메뉴 건너뛰기




Volumn 295, Issue 4, 2008, Pages

Mechanical loading by fluid shear is sufficient to alter the cytoskeletal composition of osteoblastic cells

Author keywords

actinin; Cytoskeleton; Filamin; Human fetal osteoblasts; MC3T3 E1

Indexed keywords

ALPHA ACTININ; FILAMIN; MONOMER; STRUCTURAL PROTEIN; TALIN; VIMENTIN;

EID: 57049185878     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00509.2007     Document Type: Article
Times cited : (49)

References (65)
  • 1
    • 0035059024 scopus 로고    scopus 로고
    • The production of nitric oxide and prostaglandin E(2) by primary bone cells is shear stress dependent
    • Bakker AD, Soejima K, Klein-Nulend J, Burger EH. The production of nitric oxide and prostaglandin E(2) by primary bone cells is shear stress dependent. J Biomech 34: 671-677, 2001.
    • (2001) J Biomech , vol.34 , pp. 671-677
    • Bakker, A.D.1    Soejima, K.2    Klein-Nulend, J.3    Burger, E.H.4
  • 2
    • 0019741614 scopus 로고
    • The application of scanning electron microscopy to the study of the cytoskeleton of cells in culture
    • Bell PB Jr. The application of scanning electron microscopy to the study of the cytoskeleton of cells in culture. Scan Electron Microsc: 139-157, 1981.
    • (1981) Scan Electron Microsc , pp. 139-157
    • Bell Jr., P.B.1
  • 3
    • 0001677717 scopus 로고
    • Controlling the false discovery rate: A practical and powerful approach to multiple testing
    • Benjamini Y, Hochberg Y. Controlling the false discovery rate: a practical and powerful approach to multiple testing. J Royal Stat Soc Series B 57: 290-300, 1995.
    • (1995) J Royal Stat Soc Series B , vol.57 , pp. 290-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 5
    • 0032882048 scopus 로고    scopus 로고
    • Progressive association of a "soluble" glycolytic enzyme with the detergent-insoluble cytoskeleton during in vitro morphogenesis of MDCK epithelial cells
    • Cao F, Yanagihara N, Burke JM. Progressive association of a "soluble" glycolytic enzyme with the detergent-insoluble cytoskeleton during in vitro morphogenesis of MDCK epithelial cells. Cell Motil Cytoskeleton 44: 133-142, 1999.
    • (1999) Cell Motil Cytoskeleton , vol.44 , pp. 133-142
    • Cao, F.1    Yanagihara, N.2    Burke, J.M.3
  • 6
    • 0036109559 scopus 로고    scopus 로고
    • Single cell mechanotransduction and its modulation analyzed by atomic force microscope indentation
    • Charras GT, Horton MA. Single cell mechanotransduction and its modulation analyzed by atomic force microscope indentation. Biophys J 82: 2970-2981, 2002.
    • (2002) Biophys J , vol.82 , pp. 2970-2981
    • Charras, G.T.1    Horton, M.A.2
  • 8
    • 0033046706 scopus 로고    scopus 로고
    • MEKK1 interacts with alpha-actinin and localizes to stress fibers and focal adhesions
    • Christerson LB, Vanderbilt CA, Cobb MH. MEKK1 interacts with alpha-actinin and localizes to stress fibers and focal adhesions. Cell Motil Cytoskeleton 43: 186-198, 1999.
    • (1999) Cell Motil Cytoskeleton , vol.43 , pp. 186-198
    • Christerson, L.B.1    Vanderbilt, C.A.2    Cobb, M.H.3
  • 10
    • 0037033117 scopus 로고    scopus 로고
    • Interaction of p38 and Sp1 in a mechanical force-induced, beta 1 integrin-mediated transcriptional circuit that regulates the actin-binding protein filamin-A
    • D'Addario M, Arora PD, Ellen RP, McCulloch CAG. Interaction of p38 and Sp1 in a mechanical force-induced, beta 1 integrin-mediated transcriptional circuit that regulates the actin-binding protein filamin-A. J Biol Chem 277: 47541-47550, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 47541-47550
    • D'Addario, M.1    Arora, P.D.2    Ellen, R.P.3    McCulloch, C.A.G.4
  • 11
    • 0035943713 scopus 로고    scopus 로고
    • Cytoprotection against mechanical forces delivered through beta 1 integrins requires induction of filamin A
    • D'Addario M, Arora PD, Fan J, Ganss B, Ellen RP, McCulloch CAG. Cytoprotection against mechanical forces delivered through beta 1 integrins requires induction of filamin A. J Biol Chem 276: 31969-31977, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 31969-31977
    • D'Addario, M.1    Arora, P.D.2    Fan, J.3    Ganss, B.4    Ellen, R.P.5    McCulloch, C.A.G.6
  • 13
    • 33750069729 scopus 로고    scopus 로고
    • A Direct Interaction between actin and vimentin filaments mediated by the tail domain of vimentin
    • Esue O, Carson AA, Tseng Y, Wirtz D. A Direct Interaction between actin and vimentin filaments mediated by the tail domain of vimentin. J Biol Chem 281: 30393-30399, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 30393-30399
    • Esue, O.1    Carson, A.A.2    Tseng, Y.3    Wirtz, D.4
  • 14
    • 13844313879 scopus 로고    scopus 로고
    • Housekeeping proteins: A preliminary study illustrating some limitations as useful references in protein expression studies
    • Ferguson RE, Carroll HP, Harris A, Maher ER, Selby PJ, Banks RE. Housekeeping proteins: a preliminary study illustrating some limitations as useful references in protein expression studies. Proteomics 5: 566-571, 2005.
    • (2005) Proteomics , vol.5 , pp. 566-571
    • Ferguson, R.E.1    Carroll, H.P.2    Harris, A.3    Maher, E.R.4    Selby, P.J.5    Banks, R.E.6
  • 15
    • 0029011651 scopus 로고
    • On the possible role of cytoskeletal filamentous networks in intracellular signaling: An approach based on percolation
    • Forgacs G. On the possible role of cytoskeletal filamentous networks in intracellular signaling: an approach based on percolation. J Cell Sci 108: 2131-2143, 1995.
    • (1995) J Cell Sci , vol.108 , pp. 2131-2143
    • Forgacs, G.1
  • 16
    • 17644402480 scopus 로고    scopus 로고
    • Phosphoinositide binding regulates alpha-actinin dynamics: Mechanism for modulating cytoskeletal remodeling
    • Fraley TS, Pereira CB, Tran TC, Singleton C, Greenwood JA. Phosphoinositide binding regulates alpha-actinin dynamics: mechanism for modulating cytoskeletal remodeling. J Biol Chem 280: 15479-15482, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 15479-15482
    • Fraley, T.S.1    Pereira, C.B.2    Tran, T.C.3    Singleton, C.4    Greenwood, J.A.5
  • 17
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith CG, Yamada KM, Sheetz MP. The relationship between force and focal complex development. J Cell Biol 159: 695-705, 2002.
    • (2002) J Cell Biol , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 19
    • 0242361579 scopus 로고    scopus 로고
    • Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation
    • Giannone G, Jiang G, Sutton DH, Critchley DR, Sheetz MP. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J Cell Biol 163: 409-419, 2003.
    • (2003) J Cell Biol , vol.163 , pp. 409-419
    • Giannone, G.1    Jiang, G.2    Sutton, D.H.3    Critchley, D.R.4    Sheetz, M.P.5
  • 21
    • 0031020163 scopus 로고    scopus 로고
    • Calcium ions and tyrosine phosphorylation interact coordinately with actin to regulate cytoprotective responses to stretching
    • Glogauer M, Arora P, Yao G, Sokholov I, Ferrier J, McCulloch C. Calcium ions and tyrosine phosphorylation interact coordinately with actin to regulate cytoprotective responses to stretching. J Cell Sci 110: 11-21, 1997.
    • (1997) J Cell Sci , vol.110 , pp. 11-21
    • Glogauer, M.1    Arora, P.2    Yao, G.3    Sokholov, I.4    Ferrier, J.5    McCulloch, C.6
  • 22
    • 0031817205 scopus 로고    scopus 로고
    • Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy
    • Goldmann WH, Galneder R, Ludwig M, Xu W, Adamson ED, Wang N, Ezzell RM. Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy. Exp Cell Res 239: 235-242, 1998.
    • (1998) Exp Cell Res , vol.239 , pp. 235-242
    • Goldmann, W.H.1    Galneder, R.2    Ludwig, M.3    Xu, W.4    Adamson, E.D.5    Wang, N.6    Ezzell, R.M.7
  • 23
    • 2942607517 scopus 로고    scopus 로고
    • Leukocyte-specific protein 1 targets the ERK/MAP kinase scaffold protein KSR and MEK1 and ERK2 to the actin cytoskeleton
    • Harrison RE, Sikorski BA, Jongstra J. Leukocyte-specific protein 1 targets the ERK/MAP kinase scaffold protein KSR and MEK1 and ERK2 to the actin cytoskeleton. J Cell Sci 117: 2151-2157, 2004.
    • (2004) J Cell Sci , vol.117 , pp. 2151-2157
    • Harrison, R.E.1    Sikorski, B.A.2    Jongstra, J.3
  • 25
    • 40949165235 scopus 로고    scopus 로고
    • Actin stress fibers transmit and focus force to activate mechanosensitive channels
    • Hayakawa K, Tatsumi H, Sokabe M. Actin stress fibers transmit and focus force to activate mechanosensitive channels. J Cell Sci 121: 496-503, 2008.
    • (2008) J Cell Sci , vol.121 , pp. 496-503
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 26
    • 34249661685 scopus 로고    scopus 로고
    • Adaptation of cellular mechanical behavior to mechanical loading for osteoblastic cells
    • Jaasma MJ, Jackson WM, Tang RY, Keaveny TM. Adaptation of cellular mechanical behavior to mechanical loading for osteoblastic cells. J Biomech 40: 1938-1945, 2007.
    • (2007) J Biomech , vol.40 , pp. 1938-1945
    • Jaasma, M.J.1    Jackson, W.M.2    Tang, R.Y.3    Keaveny, T.M.4
  • 27
    • 57049089619 scopus 로고    scopus 로고
    • Over-expression of alpha-actinin with a GFP fusion protein is sufficient to increase whole-cell stiffness in human osteoblasts
    • In press
    • Jackson WM, Jaasma MJ, Baik AB, Keaveny TM. Over-expression of alpha-actinin with a GFP fusion protein is sufficient to increase whole-cell stiffness in human osteoblasts. Annals Biomed Eng In press.
    • Annals Biomed Eng
    • Jackson, W.M.1    Jaasma, M.J.2    Baik, A.B.3    Keaveny, T.M.4
  • 29
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signaling: Component localization and mechanical coupling
    • Janmey PA. The cytoskeleton and cell signaling: component localization and mechanical coupling. Physiol Rev 78: 763-781, 1998.
    • (1998) Physiol Rev , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 30
    • 0025803565 scopus 로고
    • Mechanical properties of cytoskeletal polymers
    • Janmey PA. Mechanical properties of cytoskeletal polymers. Curr Opin Cell Biol 3: 4-11, 1991.
    • (1991) Curr Opin Cell Biol , vol.3 , pp. 4-11
    • Janmey, P.A.1
  • 31
    • 0025765110 scopus 로고
    • Viscoelastic properties of vimentin compared with other filamentous biopolymer networks
    • Janmey PA, Euteneuer U, Traub P, Schliwa M. Viscoelastic properties of vimentin compared with other filamentous biopolymer networks. J Cell Biol 113: 155-160, 1991.
    • (1991) J Cell Biol , vol.113 , pp. 155-160
    • Janmey, P.A.1    Euteneuer, U.2    Traub, P.3    Schliwa, M.4
  • 32
    • 0025366458 scopus 로고
    • Resemblance of actin-binding protein/actin gels to covalently cross-linked networks
    • Janmey PA, Hvidt S, Lamb J, Stossel TP. Resemblance of actin-binding protein/actin gels to covalently cross-linked networks. Nature 345: 89-92, 1990.
    • (1990) Nature , vol.345 , pp. 89-92
    • Janmey, P.A.1    Hvidt, S.2    Lamb, J.3    Stossel, T.P.4
  • 33
    • 0034065138 scopus 로고    scopus 로고
    • Partners in protection: Interdependence of cytoskeleton and plasma membrane in adaptations to applied forces
    • Ko KS, McCulloch CA. Partners in protection: interdependence of cytoskeleton and plasma membrane in adaptations to applied forces. J Membr Biol 174: 85-95, 2000.
    • (2000) J Membr Biol , vol.174 , pp. 85-95
    • Ko, K.S.1    McCulloch, C.A.2
  • 34
    • 0034812535 scopus 로고    scopus 로고
    • Intercellular mechanotransduction: Cellular circuits that coordinate tissue responses to mechanical loading
    • Ko KS, McCulloch CAG. Intercellular mechanotransduction: cellular circuits that coordinate tissue responses to mechanical loading. Biochem Biophys Res Commun 285: 1077-1083, 2001.
    • (2001) Biochem Biophys Res Commun , vol.285 , pp. 1077-1083
    • Ko, K.S.1    McCulloch, C.A.G.2
  • 35
    • 20444389065 scopus 로고    scopus 로고
    • Fluid flow stimulates expression of osteopontin and bone sialoprotein by bone marrow stromal cells in a temporally dependent manner
    • Kreke MR, Huckle WR, Goldstein AS. Fluid flow stimulates expression of osteopontin and bone sialoprotein by bone marrow stromal cells in a temporally dependent manner. Bone 36: 1047-1055, 2005.
    • (2005) Bone , vol.36 , pp. 1047-1055
    • Kreke, M.R.1    Huckle, W.R.2    Goldstein, A.S.3
  • 36
    • 34948844539 scopus 로고    scopus 로고
    • Time-dependent deformations in bone cells exposed to fluid flow in vitro: Investigating the role of cellular deformation in fluid flow-induced signaling
    • Kwon RY, Jacobs CR. Time-dependent deformations in bone cells exposed to fluid flow in vitro: investigating the role of cellular deformation in fluid flow-induced signaling. J Biomech 40: 3162-3168, 2007.
    • (2007) J Biomech , vol.40 , pp. 3162-3168
    • Kwon, R.Y.1    Jacobs, C.R.2
  • 37
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 38
    • 0021711645 scopus 로고
    • Ultrastructural localization of alpha-actinin and filamin in cultured cells with the immunogold staining (IGS) method
    • Langanger G, de Mey J, Moeremans M, Daneels G, de Brabander M, Small JV. Ultrastructural localization of alpha-actinin and filamin in cultured cells with the immunogold staining (IGS) method. J Cell Biol 99: 1324-1334, 1984.
    • (1984) J Cell Biol , vol.99 , pp. 1324-1334
    • Langanger, G.1    de Mey, J.2    Moeremans, M.3    Daneels, G.4    de Brabander, M.5    Small, J.V.6
  • 39
    • 33744509705 scopus 로고    scopus 로고
    • Ballistic intracellular nanorheology reveals ROCK-hard cytoplasmic stiffening response to fluid flow
    • Lee JS, Panorchan P, Hale CM, Khatau SB, Kole TP, Tseng Y, Wirtz D. Ballistic intracellular nanorheology reveals ROCK-hard cytoplasmic stiffening response to fluid flow. J Cell Sci 119: 1760-1768, 2006.
    • (2006) J Cell Sci , vol.119 , pp. 1760-1768
    • Lee, J.S.1    Panorchan, P.2    Hale, C.M.3    Khatau, S.B.4    Kole, T.P.5    Tseng, Y.6    Wirtz, D.7
  • 40
    • 0022160653 scopus 로고
    • The elongation and orientation of cultured endothelial cells in response to shear stress
    • Levesque MJ, Nerem RM. The elongation and orientation of cultured endothelial cells in response to shear stress. J Biomech Eng 107: 341-347, 1985.
    • (1985) J Biomech Eng , vol.107 , pp. 341-347
    • Levesque, M.J.1    Nerem, R.M.2
  • 41
    • 0026703756 scopus 로고
    • Preservation and visualization of molecular structure in detergent-extracted whole mounts of cultured cells
    • Lindroth M, Bell PB Jr, Fredriksson BA, and Liu XD. Preservation and visualization of molecular structure in detergent-extracted whole mounts of cultured cells. Microsc Res Tech 22: 130-150, 1992.
    • (1992) Microsc Res Tech , vol.22 , pp. 130-150
    • Lindroth, M.1    Bell Jr, P.B.2    Fredriksson, B.A.3    Liu, X.D.4
  • 42
    • 0010483627 scopus 로고
    • Microfilament organization and actin-binding proteins
    • edited by Hesketh JE and Pryme IF. Greenwich: JAI
    • Maciver SK. Microfilament organization and actin-binding proteins. In: The Cytoskeleton, edited by Hesketh JE and Pryme IF. Greenwich: JAI, 1995, p. 1-45.
    • (1995) The Cytoskeleton , pp. 1-45
    • Maciver, S.K.1
  • 45
    • 0035062331 scopus 로고    scopus 로고
    • Osteoblasts respond to pulsatile fluid flow with short-term increases in PGE2 but no change in mineralization
    • Nauman EA, Satcher RL, Keaveny TM, Halloran BP, Bikle DD. Osteoblasts respond to pulsatile fluid flow with short-term increases in PGE2 but no change in mineralization. J Appl Physiol 90: 1849-1854, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 1849-1854
    • Nauman, E.A.1    Satcher, R.L.2    Keaveny, T.M.3    Halloran, B.P.4    Bikle, D.D.5
  • 46
    • 1342283036 scopus 로고    scopus 로고
    • Fluid shear stress induction of COX-2 protein and prostaglandin release in cultured MC3T3-E1 osteoblasts does not require intact microfilaments or microtubules
    • Norvell SM, Ponik SM, Bowen DK, Gerard R, Pavalko FM. Fluid shear stress induction of COX-2 protein and prostaglandin release in cultured MC3T3-E1 osteoblasts does not require intact microfilaments or microtubules. J Appl Physiol 96: 957-966, 2004.
    • (2004) J Appl Physiol , vol.96 , pp. 957-966
    • Norvell, S.M.1    Ponik, S.M.2    Bowen, D.K.3    Gerard, R.4    Pavalko, F.M.5
  • 47
    • 0023850743 scopus 로고
    • On the elasticity of cytoskeletal networks
    • Nossal R. On the elasticity of cytoskeletal networks. Biophys J 53: 349-359, 1988.
    • (1988) Biophys J , vol.53 , pp. 349-359
    • Nossal, R.1
  • 50
    • 33846560757 scopus 로고    scopus 로고
    • Osteoblasts and osteocytes respond differently to oscillatory and unidirectional fluid flow profiles
    • Ponik SM, Triplett JW, Pavalko FM. Osteoblasts and osteocytes respond differently to oscillatory and unidirectional fluid flow profiles. J Cell Biochem 100: 794-807, 2007.
    • (2007) J Cell Biochem , vol.100 , pp. 794-807
    • Ponik, S.M.1    Triplett, J.W.2    Pavalko, F.M.3
  • 52
    • 0029859177 scopus 로고    scopus 로고
    • The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development
    • Rivero F, Koppel B, Peracino B, Bozzaro S, Siegert F, Weijer CJ, Schleicher M, Albrecht R, Noegel AA. The role of the cortical cytoskeleton: F-actin crosslinking proteins protect against osmotic stress, ensure cell size, cell shape and motility, and contribute to phagocytosis and development. J Cell Sci 109: 2679-2691, 1996.
    • (1996) J Cell Sci , vol.109 , pp. 2679-2691
    • Rivero, F.1    Koppel, B.2    Peracino, B.3    Bozzaro, S.4    Siegert, F.5    Weijer, C.J.6    Schleicher, M.7    Albrecht, R.8    Noegel, A.A.9
  • 53
    • 0034127331 scopus 로고    scopus 로고
    • Drug-induced changes of cytoskeletal structure and mechanics in fibroblasts: An atomic force microscopy study
    • Rotsch C, Radmacher M. Drug-induced changes of cytoskeletal structure and mechanics in fibroblasts: an atomic force microscopy study. Biophys J 78: 520-535, 2000.
    • (2000) Biophys J , vol.78 , pp. 520-535
    • Rotsch, C.1    Radmacher, M.2
  • 54
    • 0036348974 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase associates with actin filaments in serum deprived NIH 3T3 cells only
    • Schmitz HD, Bereiter-Hahn J. Glyceraldehyde-3-phosphate dehydrogenase associates with actin filaments in serum deprived NIH 3T3 cells only. Cell Biol Int 26: 155-164, 2002.
    • (2002) Cell Biol Int , vol.26 , pp. 155-164
    • Schmitz, H.D.1    Bereiter-Hahn, J.2
  • 55
    • 0031562685 scopus 로고    scopus 로고
    • Strain reorganizes focal adhesions and cytoskeleton in cultured airway smooth muscle cells
    • Smith PG, Garcia R, Kogerman L. Strain reorganizes focal adhesions and cytoskeleton in cultured airway smooth muscle cells. Exp Cell Res 232: 127-136, 1997.
    • (1997) Exp Cell Res , vol.232 , pp. 127-136
    • Smith, P.G.1    Garcia, R.2    Kogerman, L.3
  • 57
    • 0035816209 scopus 로고    scopus 로고
    • Micromechanics and ultrastructure of actin filament networks crosslinked by human fascin: A comparison with alpha-actinin
    • Tseng Y, Fedorov E, McCaffery JM, Almo SC, Wirtz D. Micromechanics and ultrastructure of actin filament networks crosslinked by human fascin: a comparison with alpha-actinin. J Mol Biol 310: 351-366, 2001.
    • (2001) J Mol Biol , vol.310 , pp. 351-366
    • Tseng, Y.1    Fedorov, E.2    McCaffery, J.M.3    Almo, S.C.4    Wirtz, D.5
  • 59
    • 0037067679 scopus 로고    scopus 로고
    • Functional synergy of actin filament cross-linking proteins
    • Tseng Y, Schafer BW, Almo SC, Wirtz D. Functional synergy of actin filament cross-linking proteins. J Biol Chem 277: 25609-25616, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 25609-25616
    • Tseng, Y.1    Schafer, B.W.2    Almo, S.C.3    Wirtz, D.4
  • 60
    • 0028265522 scopus 로고
    • Cross-linker dynamics determine the mechanical properties of actin gels
    • Wachsstock DH, Schwarz WH, Pollard TD. Cross-linker dynamics determine the mechanical properties of actin gels. Biophys J 66: 801-809, 1994.
    • (1994) Biophys J , vol.66 , pp. 801-809
    • Wachsstock, D.H.1    Schwarz, W.H.2    Pollard, T.D.3
  • 61
    • 0031878403 scopus 로고    scopus 로고
    • Mechanical interactions among cytoskeletal filaments
    • Wang N. Mechanical interactions among cytoskeletal filaments. Hypertension 32: 162-165, 1998.
    • (1998) Hypertension , vol.32 , pp. 162-165
    • Wang, N.1
  • 62
    • 0028386524 scopus 로고
    • A model for the excitation of osteocytes by mechanical loading-induced bone fluid shear stresses
    • Weinbaum S, Cowin SC, Zeng Y. A model for the excitation of osteocytes by mechanical loading-induced bone fluid shear stresses. J Biomech 27: 339-360, 1994.
    • (1994) J Biomech , vol.27 , pp. 339-360
    • Weinbaum, S.1    Cowin, S.C.2    Zeng, Y.3
  • 63
    • 0034680846 scopus 로고    scopus 로고
    • Strain hardening of actin filament networks. Regulation by the dynamic cross-linking protein alpha-actinin
    • Xu J, Tseng Y, Wirtz D. Strain hardening of actin filament networks. Regulation by the dynamic cross-linking protein alpha-actinin. J Biol Chem 275: 35886-35892, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 35886-35892
    • Xu, J.1    Tseng, Y.2    Wirtz, D.3
  • 64
    • 0032540368 scopus 로고    scopus 로고
    • Dynamic cross-linking by alpha-actinin determines the mechanical properties of actin filament networks
    • Xu J, Wirtz D, Pollard TD. Dynamic cross-linking by alpha-actinin determines the mechanical properties of actin filament networks. J Biol Chem 273: 9570-9576, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 9570-9576
    • Xu, J.1    Wirtz, D.2    Pollard, T.D.3
  • 65
    • 0033804637 scopus 로고    scopus 로고
    • Substrate deformation levels associated with routine physical activity are less stimulatory to bone cells relative to loading-induced oscillatory fluid flow
    • You J, Yellowley CE, Donahue HJ, Zhang Y, Chen Q, Jacobs CR. Substrate deformation levels associated with routine physical activity are less stimulatory to bone cells relative to loading-induced oscillatory fluid flow. J Biomech Eng 122: 387-393, 2000.
    • (2000) J Biomech Eng , vol.122 , pp. 387-393
    • You, J.1    Yellowley, C.E.2    Donahue, H.J.3    Zhang, Y.4    Chen, Q.5    Jacobs, C.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.