메뉴 건너뛰기




Volumn 21, Issue 4, 2014, Pages 333-344

Vimentin as an integral regulator of cell adhesion and endothelial sprouting

Author keywords

Angiogenesis; Calpain; Cancer; Cell adhesion; Cytoskeleton; Endothelial cell; Extracellular matrix; Intermediate filaments; MT1 MMP; Signal transduction; Vimentin; Wall shear stress

Indexed keywords

AURORA B KINASE; CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CALPAIN; CASPASE 3; CASPASE 6; CASPASE 7; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIN DEPENDENT KINASE 1; MATRIX METALLOPROTEINASE 14; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; P21 ACTIVATED KINASE; POLO LIKE KINASE 1; PROTEIN KINASE; PROTEIN KINASE C; PROTEINASE; RHO ASSOCIATED PROTEIN KINASE; UNCLASSIFIED DRUG; VIMENTIN;

EID: 84901016847     PISSN: 10739688     EISSN: 15498719     Source Type: Journal    
DOI: 10.1111/micc.12111     Document Type: Review
Times cited : (141)

References (151)
  • 1
    • 34249689753 scopus 로고    scopus 로고
    • Molecular regulation of angiogenesis and lymphangiogenesis
    • Adams RH, Alitalo K. Molecular regulation of angiogenesis and lymphangiogenesis. Nat Rev Mol Cell Biol 8: 464-478, 2007.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 464-478
    • Adams, R.H.1    Alitalo, K.2
  • 2
    • 0024512061 scopus 로고
    • Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure
    • Ando S, Tanabe K, Gonda Y, Sato C, Inagaki M. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. Biochemistry 28: 2974-2979, 1989.
    • (1989) Biochemistry , vol.28 , pp. 2974-2979
    • Ando, S.1    Tanabe, K.2    Gonda, Y.3    Sato, C.4    Inagaki, M.5
  • 3
    • 0025729228 scopus 로고
    • Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2(+)-calmodulin-dependent protein kinase II
    • Ando S, Tokui T, Yamauchi T, Sugiura H, Tanabe K, Inagaki M. Evidence that Ser-82 is a unique phosphorylation site on vimentin for Ca2(+)-calmodulin-dependent protein kinase II. Biochem Biophys Res Commun 175: 955-962, 1991.
    • (1991) Biochem Biophys Res Commun , vol.175 , pp. 955-962
    • Ando, S.1    Tokui, T.2    Yamauchi, T.3    Sugiura, H.4    Tanabe, K.5    Inagaki, M.6
  • 4
    • 0035089777 scopus 로고    scopus 로고
    • Localized activation of m-calpain in migrating human umbilical vein endothelial cells stimulated by shear stress
    • Ariyoshi H, Yoshikawa N, Aono Y, Tsuji Y, Ueda A, Tokunaga M, Sakon M, Monden M. Localized activation of m-calpain in migrating human umbilical vein endothelial cells stimulated by shear stress. J Cell Biochem 81: 184-192, 2001.
    • (2001) J Cell Biochem , vol.81 , pp. 184-192
    • Ariyoshi, H.1    Yoshikawa, N.2    Aono, Y.3    Tsuji, Y.4    Ueda, A.5    Tokunaga, M.6    Sakon, M.7    Monden, M.8
  • 5
    • 82955248167 scopus 로고    scopus 로고
    • How focal adhesion kinase achieves regulation by linking ligand binding, localization and action
    • Arold ST. How focal adhesion kinase achieves regulation by linking ligand binding, localization and action. Curr Opin Struct Biol 21: 808-813, 2011.
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 808-813
    • Arold, S.T.1
  • 6
    • 5144228375 scopus 로고    scopus 로고
    • The biology of desmin filaments: how do mutations affect their structure, assembly, and organisation?
    • Bar H, Strelkov SV, Sjoberg G, Aebi U, Herrmann H. The biology of desmin filaments: how do mutations affect their structure, assembly, and organisation? J Struct Biol 148: 137-152, 2004.
    • (2004) J Struct Biol , vol.148 , pp. 137-152
    • Bar, H.1    Strelkov, S.V.2    Sjoberg, G.3    Aebi, U.4    Herrmann, H.5
  • 7
    • 79959508436 scopus 로고    scopus 로고
    • Targeting the phosphoinositide-3 (PI3) kinase pathway in breast cancer
    • Baselga J. Targeting the phosphoinositide-3 (PI3) kinase pathway in breast cancer. Oncologist 16(Suppl. 1): 12-19, 2011.
    • (2011) Oncologist , vol.16 , Issue.SUPPL. 1 , pp. 12-19
    • Baselga, J.1
  • 8
    • 0028355888 scopus 로고
    • PDGF-BB modulates endothelial proliferation and angiogenesis in vitro via PDGF beta-receptors
    • Battegay EJ, Rupp J, Iruela-Arispe L, Sage EH, Pech M. PDGF-BB modulates endothelial proliferation and angiogenesis in vitro via PDGF beta-receptors. J Cell Biol 125: 917-928, 1994.
    • (1994) J Cell Biol , vol.125 , pp. 917-928
    • Battegay, E.J.1    Rupp, J.2    Iruela-Arispe, L.3    Sage, E.H.4    Pech, M.5
  • 9
    • 0344495425 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate markedly induces matrix metalloproteinase and integrin-dependent human endothelial cell invasion and lumen formation in three-dimensional collagen and fibrin matrices
    • Bayless KJ, Davis GE. Sphingosine-1-phosphate markedly induces matrix metalloproteinase and integrin-dependent human endothelial cell invasion and lumen formation in three-dimensional collagen and fibrin matrices. Biochem Biophys Res Commun 312: 903-913, 2003.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 903-913
    • Bayless, K.J.1    Davis, G.E.2
  • 10
    • 74949103571 scopus 로고    scopus 로고
    • Investigating endothelial invasion and sprouting behavior in three-dimensional collagen matrices
    • Bayless KJ, Kwak HI, Su SC. Investigating endothelial invasion and sprouting behavior in three-dimensional collagen matrices. Nat Protoc 4: 1888-1898, 2009.
    • (2009) Nat Protoc , vol.4 , pp. 1888-1898
    • Bayless, K.J.1    Kwak, H.I.2    Su, S.C.3
  • 11
    • 0033847194 scopus 로고    scopus 로고
    • RGD-dependent vacuolation and lumen formation observed during endothelial cell morphogenesis in three-dimensional fibrin matrices involves the alpha(v)beta(3) and alpha(5)beta(1) integrins
    • Bayless KJ, Salazar R, Davis GE. RGD-dependent vacuolation and lumen formation observed during endothelial cell morphogenesis in three-dimensional fibrin matrices involves the alpha(v)beta(3) and alpha(5)beta(1) integrins. Am J Pathol 156: 1673-1683, 2000.
    • (2000) Am J Pathol , vol.156 , pp. 1673-1683
    • Bayless, K.J.1    Salazar, R.2    Davis, G.E.3
  • 12
    • 0028360872 scopus 로고
    • Structural elements of the amino-terminal head domain of vimentin essential for intermediate filament formation in vivo and in vitro
    • Beuttenmuller M, Chen M, Janetzko A, Kuhn S, Traub P. Structural elements of the amino-terminal head domain of vimentin essential for intermediate filament formation in vivo and in vitro. Exp Cell Res 213: 128-142, 1994.
    • (1994) Exp Cell Res , vol.213 , pp. 128-142
    • Beuttenmuller, M.1    Chen, M.2    Janetzko, A.3    Kuhn, S.4    Traub, P.5
  • 13
    • 29944436856 scopus 로고    scopus 로고
    • Endothelial FAK is essential for vascular network stability, cell survival, and lamellipodial formation
    • Braren R, Hu H, Kim YH, Beggs HE, Reichardt LF, Wang R. Endothelial FAK is essential for vascular network stability, cell survival, and lamellipodial formation. J Cell Biol 172: 151-162, 2006.
    • (2006) J Cell Biol , vol.172 , pp. 151-162
    • Braren, R.1    Hu, H.2    Kim, Y.H.3    Beggs, H.E.4    Reichardt, L.F.5    Wang, R.6
  • 14
    • 0028362876 scopus 로고
    • Requirement of vascular integrin alpha v beta 3 for angiogenesis
    • Brooks PC, Clark RA, Cheresh DA. Requirement of vascular integrin alpha v beta 3 for angiogenesis. Science 264: 569-571, 1994.
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 15
    • 77958038961 scopus 로고    scopus 로고
    • Keeping the vimentin network under control: cell-matrix adhesion-associated plectin 1f affects cell shape and polarity of fibroblasts
    • Burgstaller G, Gregor M, Winter L, Wiche G. Keeping the vimentin network under control: cell-matrix adhesion-associated plectin 1f affects cell shape and polarity of fibroblasts. Mol Biol Cell 21: 3362-3375, 2010.
    • (2010) Mol Biol Cell , vol.21 , pp. 3362-3375
    • Burgstaller, G.1    Gregor, M.2    Winter, L.3    Wiche, G.4
  • 16
    • 0035020420 scopus 로고    scopus 로고
    • Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis
    • Byun Y, Chen F, Chang R, Trivedi M, Green KJ, Cryns VL. Caspase cleavage of vimentin disrupts intermediate filaments and promotes apoptosis. Cell Death Differ 8: 443-450, 2001.
    • (2001) Cell Death Differ , vol.8 , pp. 443-450
    • Byun, Y.1    Chen, F.2    Chang, R.3    Trivedi, M.4    Green, K.J.5    Cryns, V.L.6
  • 17
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood DA. Integrin activation. J Cell Sci 117: 657-666, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 18
    • 0037699955 scopus 로고    scopus 로고
    • Angiogenesis in health and disease
    • Carmeliet P. Angiogenesis in health and disease. Nat Med 9: 653-660, 2003.
    • (2003) Nat Med , vol.9 , pp. 653-660
    • Carmeliet, P.1
  • 19
    • 22444447946 scopus 로고    scopus 로고
    • Common mechanisms of nerve and blood vessel wiring
    • Carmeliet P, Tessier-Lavigne M. Common mechanisms of nerve and blood vessel wiring. Nature 436: 193-200, 2005.
    • (2005) Nature , vol.436 , pp. 193-200
    • Carmeliet, P.1    Tessier-Lavigne, M.2
  • 20
    • 0026699760 scopus 로고
    • The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes
    • Cheng J, Syder AJ, Yu QC, Letai A, Paller AS, Fuchs E. The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes. Cell 70: 811-819, 1992.
    • (1992) Cell , vol.70 , pp. 811-819
    • Cheng, J.1    Syder, A.J.2    Yu, Q.C.3    Letai, A.4    Paller, A.S.5    Fuchs, E.6
  • 22
    • 0025895855 scopus 로고
    • The regulation of intermediate filament reorganization in mitosis. p34cdc2 phosphorylates vimentin at a unique N-terminal site
    • Chou YH, Ngai KL, Goldman R. The regulation of intermediate filament reorganization in mitosis. p34cdc2 phosphorylates vimentin at a unique N-terminal site. J Biol Chem 266: 7325-7328, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 7325-7328
    • Chou, Y.H.1    Ngai, K.L.2    Goldman, R.3
  • 25
    • 0027465098 scopus 로고
    • Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis
    • Cote F, Collard JF, Julien JP. Progressive neuronopathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis. Cell 73: 35-46, 1993.
    • (1993) Cell , vol.73 , pp. 35-46
    • Cote, F.1    Collard, J.F.2    Julien, J.P.3
  • 26
    • 0026730798 scopus 로고
    • Expression of the class VI intermediate filament nestin in human central nervous system tumors
    • Dahlstrand J, Collins VP, Lendahl U. Expression of the class VI intermediate filament nestin in human central nervous system tumors. Cancer Res 52: 5334-5341, 1992.
    • (1992) Cancer Res , vol.52 , pp. 5334-5341
    • Dahlstrand, J.1    Collins, V.P.2    Lendahl, U.3
  • 27
    • 84886930695 scopus 로고    scopus 로고
    • Proteomic profiling of endothelial invasion revealed receptor for activated C kinase 1 (RACK1) complexed with vimentin to regulate focal adhesion kinase (FAK)
    • Dave JM, Kang H, Abbey CA, Maxwell SA, Bayless KJ. Proteomic profiling of endothelial invasion revealed receptor for activated C kinase 1 (RACK1) complexed with vimentin to regulate focal adhesion kinase (FAK). J Biol Chem 288: 30720-30733, 2013.
    • (2013) J Biol Chem , vol.288 , pp. 30720-30733
    • Dave, J.M.1    Kang, H.2    Abbey, C.A.3    Maxwell, S.A.4    Bayless, K.J.5
  • 28
    • 79953800449 scopus 로고    scopus 로고
    • Molecular basis for endothelial lumen formation and tubulogenesis during vasculogenesis and angiogenic sprouting
    • Davis GE, Stratman AN, Sacharidou A, Koh W. Molecular basis for endothelial lumen formation and tubulogenesis during vasculogenesis and angiogenic sprouting. Int Rev Cell Mol Biol 288: 101-165, 2011.
    • (2011) Int Rev Cell Mol Biol , vol.288 , pp. 101-165
    • Davis, G.E.1    Stratman, A.N.2    Sacharidou, A.3    Koh, W.4
  • 29
    • 0025924582 scopus 로고
    • A complex containing p34cdc2 and cyclin B phosphorylates the nuclear lamin and disassembles nuclei of clam oocytes in vitro
    • Dessev G, Iovcheva-Dessev C, Bischoff JR, Beach D, Goldman R. A complex containing p34cdc2 and cyclin B phosphorylates the nuclear lamin and disassembles nuclei of clam oocytes in vitro. J Cell Biol 112: 523-533, 1991.
    • (1991) J Cell Biol , vol.112 , pp. 523-533
    • Dessev, G.1    Iovcheva-Dessev, C.2    Bischoff, J.R.3    Beach, D.4    Goldman, R.5
  • 31
    • 0032504745 scopus 로고    scopus 로고
    • Fluid shear stress stimulates phosphorylation of Akt in human endothelial cells: involvement in suppression of apoptosis
    • Dimmeler S, Assmus B, Hermann C, Haendeler J, Zeiher AM. Fluid shear stress stimulates phosphorylation of Akt in human endothelial cells: involvement in suppression of apoptosis. Circ Res 83: 334-341, 1998.
    • (1998) Circ Res , vol.83 , pp. 334-341
    • Dimmeler, S.1    Assmus, B.2    Hermann, C.3    Haendeler, J.4    Zeiher, A.M.5
  • 32
    • 0033542476 scopus 로고    scopus 로고
    • Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation
    • Dimmeler S, Fleming I, Fisslthaler B, Hermann C, Busse R, Zeiher AM. Activation of nitric oxide synthase in endothelial cells by Akt-dependent phosphorylation. Nature 399: 601-605, 1999.
    • (1999) Nature , vol.399 , pp. 601-605
    • Dimmeler, S.1    Fleming, I.2    Fisslthaler, B.3    Hermann, C.4    Busse, R.5    Zeiher, A.M.6
  • 33
    • 0028981497 scopus 로고
    • An antagonist of integrin alpha v beta 3 prevents maturation of blood vessels during embryonic neovascularization
    • Drake CJ, Cheresh DA, Little CD. An antagonist of integrin alpha v beta 3 prevents maturation of blood vessels during embryonic neovascularization. J Cell Sci 108(Pt 7): 2655-2661, 1995.
    • (1995) J Cell Sci , vol.108 , Issue.PART 7 , pp. 2655-2661
    • Drake, C.J.1    Cheresh, D.A.2    Little, C.D.3
  • 37
    • 41949103193 scopus 로고    scopus 로고
    • The type III neurofilament peripherin is expressed in the tuberomammillary neurons of the mouse
    • Eriksson KS, Zhang S, Lin L, Lariviere RC, Julien JP, Mignot E. The type III neurofilament peripherin is expressed in the tuberomammillary neurons of the mouse. BMC Neurosci 9: 26, 2008.
    • (2008) BMC Neurosci , vol.9 , pp. 26
    • Eriksson, K.S.1    Zhang, S.2    Lin, L.3    Lariviere, R.C.4    Julien, J.P.5    Mignot, E.6
  • 38
    • 0024526186 scopus 로고
    • Phosphorylation of vimentin in mitotically selected cells. In vitro cyclic AMP-independent kinase and calcium-stimulated phosphatase activities
    • Evans RM. Phosphorylation of vimentin in mitotically selected cells. In vitro cyclic AMP-independent kinase and calcium-stimulated phosphatase activities. J Cell Biol 108: 67-78, 1989.
    • (1989) J Cell Biol , vol.108 , pp. 67-78
    • Evans, R.M.1
  • 39
    • 0031912140 scopus 로고    scopus 로고
    • Vimentin: the conundrum of the intermediate filament gene family
    • Evans RM. Vimentin: the conundrum of the intermediate filament gene family. BioEssays 20: 79-86, 1998.
    • (1998) BioEssays , vol.20 , pp. 79-86
    • Evans, R.M.1
  • 40
    • 64949162015 scopus 로고    scopus 로고
    • O-GlcNAc modification of radial glial vimentin filaments in the developing chick brain
    • Farach AM, Galileo DS. O-GlcNAc modification of radial glial vimentin filaments in the developing chick brain. Brain Cell Biol 36: 191-202, 2008.
    • (2008) Brain Cell Biol , vol.36 , pp. 191-202
    • Farach, A.M.1    Galileo, D.S.2
  • 41
    • 0034499732 scopus 로고    scopus 로고
    • Vascular endothelial growth factor and the regulation of angiogenesis
    • discussion 35-16
    • Ferrara N. Vascular endothelial growth factor and the regulation of angiogenesis. Recent Prog Horm Res 55: 15-35; discussion 35-16, 2000.
    • (2000) Recent Prog Horm Res , vol.55 , pp. 15-35
    • Ferrara, N.1
  • 42
    • 2942590261 scopus 로고    scopus 로고
    • Vascular endothelial growth factor as a target for anticancer therapy
    • Ferrara N. Vascular endothelial growth factor as a target for anticancer therapy. Oncologist 9(Suppl. 1): 2-10, 2004.
    • (2004) Oncologist , vol.9 , Issue.SUPPL. 1 , pp. 2-10
    • Ferrara, N.1
  • 44
    • 27144465277 scopus 로고    scopus 로고
    • Role of PECAM-1 in the shear-stress-induced activation of Akt and the endothelial nitric oxide synthase (eNOS) in endothelial cells
    • Fleming I, Fisslthaler B, Dixit M, Busse R. Role of PECAM-1 in the shear-stress-induced activation of Akt and the endothelial nitric oxide synthase (eNOS) in endothelial cells. J Cell Sci 118: 4103-4111, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 4103-4111
    • Fleming, I.1    Fisslthaler, B.2    Dixit, M.3    Busse, R.4
  • 45
    • 0026846928 scopus 로고
    • The role of angiogenesis in tumor growth
    • Folkman J. The role of angiogenesis in tumor growth. Semin Cancer Biol 3: 65-71, 1992.
    • (1992) Semin Cancer Biol , vol.3 , pp. 65-71
    • Folkman, J.1
  • 46
    • 0030448814 scopus 로고    scopus 로고
    • Blood vessel formation: what is its molecular basis?
    • Folkman J, D'Amore PA. Blood vessel formation: what is its molecular basis? Cell 87: 1153-1155, 1996.
    • (1996) Cell , vol.87 , pp. 1153-1155
    • Folkman, J.1    D'Amore, P.A.2
  • 47
    • 0018756083 scopus 로고
    • Intermediate-sized filaments of human endothelial cells
    • Franke WW, Schmid E, Osborn M, Weber K. Intermediate-sized filaments of human endothelial cells. J Cell Biol 81: 570-580, 1979.
    • (1979) J Cell Biol , vol.81 , pp. 570-580
    • Franke, W.W.1    Schmid, E.2    Osborn, M.3    Weber, K.4
  • 48
    • 0020826780 scopus 로고
    • Unraveling the structure of the intermediate filaments
    • Fuchs E, Hanukoglu I. Unraveling the structure of the intermediate filaments. Cell 34: 332-334, 1983.
    • (1983) Cell , vol.34 , pp. 332-334
    • Fuchs, E.1    Hanukoglu, I.2
  • 50
    • 0015982084 scopus 로고
    • Tumor growth and neovascularization: an experimental model using the rabbit cornea
    • Gimbrone MA, Jr, Cotran RS, Leapman SB, Folkman J. Tumor growth and neovascularization: an experimental model using the rabbit cornea. J Natl Cancer Inst 52: 413-427, 1974.
    • (1974) J Natl Cancer Inst , vol.52 , pp. 413-427
    • Gimbrone Jr, M.A.1    Cotran, R.S.2    Leapman, S.B.3    Folkman, J.4
  • 51
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: calpain proteases in cell motility
    • Glading A, Lauffenburger DA, Wells A. Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol 12: 46-54, 2002.
    • (2002) Trends Cell Biol , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 52
    • 34248578409 scopus 로고    scopus 로고
    • Dissecting the 3-D structure of vimentin intermediate filaments by cryo-electron tomography
    • Goldie KN, Wedig T, Mitra AK, Aebi U, Herrmann H, Hoenger A. Dissecting the 3-D structure of vimentin intermediate filaments by cryo-electron tomography. J Struct Biol 158: 378-385, 2007.
    • (2007) J Struct Biol , vol.158 , pp. 378-385
    • Goldie, K.N.1    Wedig, T.2    Mitra, A.K.3    Aebi, U.4    Herrmann, H.5    Hoenger, A.6
  • 54
    • 0023989757 scopus 로고
    • Basic fibroblast growth factor: expression in cultured bovine vascular smooth muscle cells
    • Gospodarowicz D, Ferrara N, Haaparanta T, Neufeld G. Basic fibroblast growth factor: expression in cultured bovine vascular smooth muscle cells. Eur J Cell Biol 46: 144-151, 1988.
    • (1988) Eur J Cell Biol , vol.46 , pp. 144-151
    • Gospodarowicz, D.1    Ferrara, N.2    Haaparanta, T.3    Neufeld, G.4
  • 55
    • 0032496146 scopus 로고    scopus 로고
    • Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis
    • Goto H, Kosako H, Tanabe K, Yanagida M, Sakurai M, Amano M, Kaibuchi K, Inagaki M. Phosphorylation of vimentin by Rho-associated kinase at a unique amino-terminal site that is specifically phosphorylated during cytokinesis. J Biol Chem 273: 11728-11736, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 11728-11736
    • Goto, H.1    Kosako, H.2    Tanabe, K.3    Yanagida, M.4    Sakurai, M.5    Amano, M.6    Kaibuchi, K.7    Inagaki, M.8
  • 56
    • 0036199426 scopus 로고    scopus 로고
    • Phosphorylation and reorganization of vimentin by p21-activated kinase (PAK)
    • Goto H, Tanabe K, Manser E, Lim L, Yasui Y, Inagaki M. Phosphorylation and reorganization of vimentin by p21-activated kinase (PAK). Genes Cells 7: 91-97, 2002.
    • (2002) Genes Cells , vol.7 , pp. 91-97
    • Goto, H.1    Tanabe, K.2    Manser, E.3    Lim, L.4    Yasui, Y.5    Inagaki, M.6
  • 57
    • 0037424487 scopus 로고    scopus 로고
    • Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process
    • Goto H, Yasui Y, Kawajiri A, Nigg EA, Terada Y, Tatsuka M, Nagata K, Inagaki M. Aurora-B regulates the cleavage furrow-specific vimentin phosphorylation in the cytokinetic process. J Biol Chem 278: 8526-8530, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 8526-8530
    • Goto, H.1    Yasui, Y.2    Kawajiri, A.3    Nigg, E.A.4    Terada, Y.5    Tatsuka, M.6    Nagata, K.7    Inagaki, M.8
  • 58
    • 38649096645 scopus 로고    scopus 로고
    • Friendly fire against neutrophils: proteolytic enzymes confuse the recognition of apoptotic cells by macrophages
    • Guzik K, Potempa J. Friendly fire against neutrophils: proteolytic enzymes confuse the recognition of apoptotic cells by macrophages. Biochimie 90: 405-415, 2008.
    • (2008) Biochimie , vol.90 , pp. 405-415
    • Guzik, K.1    Potempa, J.2
  • 59
    • 1642503683 scopus 로고    scopus 로고
    • Intermediate filaments are dynamic and motile elements of cellular architecture
    • Helfand BT, Chang L, Goldman RD. Intermediate filaments are dynamic and motile elements of cellular architecture. J Cell Sci 117: 133-141, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 133-141
    • Helfand, B.T.1    Chang, L.2    Goldman, R.D.3
  • 60
    • 0037182581 scopus 로고    scopus 로고
    • A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization
    • Helfand BT, Mikami A, Vallee RB, Goldman RD. A requirement for cytoplasmic dynein and dynactin in intermediate filament network assembly and organization. J Cell Biol 157: 795-806, 2002.
    • (2002) J Cell Biol , vol.157 , pp. 795-806
    • Helfand, B.T.1    Mikami, A.2    Vallee, R.B.3    Goldman, R.D.4
  • 61
    • 79954507607 scopus 로고    scopus 로고
    • Expression of nestin by neural cells in the adult rat and human brain
    • Hendrickson ML, Rao AJ, Demerdash ON, Kalil RE. Expression of nestin by neural cells in the adult rat and human brain. PLoS ONE 6: e18535, 2011.
    • (2011) PLoS ONE , vol.6
    • Hendrickson, M.L.1    Rao, A.J.2    Demerdash, O.N.3    Kalil, R.E.4
  • 63
    • 0034907507 scopus 로고    scopus 로고
    • Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18
    • Hesse M, Magin TM, Weber K. Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18. J Cell Sci 114: 2569-2575, 2001.
    • (2001) J Cell Sci , vol.114 , pp. 2569-2575
    • Hesse, M.1    Magin, T.M.2    Weber, K.3
  • 64
    • 78149450610 scopus 로고    scopus 로고
    • Moderation of calpain activity promotes neovascular integration and lumen formation during VEGF-induced pathological angiogenesis
    • Hoang MV, Nagy JA, Fox JE, Senger DR. Moderation of calpain activity promotes neovascular integration and lumen formation during VEGF-induced pathological angiogenesis. PLoS ONE 5: e13612, 2010.
    • (2010) PLoS ONE , vol.5
    • Hoang, M.V.1    Nagy, J.A.2    Fox, J.E.3    Senger, D.R.4
  • 65
    • 0031754831 scopus 로고    scopus 로고
    • Endothelial cells assemble two distinct alpha6beta4-containing vimentin-associated structures: roles for ligand binding and the beta4 cytoplasmic tail
    • Homan SM, Mercurio AM, LaFlamme SE. Endothelial cells assemble two distinct alpha6beta4-containing vimentin-associated structures: roles for ligand binding and the beta4 cytoplasmic tail. J Cell Sci 111(Pt 18): 2717-2728, 1998.
    • (1998) J Cell Sci , vol.111 , Issue.PART 18 , pp. 2717-2728
    • Homan, S.M.1    Mercurio, A.M.2    LaFlamme, S.E.3
  • 66
    • 0034641107 scopus 로고    scopus 로고
    • Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3
    • Hotary K, Allen E, Punturieri A, Yana I, Weiss SJ. Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3. J Cell Biol 149: 1309-1323, 2000.
    • (2000) J Cell Biol , vol.149 , pp. 1309-1323
    • Hotary, K.1    Allen, E.2    Punturieri, A.3    Yana, I.4    Weiss, S.J.5
  • 67
    • 0029739975 scopus 로고    scopus 로고
    • Angiogenic potential of microvessel fragments established in three-dimensional collagen gels
    • Hoying JB, Boswell CA, Williams SK. Angiogenic potential of microvessel fragments established in three-dimensional collagen gels. In Vitro Cell Dev Biol Anim 32: 409-419, 1996.
    • (1996) In Vitro Cell Dev Biol Anim , vol.32 , pp. 409-419
    • Hoying, J.B.1    Boswell, C.A.2    Williams, S.K.3
  • 69
    • 0026770377 scopus 로고
    • Integrins: versatility, modulation, and signaling in cell adhesion
    • Hynes RO. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69: 11-25, 1992.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 70
    • 0023928876 scopus 로고
    • Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly-disassembly of desmin
    • Inagaki M, Gonda Y, Matsuyama M, Nishizawa K, Nishi Y, Sato C. Intermediate filament reconstitution in vitro. The role of phosphorylation on the assembly-disassembly of desmin. J Biol Chem 263: 5970-5978, 1988.
    • (1988) J Biol Chem , vol.263 , pp. 5970-5978
    • Inagaki, M.1    Gonda, Y.2    Matsuyama, M.3    Nishizawa, K.4    Nishi, Y.5    Sato, C.6
  • 72
    • 0023239962 scopus 로고
    • Site-specific phosphorylation induces disassembly of vimentin filaments in vitro
    • Inagaki M, Nishi Y, Nishizawa K, Matsuyama M, Sato C. Site-specific phosphorylation induces disassembly of vimentin filaments in vitro. Nature 328: 649-652, 1987.
    • (1987) Nature , vol.328 , pp. 649-652
    • Inagaki, M.1    Nishi, Y.2    Nishizawa, K.3    Matsuyama, M.4    Sato, C.5
  • 73
    • 0024473081 scopus 로고
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain. J Biol Chem 264: 18119-18127, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 18119-18127
    • Inagaki, M.1    Takahara, H.2    Nishi, Y.3    Sugawara, K.4    Sato, C.5
  • 74
    • 59649104201 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of vascular lumen formation
    • Iruela-Arispe ML, Davis GE. Cellular and molecular mechanisms of vascular lumen formation. Dev Cell 16: 222-231, 2009.
    • (2009) Dev Cell , vol.16 , pp. 222-231
    • Iruela-Arispe, M.L.1    Davis, G.E.2
  • 75
    • 34249682108 scopus 로고    scopus 로고
    • Novel functions of vimentin in cell adhesion, migration, and signaling
    • Ivaska J, Pallari HM, Nevo J, Eriksson JE. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp Cell Res 313: 2050-2062, 2007.
    • (2007) Exp Cell Res , vol.313 , pp. 2050-2062
    • Ivaska, J.1    Pallari, H.M.2    Nevo, J.3    Eriksson, J.E.4
  • 76
    • 33646004279 scopus 로고    scopus 로고
    • Regulatory mechanisms and functions of intermediate filaments: a study using site- and phosphorylation state-specific antibodies
    • Izawa I, Inagaki M. Regulatory mechanisms and functions of intermediate filaments: a study using site- and phosphorylation state-specific antibodies. Cancer Sci 97: 167-174, 2006.
    • (2006) Cancer Sci , vol.97 , pp. 167-174
    • Izawa, I.1    Inagaki, M.2
  • 77
    • 33746760588 scopus 로고    scopus 로고
    • Expression of membrane type-1 matrix metalloproteinase, MT1-MMP in human breast cancer and its impact on invasiveness of breast cancer cells
    • Jiang WG, Davies G, Martin TA, Parr C, Watkins G, Mason MD, Mansel RE. Expression of membrane type-1 matrix metalloproteinase, MT1-MMP in human breast cancer and its impact on invasiveness of breast cancer cells. Int J Mol Med 17: 583-590, 2006.
    • (2006) Int J Mol Med , vol.17 , pp. 583-590
    • Jiang, W.G.1    Davies, G.2    Martin, T.A.3    Parr, C.4    Watkins, G.5    Mason, M.D.6    Mansel, R.E.7
  • 78
    • 57049185877 scopus 로고    scopus 로고
    • Fluid shear stress modulates endothelial cell invasion into three-dimensional collagen matrices
    • Kang H, Bayless KJ, Kaunas R. Fluid shear stress modulates endothelial cell invasion into three-dimensional collagen matrices. Am J Physiol Heart Circ Physiol 295: H2087-H2097, 2008.
    • (2008) Am J Physiol Heart Circ Physiol , vol.295
    • Kang, H.1    Bayless, K.J.2    Kaunas, R.3
  • 79
    • 82755167748 scopus 로고    scopus 로고
    • Fluid shear stress and sphingosine 1-phosphate activate calpain to promote membrane type 1 matrix metalloproteinase (MT1-MMP) membrane translocation and endothelial invasion into three-dimensional collagen matrices
    • Kang H, Kwak HI, Kaunas R, Bayless KJ. Fluid shear stress and sphingosine 1-phosphate activate calpain to promote membrane type 1 matrix metalloproteinase (MT1-MMP) membrane translocation and endothelial invasion into three-dimensional collagen matrices. J Biol Chem 286: 42017-42026, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 42017-42026
    • Kang, H.1    Kwak, H.I.2    Kaunas, R.3    Bayless, K.J.4
  • 80
    • 0025469588 scopus 로고
    • Alpha-internexin, a novel neuronal intermediate filament protein, precedes the low molecular weight neurofilament protein (NF-L) in the developing rat brain
    • Kaplan MP, Chin SS, Fliegner KH, Liem RK. Alpha-internexin, a novel neuronal intermediate filament protein, precedes the low molecular weight neurofilament protein (NF-L) in the developing rat brain. J Neurosci 10: 2735-2748, 1990.
    • (1990) J Neurosci , vol.10 , pp. 2735-2748
    • Kaplan, M.P.1    Chin, S.S.2    Fliegner, K.H.3    Liem, R.K.4
  • 81
    • 0024566964 scopus 로고
    • Positivity to glial fibrillary acidic protein in bone, cartilage, and chordoma
    • Kasantikul V, Shuangshoti S. Positivity to glial fibrillary acidic protein in bone, cartilage, and chordoma. J Surg Oncol 41: 22-26, 1989.
    • (1989) J Surg Oncol , vol.41 , pp. 22-26
    • Kasantikul, V.1    Shuangshoti, S.2
  • 82
    • 84856443862 scopus 로고    scopus 로고
    • Synergistic regulation of angiogenic sprouting by biochemical factors and wall shear stress
    • Kaunas R, Kang H, Bayless KJ. Synergistic regulation of angiogenic sprouting by biochemical factors and wall shear stress. Cell Mol Bioeng 4: 547-559, 2011.
    • (2011) Cell Mol Bioeng , vol.4 , pp. 547-559
    • Kaunas, R.1    Kang, H.2    Bayless, K.J.3
  • 83
    • 67749091209 scopus 로고    scopus 로고
    • Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase
    • Kiely PA, Baillie GS, Barrett R, Buckley DA, Adams DR, Houslay MD, O'Connor R. Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-like growth factor I-mediated regulation of focal adhesion kinase. J Biol Chem 284: 20263-20274, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 20263-20274
    • Kiely, P.A.1    Baillie, G.S.2    Barrett, R.3    Buckley, D.A.4    Adams, D.R.5    Houslay, M.D.6    O'Connor, R.7
  • 84
    • 14844293473 scopus 로고    scopus 로고
    • RACK1-mediated integration of adhesion and insulin-like growth factor I (IGF-I) signaling and cell migration are defective in cells expressing an IGF-I receptor mutated at tyrosines 1250 and 1251
    • Kiely PA, Leahy M, O'Gorman D, O'Connor R. RACK1-mediated integration of adhesion and insulin-like growth factor I (IGF-I) signaling and cell migration are defective in cells expressing an IGF-I receptor mutated at tyrosines 1250 and 1251. J Biol Chem 280: 7624-7633, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 7624-7633
    • Kiely, P.A.1    Leahy, M.2    O'Gorman, D.3    O'Connor, R.4
  • 85
  • 87
    • 15044360781 scopus 로고    scopus 로고
    • The intermediate filament protein vimentin binds specifically to a recombinant integrin alpha2/beta1 cytoplasmic tail complex and co-localizes with native alpha2/beta1 in endothelial cell focal adhesions
    • Kreis S, Schonfeld HJ, Melchior C, Steiner B, Kieffer N. The intermediate filament protein vimentin binds specifically to a recombinant integrin alpha2/beta1 cytoplasmic tail complex and co-localizes with native alpha2/beta1 in endothelial cell focal adhesions. Exp Cell Res 305: 110-121, 2005.
    • (2005) Exp Cell Res , vol.305 , pp. 110-121
    • Kreis, S.1    Schonfeld, H.J.2    Melchior, C.3    Steiner, B.4    Kieffer, N.5
  • 88
    • 84865127296 scopus 로고    scopus 로고
    • Calpain-mediated vimentin cleavage occurs upstream of MT1-MMP membrane translocation to facilitate endothelial sprout initiation
    • Kwak HI, Kang H, Dave JM, Mendoza EA, Su SC, Maxwell SA, Bayless KJ. Calpain-mediated vimentin cleavage occurs upstream of MT1-MMP membrane translocation to facilitate endothelial sprout initiation. Angiogenesis 15: 287-303, 2012.
    • (2012) Angiogenesis , vol.15 , pp. 287-303
    • Kwak, H.I.1    Kang, H.2    Dave, J.M.3    Mendoza, E.A.4    Su, S.C.5    Maxwell, S.A.6    Bayless, K.J.7
  • 91
    • 0031281832 scopus 로고    scopus 로고
    • Expression of nuclear lamins in human tissues and cancer cell lines and transcription from the promoters of the lamin A/C and B1 genes
    • Lin F, Worman HJ. Expression of nuclear lamins in human tissues and cancer cell lines and transcription from the promoters of the lamin A/C and B1 genes. Exp Cell Res 236: 378-384, 1997.
    • (1997) Exp Cell Res , vol.236 , pp. 378-384
    • Lin, F.1    Worman, H.J.2
  • 93
    • 4444223559 scopus 로고    scopus 로고
    • Under stress, the absence of intermediate filaments from Muller cells in the retina has structural and functional consequences
    • Lundkvist A, Reichenbach A, Betsholtz C, Carmeliet P, Wolburg H, Pekny M. Under stress, the absence of intermediate filaments from Muller cells in the retina has structural and functional consequences. J Cell Sci 117: 3481-3488, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 3481-3488
    • Lundkvist, A.1    Reichenbach, A.2    Betsholtz, C.3    Carmeliet, P.4    Wolburg, H.5    Pekny, M.6
  • 94
    • 0032949408 scopus 로고    scopus 로고
    • Intermediate filaments in motion: observations of intermediate filaments in cells using green fluorescent protein-vimentin
    • Martys JL, Ho CL, Liem RK, Gundersen GG. Intermediate filaments in motion: observations of intermediate filaments in cells using green fluorescent protein-vimentin. Mol Biol Cell 10: 1289-1295, 1999.
    • (1999) Mol Biol Cell , vol.10 , pp. 1289-1295
    • Martys, J.L.1    Ho, C.L.2    Liem, R.K.3    Gundersen, G.G.4
  • 96
    • 0026046947 scopus 로고
    • Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell
    • Merdes A, Brunkener M, Horstmann H, Georgatos SD. Filensin: a new vimentin-binding, polymerization-competent, and membrane-associated protein of the lens fiber cell. J Cell Biol 115: 397-410, 1991.
    • (1991) J Cell Biol , vol.115 , pp. 397-410
    • Merdes, A.1    Brunkener, M.2    Horstmann, H.3    Georgatos, S.D.4
  • 97
    • 35048900480 scopus 로고    scopus 로고
    • 2+ influx- and phosphatidylinositol 3-kinase-mediated m-calpain activity for shear stress-induced endothelial cell polarity
    • 2+ influx- and phosphatidylinositol 3-kinase-mediated m-calpain activity for shear stress-induced endothelial cell polarity. Am J Physiol Cell Physiol 293: C1216-C1225, 2007.
    • (2007) Am J Physiol Cell Physiol , vol.293
    • Miyazaki, T.1    Honda, K.2    Ohata, H.3
  • 99
    • 33646088738 scopus 로고    scopus 로고
    • Cell surface expression of intermediate filament proteins vimentin and lamin B1 in human neutrophil spontaneous apoptosis
    • Moisan E, Girard D. Cell surface expression of intermediate filament proteins vimentin and lamin B1 in human neutrophil spontaneous apoptosis. J Leukoc Biol 79: 489-498, 2006.
    • (2006) J Leukoc Biol , vol.79 , pp. 489-498
    • Moisan, E.1    Girard, D.2
  • 100
    • 0021055582 scopus 로고
    • In vitro rapid organization of endothelial cells into capillary-like networks is promoted by collagen matrices
    • Montesano R, Orci L, Vassalli P. In vitro rapid organization of endothelial cells into capillary-like networks is promoted by collagen matrices. J Cell Biol 97: 1648-1652, 1983.
    • (1983) J Cell Biol , vol.97 , pp. 1648-1652
    • Montesano, R.1    Orci, L.2    Vassalli, P.3
  • 101
    • 0023412798 scopus 로고
    • Phorbol ester induces cultured endothelial cells to invade a fibrin matrix in the presence of fibrinolytic inhibitors
    • Montesano R, Pepper MS, Vassalli JD, Orci L. Phorbol ester induces cultured endothelial cells to invade a fibrin matrix in the presence of fibrinolytic inhibitors. J Cell Physiol 132: 509-516, 1987.
    • (1987) J Cell Physiol , vol.132 , pp. 509-516
    • Montesano, R.1    Pepper, M.S.2    Vassalli, J.D.3    Orci, L.4
  • 102
    • 52049092728 scopus 로고    scopus 로고
    • An optimized three-dimensional in vitro model for the analysis of angiogenesis
    • Nakatsu MN, Hughes CC. An optimized three-dimensional in vitro model for the analysis of angiogenesis. Methods Enzymol 443: 65-82, 2008.
    • (2008) Methods Enzymol , vol.443 , pp. 65-82
    • Nakatsu, M.N.1    Hughes, C.C.2
  • 103
    • 0019393171 scopus 로고
    • 2+-activated protease specific for the intermediate-sized filament protein vimentin in Ehrlich-ascites-tumour cells
    • 2+-activated protease specific for the intermediate-sized filament protein vimentin in Ehrlich-ascites-tumour cells. Eur J Biochem 116: 51-57, 1981.
    • (1981) Eur J Biochem , vol.116 , pp. 51-57
    • Nelson, W.J.1    Traub, P.2
  • 104
    • 0020490635 scopus 로고
    • 2+-activated proteinase specific for the intermediate filament proteins vimentin and desmin
    • 2+-activated proteinase specific for the intermediate filament proteins vimentin and desmin. J Biol Chem 257: 5544-5553, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 5544-5553
    • Nelson, W.J.1    Traub, P.2
  • 105
    • 0035794230 scopus 로고    scopus 로고
    • Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle
    • Newey SE, Howman EV, Ponting CP, Benson MA, Nawrotzki R, Loh NY, Davies KE, Blake DJ. Syncoilin, a novel member of the intermediate filament superfamily that interacts with alpha-dystrobrevin in skeletal muscle. J Biol Chem 276: 6645-6655, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 6645-6655
    • Newey, S.E.1    Howman, E.V.2    Ponting, C.P.3    Benson, M.A.4    Nawrotzki, R.5    Loh, N.Y.6    Davies, K.E.7    Blake, D.J.8
  • 106
    • 0025364195 scopus 로고
    • Growth of microvessels in serum-free matrix culture of rat aorta. A quantitative assay of angiogenesis in vitro
    • Nicosia RF, Ottinetti A. Growth of microvessels in serum-free matrix culture of rat aorta. A quantitative assay of angiogenesis in vitro. Lab Invest 63: 115-122, 1990.
    • (1990) Lab Invest , vol.63 , pp. 115-122
    • Nicosia, R.F.1    Ottinetti, A.2
  • 108
    • 49649112970 scopus 로고    scopus 로고
    • Impaired tyrosine phosphorylation of membrane type 1-matrix metalloproteinase reduces tumor cell proliferation in three-dimensional matrices and abrogates tumor growth in mice
    • Nyalendo C, Beaulieu E, Sartelet H, Michaud M, Fontaine N, Gingras D, Beliveau R. Impaired tyrosine phosphorylation of membrane type 1-matrix metalloproteinase reduces tumor cell proliferation in three-dimensional matrices and abrogates tumor growth in mice. Carcinogenesis 29: 1655-1664, 2008.
    • (2008) Carcinogenesis , vol.29 , pp. 1655-1664
    • Nyalendo, C.1    Beaulieu, E.2    Sartelet, H.3    Michaud, M.4    Fontaine, N.5    Gingras, D.6    Beliveau, R.7
  • 109
    • 34447522132 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration
    • Nyalendo C, Michaud M, Beaulieu E, Roghi C, Murphy G, Gingras D, Beliveau R. Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration. J Biol Chem 282: 15690-15699, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 15690-15699
    • Nyalendo, C.1    Michaud, M.2    Beaulieu, E.3    Roghi, C.4    Murphy, G.5    Gingras, D.6    Beliveau, R.7
  • 110
    • 43149087359 scopus 로고    scopus 로고
    • The function of filensin and phakinin in lens transparency
    • Oka M, Kudo H, Sugama N, Asami Y, Takehana M. The function of filensin and phakinin in lens transparency. Mol Vis 14: 815-822, 2008.
    • (2008) Mol Vis , vol.14 , pp. 815-822
    • Oka, M.1    Kudo, H.2    Sugama, N.3    Asami, Y.4    Takehana, M.5
  • 112
    • 0036712430 scopus 로고    scopus 로고
    • Beyond structure: do intermediate filaments modulate cell signalling?
    • Paramio JM, Jorcano JL. Beyond structure: do intermediate filaments modulate cell signalling? BioEssays 24: 836-844, 2002.
    • (2002) BioEssays , vol.24 , pp. 836-844
    • Paramio, J.M.1    Jorcano, J.L.2
  • 113
    • 14644404885 scopus 로고    scopus 로고
    • Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve
    • Perlson E, Hanz S, Ben-Yaakov K, Segal-Ruder Y, Seger R, Fainzilber M. Vimentin-dependent spatial translocation of an activated MAP kinase in injured nerve. Neuron 45: 715-726, 2005.
    • (2005) Neuron , vol.45 , pp. 715-726
    • Perlson, E.1    Hanz, S.2    Ben-Yaakov, K.3    Segal-Ruder, Y.4    Seger, R.5    Fainzilber, M.6
  • 115
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M, Nakagawa J, Doree M, Labbe JC, Nigg EA. In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61: 591-602, 1990.
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 116
    • 0034494961 scopus 로고    scopus 로고
    • Focal adhesions: structure and dynamics
    • Petit V, Thiery JP. Focal adhesions: structure and dynamics. Biol Cell 92: 477-494, 2000.
    • (2000) Biol Cell , vol.92 , pp. 477-494
    • Petit, V.1    Thiery, J.P.2
  • 118
    • 0032487522 scopus 로고    scopus 로고
    • Rapid movements of vimentin on microtubule tracks: kinesin-dependent assembly of intermediate filament networks
    • Prahlad V, Yoon M, Moir RD, Vale RD, Goldman RD. Rapid movements of vimentin on microtubule tracks: kinesin-dependent assembly of intermediate filament networks. J Cell Biol 143: 159-170, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 159-170
    • Prahlad, V.1    Yoon, M.2    Moir, R.D.3    Vale, R.D.4    Goldman, R.D.5
  • 119
    • 27644473229 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition
    • Radisky DC. Epithelial-mesenchymal transition. J Cell Sci 118: 4325-4326, 2005.
    • (2005) J Cell Sci , vol.118 , pp. 4325-4326
    • Radisky, D.C.1
  • 120
    • 0038103790 scopus 로고    scopus 로고
    • Observations on the use of the avian chorioallantoic membrane (CAM) model in investigations into angiogenesis
    • Richardson M, Singh G. Observations on the use of the avian chorioallantoic membrane (CAM) model in investigations into angiogenesis. Current Drug Targets Cardiovasc Haematol Disord 3: 155-185, 2003.
    • (2003) Current Drug Targets Cardiovasc Haematol Disord , vol.3 , pp. 155-185
    • Richardson, M.1    Singh, G.2
  • 121
    • 80052267874 scopus 로고    scopus 로고
    • Vimentin in cancer and its potential as a molecular target for cancer therapy
    • Satelli A, Li S. Vimentin in cancer and its potential as a molecular target for cancer therapy. Cell Mol Life Sci 68: 3033-3046, 2011.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3033-3046
    • Satelli, A.1    Li, S.2
  • 122
    • 20044387216 scopus 로고    scopus 로고
    • Roles of membrane-type matrix metalloproteinase-1 in tumor invasion and metastasis
    • Sato H, Takino T, Miyamori H. Roles of membrane-type matrix metalloproteinase-1 in tumor invasion and metastasis. Cancer Sci 96: 212-217, 2005.
    • (2005) Cancer Sci , vol.96 , pp. 212-217
    • Sato, H.1    Takino, T.2    Miyamori, H.3
  • 126
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion
    • Seiki M. Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion. Cancer Lett 194: 1-11, 2003.
    • (2003) Cancer Lett , vol.194 , pp. 1-11
    • Seiki, M.1
  • 127
    • 27544515088 scopus 로고    scopus 로고
    • Calcium signaling in cancer and vitamin D
    • Sergeev IN. Calcium signaling in cancer and vitamin D. J Steroid Biochem Mol Biol 97: 145-151, 2005.
    • (2005) J Steroid Biochem Mol Biol , vol.97 , pp. 145-151
    • Sergeev, I.N.1
  • 128
    • 22344434300 scopus 로고    scopus 로고
    • Conditional knockout of focal adhesion kinase in endothelial cells reveals its role in angiogenesis and vascular development in late embryogenesis
    • Shen TL, Park AY, Alcaraz A, Peng X, Jang I, Koni P, Flavell RA, Gu H, Guan JL. Conditional knockout of focal adhesion kinase in endothelial cells reveals its role in angiogenesis and vascular development in late embryogenesis. J Cell Biol 169: 941-952, 2005.
    • (2005) J Cell Biol , vol.169 , pp. 941-952
    • Shen, T.L.1    Park, A.Y.2    Alcaraz, A.3    Peng, X.4    Jang, I.5    Koni, P.6    Flavell, R.A.7    Gu, H.8    Guan, J.L.9
  • 129
    • 0036403823 scopus 로고    scopus 로고
    • Deletion mutagenesis of the amino-terminal head domain of vimentin reveals dispensability of large internal regions for intermediate filament assembly and stability
    • Shoeman RL, Hartig R, Berthel M, Traub P. Deletion mutagenesis of the amino-terminal head domain of vimentin reveals dispensability of large internal regions for intermediate filament assembly and stability. Exp Cell Res 279: 344-353, 2002.
    • (2002) Exp Cell Res , vol.279 , pp. 344-353
    • Shoeman, R.L.1    Hartig, R.2    Berthel, M.3    Traub, P.4
  • 131
    • 33746491305 scopus 로고    scopus 로고
    • Calpain-2 regulation of VEGF-mediated angiogenesis
    • Su Y, Cui Z, Li Z, Block ER. Calpain-2 regulation of VEGF-mediated angiogenesis. FASEB J 20: 1443-1451, 2006.
    • (2006) FASEB J , vol.20 , pp. 1443-1451
    • Su, Y.1    Cui, Z.2    Li, Z.3    Block, E.R.4
  • 133
    • 0020825122 scopus 로고
    • Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments
    • Traub P, Vorgias CE. Involvement of the N-terminal polypeptide of vimentin in the formation of intermediate filaments. J Cell Sci 63: 43-67, 1983.
    • (1983) J Cell Sci , vol.63 , pp. 43-67
    • Traub, P.1    Vorgias, C.E.2
  • 134
    • 0022253980 scopus 로고
    • Expression of neurofilament antigens by normal and neoplastic human adrenal chromaffin cells
    • Trojanowski JQ, Lee VM. Expression of neurofilament antigens by normal and neoplastic human adrenal chromaffin cells. New Eng J Med 313: 101-104, 1985.
    • (1985) New Eng J Med , vol.313 , pp. 101-104
    • Trojanowski, J.Q.1    Lee, V.M.2
  • 135
    • 0347513188 scopus 로고    scopus 로고
    • The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress
    • Tsuruta D, Jones JC. The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress. J Cell Sci 116: 4977-4984, 2003.
    • (2003) J Cell Sci , vol.116 , pp. 4977-4984
    • Tsuruta, D.1    Jones, J.C.2
  • 138
    • 0034467062 scopus 로고    scopus 로고
    • Citrullination: a small change for a protein with great consequences for rheumatoid arthritis
    • van Venrooij WJ, Pruijn GJ. Citrullination: a small change for a protein with great consequences for rheumatoid arthritis. Arthritis Res 2: 249-251, 2000.
    • (2000) Arthritis Res , vol.2 , pp. 249-251
    • van Venrooij, W.J.1    Pruijn, G.J.2
  • 139
    • 0003127656 scopus 로고    scopus 로고
    • A novel, quantitative model for study of endothelial cell migration and sprout formation within three-dimensional collagen matrices
    • Vernon RB, Sage EH. A novel, quantitative model for study of endothelial cell migration and sprout formation within three-dimensional collagen matrices. Microvasc Res 57: 118-133, 1999.
    • (1999) Microvasc Res , vol.57 , pp. 118-133
    • Vernon, R.B.1    Sage, E.H.2
  • 140
    • 0034448336 scopus 로고    scopus 로고
    • Studying vascular development in the zebrafish
    • Vogel AM, Weinstein BM. Studying vascular development in the zebrafish. Trends Cardiovasc Med 10: 352-360, 2000.
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 352-360
    • Vogel, A.M.1    Weinstein, B.M.2
  • 142
    • 0031947966 scopus 로고    scopus 로고
    • The thrombospondin receptor CD47 (IAP) modulates and associates with alpha2 beta1 integrin in vascular smooth muscle cells
    • Wang XQ, Frazier WA. The thrombospondin receptor CD47 (IAP) modulates and associates with alpha2 beta1 integrin in vascular smooth muscle cells. Mol Biol Cell 9: 865-874, 1998.
    • (1998) Mol Biol Cell , vol.9 , pp. 865-874
    • Wang, X.Q.1    Frazier, W.A.2
  • 145
    • 0023110624 scopus 로고
    • Infantile neurodegenerative disease with neuronal accumulation of phosphorylated neurofilaments
    • Wiley CA, Love S, Skoglund RR, Lampert PW. Infantile neurodegenerative disease with neuronal accumulation of phosphorylated neurofilaments. Acta Neuropathol 72: 369-376, 1987.
    • (1987) Acta Neuropathol , vol.72 , pp. 369-376
    • Wiley, C.A.1    Love, S.2    Skoglund, R.R.3    Lampert, P.W.4
  • 146
    • 83355166955 scopus 로고    scopus 로고
    • Phosphorylation of membrane type 1-matrix metalloproteinase (MT1-MMP) and its vesicle-associated membrane protein 7 (VAMP7)-dependent trafficking facilitate cell invasion and migration
    • Williams KC, Coppolino MG. Phosphorylation of membrane type 1-matrix metalloproteinase (MT1-MMP) and its vesicle-associated membrane protein 7 (VAMP7)-dependent trafficking facilitate cell invasion and migration. J Biol Chem 286: 43405-43416, 2011.
    • (2011) J Biol Chem , vol.286 , pp. 43405-43416
    • Williams, K.C.1    Coppolino, M.G.2
  • 147
    • 20344391920 scopus 로고    scopus 로고
    • Differentiation and proliferation of endothelial progenitor cells from canine peripheral blood mononuclear cells
    • Wu H, Riha GM, Yang H, Li M, Yao Q, Chen C. Differentiation and proliferation of endothelial progenitor cells from canine peripheral blood mononuclear cells. J Surg Res 126: 193-198, 2005.
    • (2005) J Surg Res , vol.126 , pp. 193-198
    • Wu, H.1    Riha, G.M.2    Yang, H.3    Li, M.4    Yao, Q.5    Chen, C.6
  • 149
    • 0025906619 scopus 로고
    • Phosphorylation of keratin intermediate filaments by protein kinase C, by calmodulin-dependent protein kinase and by cAMP-dependent protein kinase
    • Yano T, Tokui T, Nishi Y, Nishizawa K, Shibata M, Kikuchi K, Tsuiki S, Yamauchi T, Inagaki M. Phosphorylation of keratin intermediate filaments by protein kinase C, by calmodulin-dependent protein kinase and by cAMP-dependent protein kinase. Eur J Biochem 197: 281-290, 1991.
    • (1991) Eur J Biochem , vol.197 , pp. 281-290
    • Yano, T.1    Tokui, T.2    Nishi, Y.3    Nishizawa, K.4    Shibata, M.5    Kikuchi, K.6    Tsuiki, S.7    Yamauchi, T.8    Inagaki, M.9
  • 150
    • 0032487443 scopus 로고    scopus 로고
    • Motile properties of vimentin intermediate filament networks in living cells
    • Yoon M, Moir RD, Prahlad V, Goldman RD. Motile properties of vimentin intermediate filament networks in living cells. J Cell Biol 143: 147-157, 1998.
    • (1998) J Cell Biol , vol.143 , pp. 147-157
    • Yoon, M.1    Moir, R.D.2    Prahlad, V.3    Goldman, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.