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Volumn 1, Issue 4, 2012, Pages 1313-1327

Cytoskeletal regulation of dermal regeneration

Author keywords

Cytoskeleton; Flightless I; Gelsolin; Repair; Skin regeneration

Indexed keywords

ARACHIDONATE 5 LIPOXYGENASE ACTIVATING PROTEIN; GELSOLIN; K RAS PROTEIN; PROTEIN CDC42; RAC PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; THYROID HORMONE; VILLIN; WNT PROTEIN;

EID: 84946831113     PISSN: None     EISSN: 20734409     Source Type: Journal    
DOI: 10.3390/cells1041313     Document Type: Review
Times cited : (9)

References (81)
  • 1
    • 79952768543 scopus 로고    scopus 로고
    • The influence of flightless i: Regeneration versus wound healing
    • Morasso, M.I. The influence of flightless i: Regeneration versus wound healing. J. Invest. Dermatol. 2011, 131, 816-817.
    • (2011) J. Invest. Dermatol. , vol.131 , pp. 816-817
    • Morasso, M.I.1
  • 2
    • 0141671441 scopus 로고    scopus 로고
    • Regeneration in the metazoans: Why does it happen?
    • Sanchez Alvarado, A. Regeneration in the metazoans: Why does it happen? Bioessays 2000, 22, 578-590.
    • (2000) Bioessays , vol.22 , pp. 578-590
    • Sanchez Alvarado, A.1
  • 3
    • 0017619384 scopus 로고
    • Tail autonomy, functional conflicts and their resolution by a salamander
    • Maiorana, V.C. Tail autonomy, functional conflicts and their resolution by a salamander. Nature 1977, 2265, 533-535.
    • (1977) Nature , vol.2265 , pp. 533-535
    • Maiorana, V.C.1
  • 4
    • 69549120779 scopus 로고
    • Regeneration of the distal phalanx
    • McKim, L.H. Regeneration of the distal phalanx. Can. Med. Assoc. J. 1932, 26, 549-550.
    • (1932) Can. Med. Assoc. J. , vol.26 , pp. 549-550
    • McKim, L.H.1
  • 5
    • 0021017776 scopus 로고
    • Treatment of fingertip amputations with bone exposure. A comparative study between surgical and conservative treatment methods
    • Soderberg, T.; Nystrom, A.; Hallmans, G.; Hulten, J., Treatment of fingertip amputations with bone exposure. A comparative study between surgical and conservative treatment methods. Scand. J. Plast. Reconstr. Surg. Suppl. 1983, 17, 147-152.
    • (1983) Scand. J. Plast. Reconstr. Surg. Suppl. , vol.17 , pp. 147-152
    • Soderberg, T.1    Nystrom, A.2    Hallmans, G.3    Hulten, J.4
  • 6
    • 84989051360 scopus 로고
    • Bone regrowth after digit tip amputation in mice is equivalent in adults and neonates
    • Neufeld, D.A.; Zhao, W. Bone regrowth after digit tip amputation in mice is equivalent in adults and neonates. Wound Repair Regen. 1995, 3, 461-466.
    • (1995) Wound Repair Regen. , vol.3 , pp. 461-466
    • Neufeld, D.A.1    Zhao, W.2
  • 7
    • 39249084246 scopus 로고    scopus 로고
    • Development and regeneration of the neonatal digit tip in mice
    • Han, M.; Yang, X.; Lee, J.; Allan, C.H.; Muneoka, K. Development and regeneration of the neonatal digit tip in mice. Dev. Biol. 2008, 315, 125-135.
    • (2008) Dev. Biol. , vol.315 , pp. 125-135
    • Han, M.1    Yang, X.2    Lee, J.3    Allan, C.H.4    Muneoka, K.5
  • 8
  • 10
    • 76449104643 scopus 로고    scopus 로고
    • Bmp signaling induces digit regeneration in neonatal mice
    • Yu, L.; Han, M.; Yan, M.; Lee, E.C.; Lee, J.; Muneoka, K. Bmp signaling induces digit regeneration in neonatal mice. Development 2010, 137, 551-559.
    • (2010) Development , vol.137 , pp. 551-559
    • Yu, L.1    Han, M.2    Yan, M.3    Lee, E.C.4    Lee, J.5    Muneoka, K.6
  • 13
    • 84855507663 scopus 로고    scopus 로고
    • Mouse digit tip regeneration is mediated by fate-restricted progenitor cells
    • Lehoczky, J.A.; Robert, B.; Tabin, C.J. Mouse digit tip regeneration is mediated by fate-restricted progenitor cells. Proc. Natl. Acad. Sci. USA 2011, 108, 20609-20614.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20609-20614
    • Lehoczky, J.A.1    Robert, B.2    Tabin, C.J.3
  • 14
    • 80052056733 scopus 로고    scopus 로고
    • Germ-layer and lineagerestricted stem/progenitors regenerate the mouse digit tip
    • Rinkevich, Y.; Lindau, P.; Ueno, H.; Longaker, M.T.; Weissman, I.L. Germ-layer and lineagerestricted stem/progenitors regenerate the mouse digit tip. Nature 2011, 476, 409-413.
    • (2011) Nature , vol.476 , pp. 409-413
    • Rinkevich, Y.1    Lindau, P.2    Ueno, H.3    Longaker, M.T.4    Weissman, I.L.5
  • 16
    • 0027469631 scopus 로고
    • Regeneration of the distal phalanx. A case report
    • Vidal, P.; Dickson, M.G. Regeneration of the distal phalanx. A case report. J. Hand. Surg. 1993, 18, 230-233.
    • (1993) J. Hand. Surg. , vol.18 , pp. 230-233
    • Vidal, P.1    Dickson, M.G.2
  • 18
  • 19
    • 0032567078 scopus 로고    scopus 로고
    • De novo hair follicle morphogenesis and hair tumors in mice expressing a truncated beta-catenin in skin
    • Gat, U.; DasGupta, R.; Degenstein, L.; Fuchs, E., De novo hair follicle morphogenesis and hair tumors in mice expressing a truncated beta-catenin in skin. Cell 1998, 95, 605-614.
    • (1998) Cell , vol.95 , pp. 605-614
    • Gat, U.1    DasGupta, R.2    Degenstein, L.3    Fuchs, E.4
  • 20
    • 33644679351 scopus 로고    scopus 로고
    • Wnt signaling induces epithelial differentiation during cutaneous wound healing
    • Fathke, C.; Wilson, L.; Shah, K.; Kim, B.; Hocking, A.; Moon, R.; Isik, F. Wnt signaling induces epithelial differentiation during cutaneous wound healing. BMC Cell Biol. 2006, 7, 4.
    • (2006) BMC Cell Biol. , vol.7 , pp. 4
    • Fathke, C.1    Wilson, L.2    Shah, K.3    Kim, B.4    Hocking, A.5    Moon, R.6    Isik, F.7
  • 23
    • 0035110953 scopus 로고    scopus 로고
    • Skin and oral fibroblasts exhibit phenotypic differences in extracellular matrix reorganization and matrix metalloproteinase activity
    • Stephens, P.; Davies, K.J.; Occleston, N.; Pleass, R.D.; Kon, C.; Daniels, J.; Khaw, P.T.; Thomas, D.W. Skin and oral fibroblasts exhibit phenotypic differences in extracellular matrix reorganization and matrix metalloproteinase activity. Br. J. Dermatol. 2001, 144, 229-237.
    • (2001) Br. J. Dermatol. , vol.144 , pp. 229-237
    • Stephens, P.1    Davies, K.J.2    Occleston, N.3    Pleass, R.D.4    Kon, C.5    Daniels, J.6    Khaw, P.T.7    Thomas, D.W.8
  • 25
    • 84969418194 scopus 로고    scopus 로고
    • Role of the actin cytoskeleton in wound healing and scar formation
    • Cowin, A. Role of the actin cytoskeleton in wound healing and scar formation. Primary Intention 2006, 14, 39-42.
    • (2006) Primary Intention , vol.14 , pp. 39-42
    • Cowin, A.1
  • 27
    • 0032559362 scopus 로고    scopus 로고
    • Rho gtpases and the actin cytoskeleton
    • Hall, A. Rho gtpases and the actin cytoskeleton. Science 1998, 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 28
    • 0034529411 scopus 로고    scopus 로고
    • Paxillin interactions
    • Turner, C.E. Paxillin interactions. J. Cell. Sci. 2000, 113, 4139-4140.
    • (2000) J. Cell. Sci. , vol.113 , pp. 4139-4140
    • Turner, C.E.1
  • 29
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing--aiming for perfect skin regeneration
    • Martin, P. Wound healing--aiming for perfect skin regeneration. Science 1997, 276, 75-81.
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 31
    • 0038806276 scopus 로고    scopus 로고
    • Differential effect of wounding on actin and its associated proteins, paxillin and gelsolin, in fetal skin explants
    • Cowin, A.J.; Hatzirodos, N.; Teusner, J.T.; Belford, D.A. Differential effect of wounding on actin and its associated proteins, paxillin and gelsolin, in fetal skin explants. J. Invest. Dermatol. 2003, 120, 1118-1129.
    • (2003) J. Invest. Dermatol. , vol.120 , pp. 1118-1129
    • Cowin, A.J.1    Hatzirodos, N.2    Teusner, J.T.3    Belford, D.A.4
  • 32
    • 0028306029 scopus 로고
    • Macrophage recruitment during limb development and wound healing in the embryonic and foetal mouse
    • Hopkinson-Woolley, J.; Hughes, D.; Gordon, S.; Martin, P. Macrophage recruitment during limb development and wound healing in the embryonic and foetal mouse. J. Cell. Sci. 1994, 107, 1159-1167.
    • (1994) J. Cell. Sci. , vol.107 , pp. 1159-1167
    • Hopkinson-Woolley, J.1    Hughes, D.2    Gordon, S.3    Martin, P.4
  • 33
    • 0031749423 scopus 로고    scopus 로고
    • Endogenous inflammatory response to dermal wound healing in the fetal and adult mouse
    • Cowin, A.J.; Brosnan, M.P.; Holmes, T.M.; Ferguson, M.W. Endogenous inflammatory response to dermal wound healing in the fetal and adult mouse. Dev. Dyn. 1998, 212, 385-393.
    • (1998) Dev. Dyn. , vol.212 , pp. 385-393
    • Cowin, A.J.1    Brosnan, M.P.2    Holmes, T.M.3    Ferguson, M.W.4
  • 34
    • 0034748462 scopus 로고    scopus 로고
    • Fetal wound healing: Progress report and future directions
    • Longaker, M.T.; Peled, Z.M.; Chang, J.; Krummel, T.M. Fetal wound healing: Progress report and future directions. Surgery 2001, 130, 785-787.
    • (2001) Surgery , vol.130 , pp. 785-787
    • Longaker, M.T.1    Peled, Z.M.2    Chang, J.3    Krummel, T.M.4
  • 36
    • 0028574054 scopus 로고
    • Skin wound healing: Transforming growth factor beta antagonists decrease scarring and improve quality
    • Ferguson, M.W. Skin wound healing: Transforming growth factor beta antagonists decrease scarring and improve quality. J. Interferon Res. 1994, 14, 303-304.
    • (1994) J. Interferon Res. , vol.14 , pp. 303-304
    • Ferguson, M.W.1
  • 38
    • 0031797018 scopus 로고    scopus 로고
    • Actin 'purse string' filaments are anchored by e-cadherin-mediated adherens junctions at the leading edge of the epithelial wound, providing coordinated cell movement
    • Danjo, Y.; Gipson, I.K. Actin 'purse string' filaments are anchored by e-cadherin-mediated adherens junctions at the leading edge of the epithelial wound, providing coordinated cell movement. J. Cell. Sci. 1998, 111, 3323-3332.
    • (1998) J. Cell. Sci. , vol.111 , pp. 3323-3332
    • Danjo, Y.1    Gipson, I.K.2
  • 39
    • 0030811065 scopus 로고    scopus 로고
    • The mechanism of excisional fetal wound repair in vitro is responsive to growth factors
    • Belford, D.A. The mechanism of excisional fetal wound repair in vitro is responsive to growth factors. Endocrinology 1997, 138, 3987-3996.
    • (1997) Endocrinology , vol.138 , pp. 3987-3996
    • Belford, D.A.1
  • 40
    • 0025224225 scopus 로고
    • Ontogenetic transition of wound healing pattern in rat skin occurring at the fetal stage
    • Ihara, S.; Motobayashi, Y.; Nagao, E.; Kistler, A. Ontogenetic transition of wound healing pattern in rat skin occurring at the fetal stage. Development 1990, 110, 671-680.
    • (1990) Development , vol.110 , pp. 671-680
    • Ihara, S.1    Motobayashi, Y.2    Nagao, E.3    Kistler, A.4
  • 42
    • 0034470281 scopus 로고    scopus 로고
    • Biological implications of a discrete mathematical model for collagen deposition and alignment in dermal wound repair
    • Dallon, J.; Sherratt, J.; Maini, P.; Ferguson, M. Biological implications of a discrete mathematical model for collagen deposition and alignment in dermal wound repair. IMA J. Math. Appl. Med. Biol. 2000, 17, 379-393.
    • (2000) IMA J. Math. Appl. Med. Biol. , vol.17 , pp. 379-393
    • Dallon, J.1    Sherratt, J.2    Maini, P.3    Ferguson, M.4
  • 43
    • 0036726924 scopus 로고    scopus 로고
    • Wound remodelling and scarring
    • O'Kane, S. Wound remodelling and scarring. J Wound Care 2002, 11, 296-299.
    • (2002) J Wound Care , vol.11 , pp. 296-299
    • O'Kane, S.1
  • 45
    • 0001027292 scopus 로고    scopus 로고
    • Gelsolin, a multifunctional actin regulatory protein
    • Sun, H.Q.; Yamamoto, M.; Mejillano, M.; Yin, H.L. Gelsolin, a multifunctional actin regulatory protein. J. Biol. Chem. 1999, 274, 33179-33182.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33179-33182
    • Sun, H.Q.1    Yamamoto, M.2    Mejillano, M.3    Yin, H.L.4
  • 46
    • 0026569069 scopus 로고
    • The extracellular actin-scavenger system and actin toxicity
    • Lee, W.M.; Galbraith, R.M. The extracellular actin-scavenger system and actin toxicity. N. Engl. J. Med. 1992, 326, 1335-1341.
    • (1992) N. Engl. J. Med. , vol.326 , pp. 1335-1341
    • Lee, W.M.1    Galbraith, R.M.2
  • 47
    • 0032718864 scopus 로고    scopus 로고
    • Relationship of admission plasma gelsolin levels to clinical outcomes in patients after major trauma
    • Mounzer, K.C.; Moncure, M.; Smith, Y.R.; Dinubile, M.J. Relationship of admission plasma gelsolin levels to clinical outcomes in patients after major trauma. Am. J. Respir. Crit. Care Med. 1999, 160, 1673-1681.
    • (1999) Am. J. Respir. Crit. Care Med. , vol.160 , pp. 1673-1681
    • Mounzer, K.C.1    Moncure, M.2    Smith, Y.R.3    Dinubile, M.J.4
  • 48
    • 0026778133 scopus 로고
    • The small gtp-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley, A.J.; Hall, A. The small gtp-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 1992, 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 50
    • 0026654125 scopus 로고
    • The small gtp-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J.; Paterson, H.F.; Johnston, C.L.; Diekmann, D.; Hall, A. The small gtp-binding protein rac regulates growth factor-induced membrane ruffling. Cell 1992, 70, 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 51
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 gtpases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C.D.; Hall, A. Rho, rac, and cdc42 gtpases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 1995, 81, 53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 54
    • 0032478691 scopus 로고    scopus 로고
    • Identification of the binding partners for flightless i, a novel protein bridging the leucine-rich repeat and the gelsolin superfamilies
    • Liu, Y.T.; Yin, H.L. Identification of the binding partners for flightless i, a novel protein bridging the leucine-rich repeat and the gelsolin superfamilies. J. Biol. Chem. 1998, 273, 7920-7927.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7920-7927
    • Liu, Y.T.1    Yin, H.L.2
  • 55
    • 0028898938 scopus 로고
    • The novel flightless-i gene brings together two gene families, actin-binding proteins related to gelsolin and leucine-rich-repeat proteins involved in ras signal transduction
    • Claudianos, C.; Campbell, H.D. The novel flightless-i gene brings together two gene families, actin-binding proteins related to gelsolin and leucine-rich-repeat proteins involved in ras signal transduction. Mol. Biol. Evol. 1995, 12, 405-414.
    • (1995) Mol. Biol. Evol. , vol.12 , pp. 405-414
    • Claudianos, C.1    Campbell, H.D.2
  • 57
    • 0033845540 scopus 로고    scopus 로고
    • The flightless i protein localizes to actin-based structures during embryonic development
    • Davy, D.A.; Ball, E.E.; Matthaei, K.I.; Campbell, H.D.; Crouch, M.F. The flightless i protein localizes to actin-based structures during embryonic development. Immunol. Cell Biol. 2000, 78, 423-429.
    • (2000) Immunol. Cell Biol. , vol.78 , pp. 423-429
    • Davy, D.A.1    Ball, E.E.2    Matthaei, K.I.3    Campbell, H.D.4    Crouch, M.F.5
  • 58
    • 80051547366 scopus 로고    scopus 로고
    • Decreased expression of flightless i, a gelsolin family member and developmental regulator, in early-gestation fetal wounds improves healing
    • Lin, C.H.; Waters, J.M.; Powell, B.C.; Arkell, R.M.; Cowin, A.J. Decreased expression of flightless i, a gelsolin family member and developmental regulator, in early-gestation fetal wounds improves healing. Mamm. Genome 2011, 22, 341-352.
    • (2011) Mamm. Genome , vol.22 , pp. 341-352
    • Lin, C.H.1    Waters, J.M.2    Powell, B.C.3    Arkell, R.M.4    Cowin, A.J.5
  • 59
    • 84863439950 scopus 로고    scopus 로고
    • Flii neutralizing antibodies improve wound healing in porcine preclinical studies
    • Jackson, J.E.; Kopecki, Z.; Adams, D.H.; Cowin, A.J. Flii neutralizing antibodies improve wound healing in porcine preclinical studies. Wound Repair Regen. 2012, 20, 523-536.
    • (2012) Wound Repair Regen. , vol.20 , pp. 523-536
    • Jackson, J.E.1    Kopecki, Z.2    Adams, D.H.3    Cowin, A.J.4
  • 60
    • 0035110642 scopus 로고    scopus 로고
    • The flightless i protein colocalizes with actin-and microtubule-based structures in motile swiss 3t3 fibroblasts: Evidence for the involvement of pi 3-kinase and ras-related small gtpases
    • Davy, D.A.; Campbell, H.D.; Fountain, S.; de Jong, D.; Crouch, M.F. The flightless i protein colocalizes with actin-and microtubule-based structures in motile swiss 3t3 fibroblasts: Evidence for the involvement of pi 3-kinase and ras-related small gtpases. J. Cell Sci. 2001, 114, 549-562.
    • (2001) J. Cell Sci. , vol.114 , pp. 549-562
    • Davy, D.A.1    Campbell, H.D.2    Fountain, S.3    de Jong, D.4    Crouch, M.F.5
  • 61
    • 77952411667 scopus 로고    scopus 로고
    • Flightless-i (fli-i) regulates the actin assembly activity of diaphanous-related formins (drfs) daam1 and mdia1 in cooperation with active rho gtpase
    • Higashi, T.; Ikeda, T.; Murakami, T.; Shirakawa, R.; Kawato, M.; Okawa, K.; Furuse, M.; Kimura, T.; Kita, T.; Horiuchi, H. Flightless-i (fli-i) regulates the actin assembly activity of diaphanous-related formins (drfs) daam1 and mdia1 in cooperation with active rho gtpase. J. Biol. Chem. 2010, 285, 16231-16238.
    • (2010) J. Biol. Chem. , vol.285 , pp. 16231-16238
    • Higashi, T.1    Ikeda, T.2    Murakami, T.3    Shirakawa, R.4    Kawato, M.5    Okawa, K.6    Furuse, M.7    Kimura, T.8    Kita, T.9    Horiuchi, H.10
  • 62
    • 4644273687 scopus 로고    scopus 로고
    • The role of rho gtpases in the regulation of the rearrangement of actin cytoskeleton and cell movement
    • Begum, R.; Nur, E.K.M.S.; Zaman, M.A. The role of rho gtpases in the regulation of the rearrangement of actin cytoskeleton and cell movement. Exp. Mol. Med. 2004, 36, 358-366.
    • (2004) Exp. Mol. Med. , vol.36 , pp. 358-366
    • Begum, R.1    Nur, E.K.M.S.2    Zaman, M.A.3
  • 63
    • 0035185853 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a rhoa-dependent mechanism
    • Bhowmick, N.A.; Ghiassi, M.; Bakin, A.; Aakre, M.; Lundquist, C.A.; Engel, M.E.; Arteaga, C.L.; Moses, H.L. Transforming growth factor-beta1 mediates epithelial to mesenchymal transdifferentiation through a rhoa-dependent mechanism. Mol. Biol. Cell 2001, 12, 27-36.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 27-36
    • Bhowmick, N.A.1    Ghiassi, M.2    Bakin, A.3    Aakre, M.4    Lundquist, C.A.5    Engel, M.E.6    Arteaga, C.L.7    Moses, H.L.8
  • 64
    • 0034729916 scopus 로고    scopus 로고
    • Rho gtpases: Molecular switches that control the organization and dynamics of the actin cytoskeleton
    • Hall, A.; Nobes, C.D. Rho gtpases: Molecular switches that control the organization and dynamics of the actin cytoskeleton. Philos. Trans. R Soc. Lond B Biol. Sci. 2000, 355, 965-970.
    • (2000) Philos. Trans. R Soc. Lond B Biol. Sci. , vol.355 , pp. 965-970
    • Hall, A.1    Nobes, C.D.2
  • 65
    • 14844337071 scopus 로고    scopus 로고
    • Transforming growth factor-beta and smad signalling in kidney diseases
    • Wang, W.; Koka, V.; Lan, H.Y. Transforming growth factor-beta and smad signalling in kidney diseases. Nephrology 2005, 10, 48-56.
    • (2005) Nephrology , vol.10 , pp. 48-56
    • Wang, W.1    Koka, V.2    Lan, H.Y.3
  • 66
    • 67651085108 scopus 로고    scopus 로고
    • Flightless i regulates hemidesmosome formation and integrin-mediated cellular adhesion and migration during wound repair
    • Kopecki, Z.; Arkell, R.; Powell, B.C.; Cowin, A.J. Flightless i regulates hemidesmosome formation and integrin-mediated cellular adhesion and migration during wound repair. J. Invest. Dermatol. 2009, 129, 2031-2045.
    • (2009) J. Invest. Dermatol. , vol.129 , pp. 2031-2045
    • Kopecki, Z.1    Arkell, R.2    Powell, B.C.3    Cowin, A.J.4
  • 67
    • 0031050310 scopus 로고    scopus 로고
    • Cytoskeletal and adhesion proteins as tumor suppressors
    • Ben-Ze'ev, A. Cytoskeletal and adhesion proteins as tumor suppressors. Curr. Opin. Cell. Biol. 1997, 9, 99-108.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 99-108
    • Ben-Ze'ev, A.1
  • 68
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the rho family gtpases in mammalian cells
    • Kaibuchi, K.; Kuroda, S.; Amano, M. Regulation of the cytoskeleton and cell adhesion by the rho family gtpases in mammalian cells. Annu. Rev. Biochem. 1999, 68, 459-486.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 69
    • 28544450380 scopus 로고    scopus 로고
    • Transforming growth factor-beta activation of phosphatidylinositol 3-kinase is independent of smad2 and smad3 and regulates fibroblast responses via p21-activated kinase-2
    • Wilkes, M.C.; Mitchell, H.; Penheiter, S.G.; Dore, J.J.; Suzuki, K.; Edens, M.; Sharma, D.K.; Pagano, R.E.; Leof, E.B. Transforming growth factor-beta activation of phosphatidylinositol 3-kinase is independent of smad2 and smad3 and regulates fibroblast responses via p21-activated kinase-2. Cancer Res. 2005, 65, 10431-10440.
    • (2005) Cancer Res. , vol.65 , pp. 10431-10440
    • Wilkes, M.C.1    Mitchell, H.2    Penheiter, S.G.3    Dore, J.J.4    Suzuki, K.5    Edens, M.6    Sharma, D.K.7    Pagano, R.E.8    Leof, E.B.9
  • 70
    • 0028174630 scopus 로고
    • Neutralising antibody to tgf-beta 1,2 reduces cutaneous scarring in adult rodents
    • Shah, M.; Foreman, D.M.; Ferguson, M.W. Neutralising antibody to tgf-beta 1,2 reduces cutaneous scarring in adult rodents. J. Cell. Sci. 1994, 107, 1137-1157.
    • (1994) J. Cell. Sci. , vol.107 , pp. 1137-1157
    • Shah, M.1    Foreman, D.M.2    Ferguson, M.W.3
  • 71
    • 79952766175 scopus 로고    scopus 로고
    • Regeneration of hair follicles is modulated by flightless i (flii) in a rodent vibrissa model
    • Waters, J.M.; Lindo, J.E.; Arkell, R.M.; Cowin, A.J. Regeneration of hair follicles is modulated by flightless i (flii) in a rodent vibrissa model. J. Invest. Dermatol. 2011.
    • (2011) J. Invest. Dermatol.
    • Waters, J.M.1    Lindo, J.E.2    Arkell, R.M.3    Cowin, A.J.4
  • 72
    • 33751000758 scopus 로고    scopus 로고
    • Interplay of fli-i and flap1 for regulation of beta-catenin dependent transcription
    • Lee, Y.H.; Stallcup, M.R. Interplay of fli-i and flap1 for regulation of beta-catenin dependent transcription. Nucleic. Acids Res. 2006, 34, 5052-5059.
    • (2006) Nucleic. Acids Res. , vol.34 , pp. 5052-5059
    • Lee, Y.H.1    Stallcup, M.R.2
  • 73
    • 10644295590 scopus 로고    scopus 로고
    • The flightless i protein and the gelsolin family in nuclear hormone receptor-mediated signalling
    • Archer, S.K.; Behm, C.A.; Claudianos, C.; Campbell, H.D. The flightless i protein and the gelsolin family in nuclear hormone receptor-mediated signalling. Biochem. Soc. Trans. 2004, 32, 940-942.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 940-942
    • Archer, S.K.1    Behm, C.A.2    Claudianos, C.3    Campbell, H.D.4
  • 74
    • 1342325341 scopus 로고    scopus 로고
    • Developmentally essential protein flightless i is a nuclear receptor coactivator with actin binding activity
    • Lee, Y.H.; Campbell, H.D.; Stallcup, M.R. Developmentally essential protein flightless i is a nuclear receptor coactivator with actin binding activity. Mol. Cell. Biol. 2004, 24, 2103-2117.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2103-2117
    • Lee, Y.H.1    Campbell, H.D.2    Stallcup, M.R.3
  • 75
    • 0344867848 scopus 로고    scopus 로고
    • Novel proteins interacting with the leucine-rich repeat domain of human flightless-i identified by the yeast two-hybrid system
    • Fong, K.S.; de Couet, H.G. Novel proteins interacting with the leucine-rich repeat domain of human flightless-i identified by the yeast two-hybrid system. Genomics 1999, 58, 146-157.
    • (1999) Genomics , vol.58 , pp. 146-157
    • Fong, K.S.1    de Couet, H.G.2
  • 76
    • 46749090373 scopus 로고    scopus 로고
    • Flightless-i, a gelsolin family member and transcriptional regulator, preferentially binds directly to activated cytosolic camk-ii
    • Seward, M.E.; Easley, C.A.T.; McLeod, J.J.; Myers, A.L.; Tombes, R.M. Flightless-i, a gelsolin family member and transcriptional regulator, preferentially binds directly to activated cytosolic camk-ii. FEBS Lett. 2008, 582, 2489-2495.
    • (2008) FEBS Lett. , vol.582 , pp. 2489-2495
    • Seward, M.E.1    Easley, C.A.T.2    McLeod, J.J.3    Myers, A.L.4    Tombes, R.M.5
  • 77
    • 84869789705 scopus 로고    scopus 로고
    • Flightless, secreted through a late endosome/lysosome pathway, binds lps and dampens cytokine secretion
    • Lei, N.; Franken, L.; Ruzehaji, N.; Offenhauser, C.; Cowin, A.J.; Murray, R.Z. Flightless, secreted through a late endosome/lysosome pathway, binds lps and dampens cytokine secretion. J. Cell. Sci. 2012.
    • (2012) J. Cell. Sci.
    • Lei, N.1    Franken, L.2    Ruzehaji, N.3    Offenhauser, C.4    Cowin, A.J.5    Murray, R.Z.6
  • 78
    • 0042889568 scopus 로고    scopus 로고
    • The roles of protein-protein interactions and protein methylation in transcriptional activation by nuclear receptors and their coactivators
    • Stallcup, M.R.; Kim, J.H.; Teyssier, C.; Lee, Y.H.; Ma, H.; Chen, D. The roles of protein-protein interactions and protein methylation in transcriptional activation by nuclear receptors and their coactivators. J. Steroid Biochem. Mol. Biol. 2003, 85, 139-145.
    • (2003) J. Steroid Biochem. Mol. Biol. , vol.85 , pp. 139-145
    • Stallcup, M.R.1    Kim, J.H.2    Teyssier, C.3    Lee, Y.H.4    Ma, H.5    Chen, D.6
  • 79
    • 77952566304 scopus 로고    scopus 로고
    • The cytosolic nucleic acid sensor lrrfip1 mediates the production of type i interferon via a beta-catenin-dependent pathway
    • Yang, P.; An, H.; Liu, X.; Wen, M.; Zheng, Y.; Rui, Y.; Cao, X. The cytosolic nucleic acid sensor lrrfip1 mediates the production of type i interferon via a beta-catenin-dependent pathway. Nat. Immunol. 2010, 11, 487-494.
    • (2010) Nat. Immunol. , vol.11 , pp. 487-494
    • Yang, P.1    An, H.2    Liu, X.3    Wen, M.4    Zheng, Y.5    Rui, Y.6    Cao, X.7
  • 80
    • 13844321895 scopus 로고    scopus 로고
    • Identification of the wnt signaling activator leucine-rich repeat in flightless interaction protein 2 by a genomewide functional analysis
    • Liu, J.; Bang, A.G.; Kintner, C.; Orth, A.P.; Chanda, S.K.; Ding, S.; Schultz, P.G. Identification of the wnt signaling activator leucine-rich repeat in flightless interaction protein 2 by a genomewide functional analysis. Proc. Natl. Acad. Sci. USA 2005, 102, 1927-1932.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1927-1932
    • Liu, J.1    Bang, A.G.2    Kintner, C.3    Orth, A.P.4    Chanda, S.K.5    Ding, S.6    Schultz, P.G.7
  • 81
    • 75149193602 scopus 로고    scopus 로고
    • Interaction of wingless protein (wnt), transforming growth factor-beta1, and hyaluronan production in fetal and postnatal fibroblasts
    • Carre, A.L.; James, A.W.; MacLeod, L.; Kong, W.; Kawai, K.; Longaker, M.T.; Lorenz, H.P. Interaction of wingless protein (wnt), transforming growth factor-beta1, and hyaluronan production in fetal and postnatal fibroblasts. Plast. Reconstr. Surg. 2010, 125, 74-88.
    • (2010) Plast. Reconstr. Surg. , vol.125 , pp. 74-88
    • Carre, A.L.1    James, A.W.2    MacLeod, L.3    Kong, W.4    Kawai, K.5    Longaker, M.T.6    Lorenz, H.P.7


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