMP-13 promoter activity in transgenic mice. Matrix Biol. 21:149-161. http://dx.doi.org/10.1016/S0945-053X(01)00 192-5.
    • (2002) Matrix Biol. , vol.21 , pp. 149-161
    • Wu, N.1    Opalenik, S.2    Liu, J.3    Jansen, E.D.4    Giro, M.G.5    Davidson, J.M.6
  • 19
    • 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. http://dx.doi.org/10.2353/ajpath.2009.081080.
    • (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
  • 20
    • 84864683850 scopus 로고    scopus 로고
    • MMP-13 regulates growth of wound granulation tissue and modulates gene expression signatures involved in inflammation, proteolysis, and cell viability
    • Toriseva M, Laato M, Carpen O, Ruohonen ST, Savontaus E, Inada M, Krane SM, Kahari VM. 2012. MMP-13 regulates growth of wound granulation tissue and modulates gene expression signatures involved in inflammation, proteolysis, and cell viability. PLoS One 7:e42596. http://dx.doi.org/10.1371/journal.pone.0042596.
    • (2012) PLoS One , vol.7
    • Toriseva, M.1    Laato, M.2    Carpen, O.3    Ruohonen, S.T.4    Savontaus, E.5    Inada, M.6    Krane, S.M.7    Kahari, V.M.8
  • 21
    • 0029009988 scopus 로고
    • A method for the isolation and serial propagation of keratinocytes, endothelial cells, and fibroblasts from a single punch biopsy of human skin
    • Normand J, Karasek MA. 1995. A method for the isolation and serial propagation of keratinocytes, endothelial cells, and fibroblasts from a single punch biopsy of human skin. In Vitro Cell Dev. Biol. Anim. 31:447-455. http://dx.doi.org/10.1007/BF02634257.
    • (1995) In Vitro Cell Dev. Biol. Anim. , vol.31 , pp. 447-455
    • Normand, J.1    Karasek, M.A.2
  • 22
    • 0022398671 scopus 로고
    • Differential requirement for SV40 early genes in immortalization and transformation of primary rat and human embryonic cells
    • Chang LS, Pan S, Pater MM, Di Mayorca G. 1985. Differential requirement for SV40 early genes in immortalization and transformation of primary rat and human embryonic cells. Virology 146:246-261. http://dx.doi.org/10.1016/0042-6822(85)90008-X.
    • (1985) Virology , vol.146 , pp. 246-261
    • Chang, L.S.1    Pan, S.2    Pater, M.M.3    Di Mayorca, G.4
  • 23
    • 0035545304 scopus 로고    scopus 로고
    • Isolation of vascular smooth muscle cells from a single murine aorta
    • Ray JL, Leach R, Herbert JM, Benson M. 2001. Isolation of vascular smooth muscle cells from a single murine aorta. Methods Cell Sci. 23:185-188. http://dx.doi.org/10.1023/A:1016357510143.
    • (2001) Methods Cell Sci. , vol.23 , pp. 185-188
    • Ray, J.L.1    Leach, R.2    Herbert, J.M.3    Benson, M.4
  • 24
    • 0028322344 scopus 로고
    • Characterization of expression and modulation of cell adhesion molecules on an immortalized human dermal microvascular endothelial cell line (HMEC-1)
    • Xu Y, Swerlick RA, Sepp N, Bosse D, Ades EW, Lawley TJ. 1994. Characterization of expression and modulation of cell adhesion molecules on an immortalized human dermal microvascular endothelial cell line (HMEC-1). J. Invest. Dermatol. 102:833-837. http://dx.doi.org/10.1111/1523-1747.ep12382086.
    • (1994) J. Invest. Dermatol. , vol.102 , pp. 833-837
    • Xu, Y.1    Swerlick, R.A.2    Sepp, N.3    Bosse, D.4    Ades, E.W.5    Lawley, T.J.6
  • 25
    • 84896539397 scopus 로고    scopus 로고
    • Splinting strategies to overcome confounding wound contraction in experimental animal models
    • Davidson JM, Yu F, Opalenik SR. 2013. Splinting strategies to overcome confounding wound contraction in experimental animal models. Advances Wound Care 2:142-148. http://dx.doi.org/10.1089/wound.2012.0424.
    • (2013) Advances Wound Care , vol.2 , pp. 142-148
    • Davidson, J.M.1    Yu, F.2    Opalenik, S.R.3
  • 26
  • 28
    • 38349050125 scopus 로고    scopus 로고
    • Nucleolin binds specifically to an AP-1 DNA sequence and represses AP1-dependent transactivation of the matrix metalloproteinase-13 gene
    • Samuel S, Twizere JC, Beifuss KK, Bernstein LR. 2008. Nucleolin binds specifically to an AP-1 DNA sequence and represses AP1-dependent transactivation of the matrix metalloproteinase-13 gene. Mol. Carcinog. 47:34-46. http://dx.doi.org/10.1002/mc.20358.
    • (2008) Mol. Carcinog. , vol.47 , pp. 34-46
    • Samuel, S.1    Twizere, J.C.2    Beifuss, K.K.3    Bernstein, L.R.4
  • 29
    • 0034640232 scopus 로고    scopus 로고
    • Allele-specific regulation of matrix metalloproteinase-12 gene activity is associated with coronary artery luminal dimensions in diabetic patients with manifest coronary artery disease
    • Jormsjo S, Ye S, Moritz J, Walter DH, Dimmeler S, Zeiher AM, Henney A, Hamsten A, Eriksson P. 2000. Allele-specific regulation of matrix metalloproteinase-12 gene activity is associated with coronary artery luminal dimensions in diabetic patients with manifest coronary artery disease. Circ. Res. 86:998-1003. http://dx.doi.org/10.1161/01.RES.86.9.998.
    • (2000) Circ. Res. , vol.86 , pp. 998-1003
    • Jormsjo, S.1    Ye, S.2    Moritz, J.3    Walter, D.H.4    Dimmeler, S.5    Zeiher, A.M.6    Henney, A.7    Hamsten, A.8    Eriksson, P.9
  • 30
    • 84864700656 scopus 로고    scopus 로고
    • AP-1-mediated transcriptional repression of matrix metalloproteinase-9 by recruitment of histone deacetylase 1 in response to interferon beta
    • Mittelstadt ML, Patel RC. 2012. AP-1-mediated transcriptional repression of matrix metalloproteinase-9 by recruitment of histone deacetylase 1 in response to interferon beta. PLoS One 7:e42152. http://dx.doi.org/10.1371/journal.pone.0042152.
    • (2012) PLoS One , vol.7
    • Mittelstadt, M.L.1    Patel, R.C.2
  • 31
    • 0033851463 scopus 로고    scopus 로고
    • Interleukin-1 induction of collagenase 3 (matrix metalloproteinase 13) gene expression in chondrocytes requires p38, c-Jun N-terminal kinase, and nuclear factor κB: differential regulation of collagenase 1 and collagenase 3
    • <801::AID-ANR10>3.0.CO;2-4
    • Mengshol JA, Vincenti MP, Coon CI, Barchowsky A, BrinckerhoffCE. 2000. Interleukin-1 induction of collagenase 3 (matrix metalloproteinase 13) gene expression in chondrocytes requires p38, c-Jun N-terminal kinase, and nuclear factor κB: differential regulation of collagenase 1 and collagenase 3. Arthritis Rheumatism 43:801-811. http://dx.doi.org/10.1002/1529-0131(200004)43:4<801::AID-ANR10>3.0.CO;2-4.
    • (2000) Arthritis Rheumatism , vol.43 , pp. 801-811
    • Mengshol, J.A.1    Vincenti, M.P.2    Coon, C.I.3    Barchowsky, A.4    Brinckerhoff, C.E.5
  • 32
    • 79955021485 scopus 로고    scopus 로고
    • AP-1 as a regulator ofMMP-13in the stromal cell of giant cell tumor of bone
    • Mak IW, Turcotte RE, Popovic S, Singh G, Ghert M. 2011. AP-1 as a regulator ofMMP-13in the stromal cell of giant cell tumor of bone. Biochem. Res. Int. 2011:164-197. http://dx.doi.org/10.1155/2011/164197.
    • (2011) Biochem. Res. Int. , vol.2011 , pp. 164-197
    • Mak, I.W.1    Turcotte, R.E.2    Popovic, S.3    Singh, G.4    Ghert, M.5
  • 33
    • 0036240838 scopus 로고    scopus 로고
    • Transcriptional regulation of collagenase (MMP-1, MMP-13) genes in arthritis: integration of complex signaling pathways for the recruitment of gene-specific transcription factors
    • Vincenti MP, BrinckerhoffCE. 2002. Transcriptional regulation of collagenase (MMP-1, MMP-13) genes in arthritis: integration of complex signaling pathways for the recruitment of gene-specific transcription factors. Arthritis Res. 4:157-164. http://dx.doi.org/10.1186/ar401.
    • (2002) Arthritis Res. , vol.4 , pp. 157-164
    • Vincenti, M.P.1    Brinckerhoff, C.E.2
  • 35
    • 0030740249 scopus 로고    scopus 로고
    • Distinct populations of stromal cells express collagenase-3 (MMP-13) and collagenase-1 (MMP-1) in chronic ulcers but not in normally healing wounds
    • Vaalamo M, Mattila L, Johansson N, Kariniemi AL, Karjalainen-Lindsberg ML, Kahari VM, Saarialho-Kere U. 1997. Distinct populations of stromal cells express collagenase-3 (MMP-13) and collagenase-1 (MMP-1) in chronic ulcers but not in normally healing wounds. J. Invest. Dermatol. 109:96-101. http://dx.doi.org/10.1111/1523-1747.ep12276722.
    • (1997) J. Invest. Dermatol. , vol.109 , pp. 96-101
    • Vaalamo, M.1    Mattila, L.2    Johansson, N.3    Kariniemi, A.L.4    Karjalainen-Lindsberg, M.L.5    Kahari, V.M.6    Saarialho-Kere, U.7
  • 36
    • 0033593335 scopus 로고    scopus 로고
    • Induction of collagenase-3 (MMP-13) expression in human skin fibroblasts by threedimensional collagen is mediated by p38 mitogen-activated protein kinase
    • Ravanti L, Heino J, Lopez-Otin C, Kahari VM. 1999. Induction of collagenase-3 (MMP-13) expression in human skin fibroblasts by threedimensional collagen is mediated by p38 mitogen-activated protein kinase. J. Biol. Chem. 274:2446-2455. http://dx.doi.org/10.1074/jbc.274.4.2446.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2446-2455
    • Ravanti, L.1    Heino, J.2    Lopez-Otin, C.3    Kahari, V.M.4
  • 37
    • 0035318547 scopus 로고    scopus 로고
    • Expression of human collagenase-3 (MMP-13) by fetal skin fibroblasts is induced by transforming growth factor beta via p38 mitogen-activated protein kinase
    • Ravanti L, Toriseva M, Penttinen R, Crombleholme T, Foschi M, Han J, Kahari VM. 2001. Expression of human collagenase-3 (MMP-13) by fetal skin fibroblasts is induced by transforming growth factor beta via p38 mitogen-activated protein kinase. FASEB J. 15:1098-1100. http://dx.doi.org/10.1096/fj.00-0588fje.
    • (2001) FASEB J. , vol.15 , pp. 1098-1100
    • Ravanti, L.1    Toriseva, M.2    Penttinen, R.3    Crombleholme, T.4    Foschi, M.5    Han, J.6    Kahari, V.M.7
  • 38
    • 85047691853 scopus 로고    scopus 로고
    • Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation
    • Balbin M, Fueyo A, Knauper V, Lopez JM, Alvarez J, Sanchez LM, Quesada V, Bordallo J, Murphy G, Lopez-Otin C. 2001. Identification and enzymatic characterization of two diverging murine counterparts of human interstitial collagenase (MMP-1) expressed at sites of embryo implantation. J. Biol. Chem. 276:10253-10262. http://dx.doi.org/10.1074/jbc. M009586200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10253-10262
    • Balbin, M.1    Fueyo, A.2    Knauper, V.3    Lopez, J.M.4    Alvarez, J.5    Sanchez, L.M.6    Quesada, V.7    Bordallo, J.8    Murphy, G.9    Lopez-Otin, C.10
  • 39
    • 33645023987 scopus 로고    scopus 로고
    • Increase of MMP-13 expression in multi-stage oral carcinogenesis and epigallocatechin- 3-gallate suppress MMP-13 expression
    • Chiang WC, Wong YK, Lin SC, Chang KW, Liu CJ. 2006. Increase of MMP-13 expression in multi-stage oral carcinogenesis and epigallocatechin- 3-gallate suppress MMP-13 expression. Oral Dis. 12:27-33. http://dx.doi.org/10.1111/j.1601-0825.2005.01151.x.
    • (2006) Oral Dis. , vol.12 , pp. 27-33
    • Chiang, W.C.1    Wong, Y.K.2    Lin, S.C.3    Chang, K.W.4    Liu, C.J.5
  • 41
    • 84862956461 scopus 로고    scopus 로고
    • Dissection of Wnt5a-Ror2 signaling leading to matrix metalloproteinase (MMP-13) expression
    • Yamagata K, Li X, Ikegaki S, Oneyama C, Okada M, Nishita M, Minami Y. 2012. Dissection of Wnt5a-Ror2 signaling leading to matrix metalloproteinase (MMP-13) expression. J. Biol. Chem. 287:1588-1599. http://dx.doi.org/10.1074/jbc. M111.315127.
    • (2012) J. Biol. Chem. , vol.287 , pp. 1588-1599
    • Yamagata, K.1    Li, X.2    Ikegaki, S.3    Oneyama, C.4    Okada, M.5    Nishita, M.6    Minami, Y.7
  • 42
    • 46249097446 scopus 로고    scopus 로고
    • Is collagenase-3 (MMP-13) expression in chondrosarcoma of the jaws a true marker for tumor aggressiveness?
    • Zyada MM, Shamaa AA. 2008. Is collagenase-3 (MMP-13) expression in chondrosarcoma of the jaws a true marker for tumor aggressiveness? Diagn. Pathol. 3:26. http://dx.doi.org/10.1186/1746-1596-3-26.
    • (2008) Diagn. Pathol. , vol.3 , pp. 26
    • Zyada, M.M.1    Shamaa, A.A.2
  • 44
    • 32944465075 scopus 로고    scopus 로고
    • Matrix metalloproteinases: role in arthritis
    • Burrage PS, Mix KS, BrinckerhoffCE. 2006. Matrix metalloproteinases: role in arthritis. Front. Biosci. 11:529-543. http://dx.doi.org/10.2741/1817.
    • (2006) Front. Biosci. , vol.11 , pp. 529-543
    • Burrage, P.S.1    Mix, K.S.2    Brinckerhoff, C.E.3
  • 45
    • 18644375615 scopus 로고    scopus 로고
    • Increased AP-1 and NF-kB activation and recruitment with the combination of the proinflammatory cytokines IL-β1, tumor necrosis factor α and IL-β17 in rheumatoid synoviocytes
    • Granet C, Maslinski W, Miossec P. 2004. Increased AP-1 and NF-kB activation and recruitment with the combination of the proinflammatory cytokines IL-β1, tumor necrosis factor α and IL-β17 in rheumatoid synoviocytes. Arthritis Res. Ther. 6:R190-R198. http://dx.doi.org/10.1186/ar1159.
    • (2004) Arthritis Res. Ther. , vol.6
    • Granet, C.1    Maslinski, W.2    Miossec, P.3
  • 46
    • 84859970435 scopus 로고    scopus 로고
    • Disruption of a GATA4/Ankrd1 signaling axis in cardiomyocytes leads to sarcomere disarray: implications for anthracycline cardiomyopathy
    • Chen B, Zhong L, Roush SF, Pentassuglia L, Peng X, Samaras S, Davidson JM, Sawyer DB, Lim CC. 2012. Disruption of a GATA4/Ankrd1 signaling axis in cardiomyocytes leads to sarcomere disarray: implications for anthracycline cardiomyopathy. PLoS One 7:e35743. http://dx.doi.org/10.1371/journal.pone.0035743.
    • (2012) PLoS One , vol.7
    • Chen, B.1    Zhong, L.2    Roush, S.F.3    Pentassuglia, L.4    Peng, X.5    Samaras, S.6    Davidson, J.M.7    Sawyer, D.B.8    Lim, C.C.9
  • 47
    • 13444292268 scopus 로고    scopus 로고
    • ANKRD1 specifically binds CASQ2 in heart extracts and both proteins are co-enriched in piglet cardiac Purkinje cells
    • Torrado M, Nespereira B, Lopez E, Centeno A, Castro-Beiras A, Mikhailov AT. 2005. ANKRD1 specifically binds CASQ2 in heart extracts and both proteins are co-enriched in piglet cardiac Purkinje cells. J. Mol. Cell Cardiol. 38:353-365. http://dx.doi.org/10.1016/j.yjmcc.2004.11.034.
    • (2005) J. Mol. Cell Cardiol. , vol.38 , pp. 353-365
    • Torrado, M.1    Nespereira, B.2    Lopez, E.3    Centeno, A.4    Castro-Beiras, A.5    Mikhailov, A.T.6
  • 48
    • 38549139612 scopus 로고    scopus 로고
    • Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2
    • Witt CC, Witt SH, Lerche S, Labeit D, Back W, Labeit S. 2008. Cooperative control of striated muscle mass and metabolism by MuRF1 and MuRF2. EMBO J. 27:350-360. http://dx.doi.org/10.1038/sj.emboj.7601952.
    • (2008) EMBO J. , vol.27 , pp. 350-360
    • Witt, C.C.1    Witt, S.H.2    Lerche, S.3    Labeit, D.4    Back, W.5    Labeit, S.6
  • 49
    • 34548607098 scopus 로고    scopus 로고
    • YB-1 binds to the MMP-13 promoter sequence and represses MMP-13 transactivation via the AP-1 site
    • Samuel S, Beifuss KK, Bernstein LR. 2007. YB-1 binds to the MMP-13 promoter sequence and represses MMP-13 transactivation via the AP-1 site. Biochim. Biophys. Acta 1769:525-531. http://dx.doi.org/10.1016/j.bbaexp.2007.07.003.
    • (2007) Biochim. Biophys. Acta , vol.1769 , pp. 525-531
    • Samuel, S.1    Beifuss, K.K.2    Bernstein, L.R.3
  • 50
    • 0034657357 scopus 로고    scopus 로고
    • Nucleolin and YB-1 are required for JNKmediated interleukin-2 mRNA stabilization during T-cell activation
    • Chen CY, Gherzi R, Andersen JS, Gaietta G, Jurchott K, Royer HD, Mann M, Karin M. 2000. Nucleolin and YB-1 are required for JNKmediated interleukin-2 mRNA stabilization during T-cell activation. Genes Dev. 14:1236-1248. http://dx.doi.org/10.1101/gad.14.10.1236.
    • (2000) Genes Dev. , vol.14 , pp. 1236-1248
    • Chen, C.Y.1    Gherzi, R.2    Andersen, J.S.3    Gaietta, G.4    Jurchott, K.5    Royer, H.D.6    Mann, M.7    Karin, M.8
  • 51
    • 38349173105 scopus 로고    scopus 로고
    • Nucleolin regulates c-Jun/Sp1-dependent transcriptional activation of cPLA2α in phorbol ester-treated non-small cell lung cancer A549 cells
    • Tsou JH, Chang KY, Wang WC, Tseng JT, Su WC, Hung LY, Chang WC, Chen BK. 2008. Nucleolin regulates c-Jun/Sp1-dependent transcriptional activation of cPLA2α in phorbol ester-treated non-small cell lung cancer A549 cells. Nucleic Acids Res. 36:217-227. http://dx.doi.org/10.1093/nar/gkm1027.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 217-227
    • Tsou, J.H.1    Chang, K.Y.2    Wang, W.C.3    Tseng, J.T.4    Su, W.C.5    Hung, L.Y.6    Chang, W.C.7    Chen, B.K.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.