메뉴 건너뛰기




Volumn 15, Issue 12, 2014, Pages 802-812

Mechanotransduction and extracellular matrix homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SMOOTH MUSCLE ACTIN; INTEGRIN; MYOSIN ADENOSINE TRIPHOSPHATASE;

EID: 84922128722     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3896     Document Type: Review
Times cited : (1544)

References (148)
  • 1
    • 84555179609 scopus 로고    scopus 로고
    • Extracellular matrix degradation and remodeling in development and disease
    • Lu P., Takai K., Weaver V. M. & Werb Z. Extracellular matrix degradation and remodeling in development and disease. Cold Spring Harb. Perspect. Biol. 3, a005058 (2011
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3 , pp. a005058
    • Lu, P.1    Takai, K.2    Weaver, V.M.3    Werb, Z.4
  • 3
    • 0023080985 scopus 로고
    • Dynamic reciprocity: How do extracellular matrix and hormones direct gene expression?
    • Bissell M. J. & Aggeler J. Dynamic reciprocity: how do extracellular matrix and hormones direct gene expression?. Prog. Clin. Biol. Res. 249, 251-262 (1987
    • (1987) Prog. Clin. Biol. Res , vol.249 , pp. 251-262
    • Bissell, M.J.1    Aggeler, J.2
  • 4
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V. & Sheetz M. Local force and geometry sensing regulate cell functions. Nature Rev. Mol. Cell Biol. 7, 265-275 (2006
    • (2006) Nature Rev. Mol. Cell Biol , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 5
    • 79960637431 scopus 로고    scopus 로고
    • Dynamic molecular processes mediate cellular mechanotransduction
    • Hoffman B. D., Grashoff C. & Schwartz M. A. Dynamic molecular processes mediate cellular mechanotransduction. Nature 475, 316-323 (2011
    • (2011) Nature , vol.475 , pp. 316-323
    • Hoffman, B.D.1    Grashoff, C.2    Schwartz, M.A.3
  • 6
    • 84922333220 scopus 로고    scopus 로고
    • Remodelling the extracellular matrix in development and diseases
    • Bonnans C., Chou J. & Werb Z. Remodelling the extracellular matrix in development and diseases. Nature Rev. Cell Mol. Biol. http://dx.doi.org/10.1038/nrm3904 (2014
    • (2014) Nature Rev. Cell Mol. Biol
    • Bonnans, C.1    Chou, J.2    Werb, Z.3
  • 7
    • 84922287672 scopus 로고    scopus 로고
    • Deconstructing extracellular matrix assembly: A multi-scale road map
    • Mouw J., Ou G. & Weaver V. M. Deconstructing extracellular matrix assembly: a multi-scale road map. Nature Rev. Cell Mol. Biol. http://dx.doi.org/10.1038/nrm3902 (2014
    • (2014) Nature Rev. Cell Mol. Biol
    • Mouw, J.1    Ou, G.2    Weaver, V.M.3
  • 8
    • 84863975330 scopus 로고    scopus 로고
    • Overview of the matrisome- an inventory of extracellular matrix constituents and functions
    • Hynes R. O. & Naba A. Overview of the matrisome- an inventory of extracellular matrix constituents and functions. Cold Spring Harb. Perspect. Biol. 4, a004903 (2012
    • (2012) Cold Spring Harb. Perspect. Biol , vol.4 , pp. a004903
    • Hynes, R.O.1    Naba, A.2
  • 9
    • 33746374311 scopus 로고    scopus 로고
    • Elastic fibres and vascular structure in hypertension
    • Arribas S. M., Hinek A. & Gonzalez M. C. Elastic fibres and vascular structure in hypertension. Pharmacol. Ther. 111, 771-791 (2006
    • (2006) Pharmacol. Ther , vol.111 , pp. 771-791
    • Arribas, S.M.1    Hinek, A.2    Gonzalez, M.C.3
  • 10
    • 33746943302 scopus 로고    scopus 로고
    • Elastic fibres in health and disease
    • Kielty C. M. Elastic fibres in health and disease. Expert Rev. Mol. Med. 8, 1-23 (2006
    • (2006) Expert Rev. Mol. Med , vol.8 , pp. 1-23
    • Kielty, C.M.1
  • 12
    • 80054112933 scopus 로고    scopus 로고
    • Mechanical assessment of elastin integrity in fibrillin 1 deficient carotid arteries: Implications for marfan syndrome
    • Ferruzzi J., Collins M. J., Yeh A. T. & Humphrey J. D. Mechanical assessment of elastin integrity in fibrillin 1 deficient carotid arteries: implications for Marfan syndrome. Cardiovasc. Res. 92, 287-295 (2011
    • (2011) Cardiovasc. Res , vol.92 , pp. 287-295
    • Ferruzzi, J.1    Collins, M.J.2    Yeh, A.T.3    Humphrey, J.D.4
  • 13
    • 0017280079 scopus 로고
    • Cyclic stretching stimulates synthesis of matrix components by arterial smooth muscle cells in vitro
    • Leung D. Y., Glagov S. & Mathews M. B. Cyclic stretching stimulates synthesis of matrix components by arterial smooth muscle cells in vitro. Science 191, 475-477 (1976
    • (1976) Science , vol.191 , pp. 475-477
    • Leung, D.Y.1    Glagov, S.2    Mathews, M.B.3
  • 14
    • 84859073207 scopus 로고    scopus 로고
    • Recent developments in myofibroblast biology: Paradigms for connective tissue remodeling
    • Hinz B., et al. Recent developments in myofibroblast biology: paradigms for connective tissue remodeling. Am. J. Pathol. 180, 1340-1355 (2012
    • (2012) Am. J. Pathol , vol.180 , pp. 1340-1355
    • Hinz, B.1
  • 15
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H., Visse R. & Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc. Res. 69, 562-573 (2006
    • (2006) Cardiovasc. Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 17
    • 84888440240 scopus 로고    scopus 로고
    • Integrating actin dynamics mechanotransduction and integrin activation: The multiple functions of actin binding proteins in focal adhesions
    • Ciobanasu C., Faivre B. & Le Clainche C. Integrating actin dynamics mechanotransduction and integrin activation: the multiple functions of actin binding proteins in focal adhesions. Eur. J. Cell Biol. 92, 339-348 (2013
    • (2013) Eur. J. Cell Biol , vol.92 , pp. 339-348
    • Ciobanasu, C.1    Faivre, B.2    Le Clainche, C.3
  • 18
    • 45249093434 scopus 로고    scopus 로고
    • Tensegrity-based mechanosensing from macro to micro
    • Ingber D. E. Tensegrity-based mechanosensing from macro to micro. Prog. Biophys. Mol. Biol. 97, 163-179 (2008
    • (2008) Prog. Biophys. Mol. Biol , vol.97 , pp. 163-179
    • Ingber, D.E.1
  • 19
    • 0035659828 scopus 로고    scopus 로고
    • Stress strain and mechanotransduction in cells
    • Humphrey J. D. Stress strain and mechanotransduction in cells. J. Biomech. Eng. 123, 638-641 (2001
    • (2001) J. Biomech. Eng , vol.123 , pp. 638-641
    • Humphrey, J.D.1
  • 20
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • Discher D. E., Janmey P. & Wang Y. L. Tissue cells feel and respond to the stiffness of their substrate. Science 310, 1139-1143 (2005
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.L.3
  • 21
    • 39149116773 scopus 로고    scopus 로고
    • Vascular adaptation and mechanical homeostasis at tissue cellular and sub-cellular levels
    • Humphrey J. D. Vascular adaptation and mechanical homeostasis at tissue cellular and sub-cellular levels. Cell Biochem. Biophys. 50, 53-78 (2008
    • (2008) Cell Biochem. Biophys , vol.50 , pp. 53-78
    • Humphrey, J.D.1
  • 22
    • 84900000951 scopus 로고    scopus 로고
    • Consistent biomechanical phenotyping of common carotid arteries from seven genetic pharmacological and surgical mouse models
    • Bersi M. R., Ferruzzi J., Eberth J. F., Gleason R. L. & Humphrey J. D. Consistent biomechanical phenotyping of common carotid arteries from seven genetic pharmacological and surgical mouse models. Ann. Biomed. Engineer. 42, 1207-1223 (2014
    • (2014) Ann. Biomed. Engineer , vol.42 , pp. 1207-1223
    • Bersi, M.R.1    Ferruzzi, J.2    Eberth, J.F.3    Gleason, R.L.4    Humphrey, J.D.5
  • 23
    • 0033397943 scopus 로고    scopus 로고
    • Mechanical design in arteries
    • Shadwick R. E. Mechanical design in arteries. J. Exp. Biol. 202, 3305-3313 (1999
    • (1999) J. Exp. Biol , vol.202 , pp. 3305-3313
    • Shadwick, R.E.1
  • 25
    • 0038701029 scopus 로고    scopus 로고
    • Mechanobiology of force transduction in dermal tissue
    • Silver F. H., Siperko L. M. & Seehra G. P. Mechanobiology of force transduction in dermal tissue. Skin Res. Technol. 9, 3-23 (2003
    • (2003) Skin Res. Technol , vol.9 , pp. 3-23
    • Silver, F.H.1    Siperko, L.M.2    Seehra, G.P.3
  • 26
    • 84896766570 scopus 로고    scopus 로고
    • Abnormal muscle mechanosignaling triggers cardiomyopathy in mice with Marfan syndrome
    • Cook J. R., et al. Abnormal muscle mechanosignaling triggers cardiomyopathy in mice with Marfan syndrome. J. Clin. Invest. 124, 1329-1339 (2014
    • (2014) J. Clin. Invest , vol.124 , pp. 1329-1339
    • Cook, J.R.1
  • 27
    • 84905252530 scopus 로고    scopus 로고
    • Clinical and biochemical profiles suggest fibromuscular dysplasia is a systemic disease with altered TGF-β expression and connective tissue features
    • Ganesh S. K., et al. Clinical and biochemical profiles suggest fibromuscular dysplasia is a systemic disease with altered TGF-β expression and connective tissue features. FASEB J. 28, 3313-3324 (2014
    • (2014) Faseb J. , vol.28 , pp. 3313-3324
    • Ganesh, S.K.1
  • 28
    • 84900298561 scopus 로고    scopus 로고
    • Cell biology dysfunctional mechanosensing in aneurysms
    • Humphrey J. D., Milewicz D. M., Tellides G. & Schwartz M. A. Cell biology. Dysfunctional mechanosensing in aneurysms. Science 344, 477-479 (2014
    • (2014) Science , vol.344 , pp. 477-479
    • Humphrey, J.D.1    Milewicz, D.M.2    Tellides, G.3    Schwartz, M.A.4
  • 29
    • 24944547482 scopus 로고    scopus 로고
    • Tensional homeostasis and the malignant phenotype
    • Paszek M. J., et al. Tensional homeostasis and the malignant phenotype. Cancer Cell 8, 241-254 (2005
    • (2005) Cancer Cell , vol.8 , pp. 241-254
    • Paszek, M.J.1
  • 30
    • 84887408112 scopus 로고    scopus 로고
    • Integrin-modulating therapy prevents fibrosis and autoimmunity in mouse models of scleroderma
    • Gerber E. E., et al. Integrin-modulating therapy prevents fibrosis and autoimmunity in mouse models of scleroderma. Nature 503, 126-130 (2013
    • (2013) Nature , vol.503 , pp. 126-130
    • Gerber, E.E.1
  • 31
    • 84904733201 scopus 로고    scopus 로고
    • Integrins and cadherins as therapeutic targets in fibrosis
    • Agarwal S. K. Integrins and cadherins as therapeutic targets in fibrosis. Front. Pharmacol. 5, 131 (2014
    • (2014) Front. Pharmacol , vol.5 , pp. 131
    • Agarwal, S.K.1
  • 33
    • 0025992778 scopus 로고
    • Measurement of mechanical forces generated by skin fibroblasts embedded in a three-dimensional collagen gel
    • Delvoye P., Wiliquet P., Leveque J. L., Nusgens B. V. & Lapiere C. M. Measurement of mechanical forces generated by skin fibroblasts embedded in a three-dimensional collagen gel. J. Invest. Dermatol. 97, 898-902 (1991
    • (1991) J. Invest. Dermatol , vol.97 , pp. 898-902
    • Delvoye, P.1    Wiliquet, P.2    Leveque, J.L.3    Nusgens, B.V.4    Lapiere, C.M.5
  • 34
    • 29144448018 scopus 로고    scopus 로고
    • The origins and regulation of tissue tension: Identification of collagen tension-fixation process in vitro
    • Marenzana M., Wilson-Jones N., Mudera V. & Brown R. A. The origins and regulation of tissue tension: identification of collagen tension-fixation process in vitro. Exp. Cell Res. 312, 423-433 (2006
    • (2006) Exp. Cell Res , vol.312 , pp. 423-433
    • Marenzana, M.1    Wilson-Jones, N.2    Mudera, V.3    Brown, R.A.4
  • 35
    • 0026519128 scopus 로고
    • Isometric contraction by fibroblasts and endothelial cells in tissue culture: A quantitative study
    • Kolodney M. S. & Wysolmerski R. B. Isometric contraction by fibroblasts and endothelial cells in tissue culture: a quantitative study. J. Cell Biol. 117, 73-82 (1992
    • (1992) J. Cell Biol , vol.117 , pp. 73-82
    • Kolodney, M.S.1    Wysolmerski, R.B.2
  • 36
    • 78649717029 scopus 로고    scopus 로고
    • Measurement of mechanical tractions exerted by cells in three-dimensional matrices
    • Legant W. R., et al. Measurement of mechanical tractions exerted by cells in three-dimensional matrices. Nature Methods 7, 969-971 (2010
    • (2010) Nature Methods , vol.7 , pp. 969-971
    • Legant, W.R.1
  • 37
    • 0035002155 scopus 로고    scopus 로고
    • Force and focal adhesion assembly: A close relationship studied using elastic micropatterned substrates
    • Balaban N. Q., et al. Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates. Nature Cell Biol. 3, 466-472 (2001
    • (2001) Nature Cell Biol , vol.3 , pp. 466-472
    • Balaban, N.Q.1
  • 38
    • 0037452695 scopus 로고    scopus 로고
    • Cells lying on a bed of microneedles: An approach to isolate mechanical force
    • Tan J. L., et al. Cells lying on a bed of microneedles: an approach to isolate mechanical force. Proc. Natl Acad. Sci. USA 100, 1484-1489 (2003
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 1484-1489
    • Tan, J.L.1
  • 39
    • 78751652828 scopus 로고    scopus 로고
    • Effects of disturbed flow on vascular endothelium: Pathophysiological basis and clinical perspectives
    • Chiu J. J. & Chien S. Effects of disturbed flow on vascular endothelium: pathophysiological basis and clinical perspectives. Physiol. Rev. 91, 327-387 (2011
    • (2011) Physiol. Rev , vol.91 , pp. 327-387
    • Chiu, J.J.1    Chien, S.2
  • 40
    • 0036013702 scopus 로고    scopus 로고
    • A constrained mixture model for growth and remodeling of soft tissues
    • Humphrey J. D. & Rajagopal K. R. A constrained mixture model for growth and remodeling of soft tissues. Math. Models Methods Appl. Sci. 12, 407-430 (2002
    • (2002) Math. Models Methods Appl. Sci , vol.12 , pp. 407-430
    • Humphrey, J.D.1    Rajagopal, K.R.2
  • 41
    • 0031896487 scopus 로고    scopus 로고
    • Stretch-induced collagen synthesis in cultured smooth muscle cells from rabbit aortic media and a possible involvement of angiotensin II and transforming growth factor-β
    • Li Q., Muragaki Y., Hatamura I., Ueno H. & Ooshima A. Stretch-induced collagen synthesis in cultured smooth muscle cells from rabbit aortic media and a possible involvement of angiotensin II and transforming growth factor-β. J. Vasc. Res. 35, 93-103 (1998
    • (1998) J. Vasc. Res , vol.35 , pp. 93-103
    • Li, Q.1    Muragaki, Y.2    Hatamura, I.3    Ueno, H.4    Ooshima, A.5
  • 42
    • 0033812921 scopus 로고    scopus 로고
    • Mechanical strain-induced extracellular matrix production by human vascular smooth muscle cells: Role of tgf-β1
    • O'Callaghan C. J. & Williams B. Mechanical strain-induced extracellular matrix production by human vascular smooth muscle cells: role of TGF-β1. Hypertension 36, 319-324 (2000
    • (2000) Hypertension , vol.36 , pp. 319-324
    • O'Callaghan, C.J.1    Williams, B.2
  • 43
    • 0033945355 scopus 로고    scopus 로고
    • Mechanical loading regulates protease production by fibroblasts in three-dimensional collagen substrates
    • Prajapati R. T., Chavally-Mis B., Herbage D., Eastwood M. & Brown R. A. Mechanical loading regulates protease production by fibroblasts in three-dimensional collagen substrates. Wound Repair Regen. 8, 226-237 (2000
    • (2000) Wound Repair Regen , vol.8 , pp. 226-237
    • Prajapati, R.T.1    Chavally-Mis, B.2    Herbage, D.3    Eastwood, M.4    Brown, R.A.5
  • 44
    • 24644452139 scopus 로고    scopus 로고
    • Strain-controlled enzymatic cleavage of collagen in loaded matrix
    • Ruberti J. W. & Hallab N. J. Strain-controlled enzymatic cleavage of collagen in loaded matrix. Biochem. Biophys. Res. Commun. 336, 483-489 (2005
    • (2005) Biochem. Biophys. Res. Commun , vol.336 , pp. 483-489
    • Ruberti, J.W.1    Hallab, N.J.2
  • 45
    • 69649089527 scopus 로고    scopus 로고
    • Evaluation of fundamental hypotheses underlying constrained mixture models of arterial growth and remodelling
    • Valentin A. & Humphrey J. D. Evaluation of fundamental hypotheses underlying constrained mixture models of arterial growth and remodelling. Philos. Trans. A Math. Phys. Eng. Sci. 367, 3585-3606 (2009
    • (2009) Philos. Trans. A Math. Phys. Eng. Sci , vol.367 , pp. 3585-3606
    • Valentin, A.1    Humphrey, J.D.2
  • 46
    • 84908211351 scopus 로고    scopus 로고
    • Mechanobiological stability: A new paradigm to understand the enlargement of aneurysms
    • Cyron C., Wilson J. S. & Humphrey J. D. Mechanobiological stability: a new paradigm to understand the enlargement of aneurysms. J. Roy. Soc. 11, 20140680 (2014
    • (2014) J. Roy. Soc , vol.11 , pp. 20140680
    • Cyron, C.1    Wilson, J.S.2    Humphrey, J.D.3
  • 47
    • 50849145156 scopus 로고    scopus 로고
    • Collagen fibrillogenesis: Fibronectin integrins and minor collagens as organizers and nucleators
    • Kadler K. E., Hill A. & Canty-Laird E. G. Collagen fibrillogenesis: fibronectin integrins and minor collagens as organizers and nucleators. Curr. Opin. Cell Biol. 20, 495-501 (2008
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 495-501
    • Kadler, K.E.1    Hill, A.2    Canty-Laird, E.G.3
  • 48
    • 0037020239 scopus 로고    scopus 로고
    • Polymerization of type i and III collagens is dependent on fibronectin and enhanced by integrins α 11β 1 and α 2β 1
    • Velling T., Risteli J., Wennerberg K., Mosher D. F. & Johansson S. Polymerization of type I and III collagens is dependent on fibronectin and enhanced by integrins α 11β 1 and α 2β 1. J. Biol. Chem. 277, 37377-37381 (2002
    • (2002) J. Biol. Chem , vol.277 , pp. 37377-37381
    • Velling, T.1    Risteli, J.2    Wennerberg, K.3    Mosher, D.F.4    Johansson, S.5
  • 49
    • 0041924762 scopus 로고    scopus 로고
    • Vascular smooth muscle cells orchestrate the assembly of type i collagen via α2β1 integrin rhoa and fibronectin polymerization
    • Li S., Van Den Diepstraten C., D'Souza S. J., Chan B. M. & Pickering J. G. Vascular smooth muscle cells orchestrate the assembly of type I collagen via α2β1 integrin RhoA and fibronectin polymerization. Am. J. Pathol. 163, 1045-1056 (2003
    • (2003) Am. J. Pathol , vol.163 , pp. 1045-1056
    • Li, S.1    Van Den Diepstraten, C.2    D'Souza, S.J.3    Chan, B.M.4    Pickering, J.G.5
  • 50
    • 13944265302 scopus 로고    scopus 로고
    • Basic mechanism of three-dimensional collagen fibre transport by fibroblasts
    • Meshel A. S., Wei Q., Adelstein R. S. & Sheetz M. P. Basic mechanism of three-dimensional collagen fibre transport by fibroblasts. Nature Cell Biol. 7, 157-164 (2005
    • (2005) Nature Cell Biol , vol.7 , pp. 157-164
    • Meshel, A.S.1    Wei, Q.2    Adelstein, R.S.3    Sheetz, M.P.4
  • 51
    • 36048943011 scopus 로고    scopus 로고
    • Dynamic protrusive cell behaviour generates force and drives early matrix contraction by fibroblasts
    • Dahlmann-Noor A. H., Martin-Martin B., Eastwood M., Khaw P. T. & Bailly M. Dynamic protrusive cell behaviour generates force and drives early matrix contraction by fibroblasts. Exp. Cell Res. 313, 4158-4169 (2007
    • (2007) Exp. Cell Res , vol.313 , pp. 4158-4169
    • Dahlmann-Noor, A.H.1    Martin-Martin, B.2    Eastwood, M.3    Khaw, P.T.4    Bailly, M.5
  • 52
    • 84886795952 scopus 로고    scopus 로고
    • Activation of extracellular transglutaminase 2 by mechanical force in the arterial wall
    • Huelsz-Prince G., Belkin A. M., VanBavel E. & Bakker E. N. Activation of extracellular transglutaminase 2 by mechanical force in the arterial wall. J. Vasc. Res. 50, 383-395 (2013
    • (2013) J. Vasc. Res , vol.50 , pp. 383-395
    • Huelsz-Prince, G.1    Belkin, A.M.2    Vanbavel, E.3    Bakker, E.N.4
  • 53
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • Baneyx G., Baugh L. & Vogel V. Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc. Natl Acad. Sci. USA 99, 5139-5143 (2002
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 54
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis a cell-mediated matrix assembly process
    • Mao Y. & Schwarzbauer J. E. Fibronectin fibrillogenesis a cell-mediated matrix assembly process. Matrix Biol. 24, 389-399 (2005
    • (2005) Matrix Biol , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 55
    • 2542439729 scopus 로고    scopus 로고
    • Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon
    • Canty E. G., et al. Coalignment of plasma membrane channels and protrusions (fibripositors) specifies the parallelism of tendon. J. Cell Biol. 165, 553-563 (2004
    • (2004) J. Cell Biol , vol.165 , pp. 553-563
    • Canty, E.G.1
  • 56
    • 33644916714 scopus 로고    scopus 로고
    • Elastic fiber macro-assembly is a hierarchical cell motion-mediated process
    • Czirok A., et al. Elastic fiber macro-assembly is a hierarchical cell motion-mediated process. J. Cell. Physiol. 207, 97-106 (2006
    • (2006) J. Cell. Physiol , vol.207 , pp. 97-106
    • Czirok, A.1
  • 57
    • 34848842170 scopus 로고    scopus 로고
    • Fibrillin-rich microfibrils: Structural determinants of morphogenetic and homeostatic events
    • Ramirez F. & Dietz H. C. Fibrillin-rich microfibrils: Structural determinants of morphogenetic and homeostatic events. J. Cell. Physiol. 213, 326-330 (2007
    • (2007) J. Cell. Physiol , vol.213 , pp. 326-330
    • Ramirez, F.1    Dietz, H.C.2
  • 58
    • 0141780878 scopus 로고    scopus 로고
    • Cell adhesion to fibrillin 1 molecules and microfibrils is mediated by α 5 β 1 and α v β 3 integrins
    • Bax D. V., et al. Cell adhesion to fibrillin 1 molecules and microfibrils is mediated by α 5 β 1 and α v β 3 integrins. J. Biol. Chem. 278, 34605-34616 (2003
    • (2003) J. Biol. Chem , vol.278 , pp. 34605-34616
    • Bax, D.V.1
  • 59
    • 67349089040 scopus 로고    scopus 로고
    • From mechanotransduction to extracellular matrix gene expression in fibroblasts
    • Chiquet M., Gelman L., Lutz R. & Maier S. From mechanotransduction to extracellular matrix gene expression in fibroblasts. Biochim. Biophys. Acta 1793, 911-920 (2009
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 911-920
    • Chiquet, M.1    Gelman, L.2    Lutz, R.3    Maier, S.4
  • 60
    • 20144365546 scopus 로고    scopus 로고
    • Extracellular matrix rigidity governs smooth muscle cell motility in a biphasic fashion
    • Peyton S. R. & Putnam A. J. Extracellular matrix rigidity governs smooth muscle cell motility in a biphasic fashion. J. Cell. Physiol. 204, 198-209 (2005
    • (2005) J. Cell. Physiol , vol.204 , pp. 198-209
    • Peyton, S.R.1    Putnam, A.J.2
  • 61
    • 0033696170 scopus 로고    scopus 로고
    • Substrate flexibility regulates growth and apoptosis of normal but not transformed cells
    • Wang H. B., Dembo M. & Wang Y. L. Substrate flexibility regulates growth and apoptosis of normal but not transformed cells. Am. J. Physiol. Cell Physiol. 279, C1345-1350 (2000
    • (2000) Am. J. Physiol. Cell Physiol , vol.279 , pp. C1345-1350
    • Wang, H.B.1    Dembo, M.2    Wang, Y.L.3
  • 62
    • 0344912596 scopus 로고    scopus 로고
    • Cell locomotion and focal adhesions are regulated by substrate flexibility
    • Pelham R. J. Jr & Wang Y. Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc. Natl Acad. Sci. USA 94, 13661-13665 (1997
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13661-13665
    • Pelham, R.J.1    Wang, Y.2
  • 63
    • 84871591464 scopus 로고    scopus 로고
    • Force fluctuations within focal adhesions mediate ECM-rigidity sensing to guide directed cell migration
    • Plotnikov S. V., Pasapera A. M., Sabass B. & Waterman C. M. Force fluctuations within focal adhesions mediate ECM-rigidity sensing to guide directed cell migration. Cell 151, 1513-1527 (2012
    • (2012) Cell , vol.151 , pp. 1513-1527
    • Plotnikov, S.V.1    Pasapera, A.M.2    Sabass, B.3    Waterman, C.M.4
  • 64
    • 0033917881 scopus 로고    scopus 로고
    • Cell movement is guided by the rigidity of the substrate
    • Lo C. M., Wang H. B., Dembo M. & Wang Y. L. Cell movement is guided by the rigidity of the substrate. Biophys. J. 79, 144-152 (2000
    • (2000) Biophys. J. , vol.79 , pp. 144-152
    • Lo, C.M.1    Wang, H.B.2    Dembo, M.3    Wang, Y.L.4
  • 65
    • 70349292059 scopus 로고    scopus 로고
    • Cell-cycle control by physiological matrix elasticity and in vivo tissue stiffening
    • Klein E. A., et al. Cell-cycle control by physiological matrix elasticity and in vivo tissue stiffening. Curr. Biol. 19, 1511-1518 (2009
    • (2009) Curr. Biol , vol.19 , pp. 1511-1518
    • Klein, E.A.1
  • 66
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler A. J., Sen S., Sweeney H. L. & Discher D. E. Matrix elasticity directs stem cell lineage specification. Cell 126, 677-689 (2006
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 67
    • 79958284636 scopus 로고    scopus 로고
    • Role of YAP/TAZ in mechanotransduction
    • Dupont S., et al. Role of YAP/TAZ in mechanotransduction. Nature 474, 179-183 (2011
    • (2011) Nature , vol.474 , pp. 179-183
    • Dupont, S.1
  • 68
    • 0027451706 scopus 로고
    • The extracellular matrix as a cell survival factor
    • Meredith J. E. Jr., Fazeli B. & Schwartz M. A. The extracellular matrix as a cell survival factor. Mol. Biol. Cell 4, 953-961 (1993
    • (1993) Mol. Biol. Cell , vol.4 , pp. 953-961
    • Meredith, J.E.1    Fazeli, B.2    Schwartz, M.A.3
  • 69
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch S. M. & Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124, 619-626 (1994
    • (1994) J. Cell Biol , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 70
    • 33847392947 scopus 로고    scopus 로고
    • New developments in fibroblast and myofibroblast biology: Implications for fibrosis and scleroderma
    • Abraham D. J., Eckes B., Rajkumar V. & Krieg T. New developments in fibroblast and myofibroblast biology: implications for fibrosis and scleroderma. Curr. Rheumatol Rep. 9, 136-143 (2007
    • (2007) Curr. Rheumatol Rep , vol.9 , pp. 136-143
    • Abraham, D.J.1    Eckes, B.2    Rajkumar, V.3    Krieg, T.4
  • 71
    • 19944428596 scopus 로고    scopus 로고
    • Effects of substrate stiffness on cell morphology cytoskeletal structure and adhesion
    • Yeung T., et al. Effects of substrate stiffness on cell morphology cytoskeletal structure and adhesion. Cell. Motil. Cytoskeleton 60, 24-34 (2005
    • (2005) Cell. Motil. Cytoskeleton , vol.60 , pp. 24-34
    • Yeung, T.1
  • 72
    • 15444367409 scopus 로고    scopus 로고
    • Fret measurements of cell-traction forces and nano-scale clustering of adhesion ligands varied by substrate stiffness
    • Kong H. J., Polte T. R., Alsberg E. & Mooney D. J. FRET measurements of cell-traction forces and nano-scale clustering of adhesion ligands varied by substrate stiffness. Proc. Natl Acad. Sci. USA 102, 4300-4305 (2005
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 4300-4305
    • Kong, H.J.1    Polte, T.R.2    Alsberg, E.3    Mooney, D.J.4
  • 73
    • 84887021862 scopus 로고    scopus 로고
    • Augmentation of integrin-mediated mechanotransduction by hyaluronic acid
    • Chopra A., et al. Augmentation of integrin-mediated mechanotransduction by hyaluronic acid. Biomaterials 35, 71-82 (2014
    • (2014) Biomaterials , vol.35 , pp. 71-82
    • Chopra, A.1
  • 74
    • 84875580590 scopus 로고    scopus 로고
    • Matrix stiffness reverses the effect of actomyosin tension on cell proliferation
    • Mih J. D., Marinkovic A., Liu F., Sharif A. S. & Tschumperlin D. J. Matrix stiffness reverses the effect of actomyosin tension on cell proliferation. J. Cell Sci. 125, 5974-5983 (2012
    • (2012) J. Cell Sci , vol.125 , pp. 5974-5983
    • Mih, J.D.1    Marinkovic, A.2    Liu, F.3    Sharif, A.S.4    Tschumperlin, D.J.5
  • 75
    • 84856134600 scopus 로고    scopus 로고
    • Fibroblast polarization is a matrix-rigidity-dependent process controlled by focal adhesion mechanosensing
    • Prager-Khoutorsky M., et al. Fibroblast polarization is a matrix-rigidity-dependent process controlled by focal adhesion mechanosensing. Nature Cell Biol. 13, 1457- 1465 (2011
    • (2011) Nature Cell Biol , vol.13 , pp. 1457-1465
    • Prager-Khoutorsky, M.1
  • 76
    • 27544435992 scopus 로고    scopus 로고
    • Mechanical force mobilizes zyxin from focal adhesions to actin filaments and regulates cytoskeletal reinforcement
    • Yoshigi M., Hoffman L. M., Jensen C. C., Yost H. J. & Beckerle M. C. Mechanical force mobilizes zyxin from focal adhesions to actin filaments and regulates cytoskeletal reinforcement. J. Cell Biol. 171, 209-215 (2005
    • (2005) J. Cell Biol , vol.171 , pp. 209-215
    • Yoshigi, M.1    Hoffman, L.M.2    Jensen, C.C.3    Yost, H.J.4    Beckerle, M.C.5
  • 77
    • 7744232293 scopus 로고    scopus 로고
    • Activation of a signaling cascade by cytoskeleton stretch
    • Tamada M., Sheetz M. P. & Sawada Y. Activation of a signaling cascade by cytoskeleton stretch. Dev. Cell 7, 709-718 (2004
    • (2004) Dev. Cell , vol.7 , pp. 709-718
    • Tamada, M.1    Sheetz, M.P.2    Sawada, Y.3
  • 78
    • 84867002885 scopus 로고    scopus 로고
    • Mechanical activation of cells induces chromatin remodeling preceding MKL nuclear transport
    • Iyer K. V., Pulford S., Mogilner A. & Shivashankar G. V. Mechanical activation of cells induces chromatin remodeling preceding MKL nuclear transport. Biophys. J. 103, 1416-1428 (2012
    • (2012) Biophys. J , vol.103 , pp. 1416-1428
    • Iyer, K.V.1    Pulford, S.2    Mogilner, A.3    Shivashankar, G.V.4
  • 79
    • 0034750658 scopus 로고    scopus 로고
    • Distinct pathways in the over-expression of matrix metalloproteinases in human fibroblasts by relaxation of mechanical tension
    • Lambert C. A., Colige A. C., Munaut C., Lapiere C. M. & Nusgens B. V. Distinct pathways in the over-expression of matrix metalloproteinases in human fibroblasts by relaxation of mechanical tension. Matrix Biol. 20, 397-408 (2001
    • (2001) Matrix Biol , vol.20 , pp. 397-408
    • Lambert, C.A.1    Colige, A.C.2    Munaut, C.3    Lapiere, C.M.4    Nusgens, B.V.5
  • 80
    • 0028566512 scopus 로고
    • Tenascin C expression by fibroblasts is elevated in stressed collagen gels
    • Chiquet-Ehrismann R., et al. Tenascin C expression by fibroblasts is elevated in stressed collagen gels. J. Cell Biol. 127, 2093-2101 (1994
    • (1994) J. Cell Biol , vol.127 , pp. 2093-2101
    • Chiquet-Ehrismann, R.1
  • 81
    • 0023603372 scopus 로고
    • Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promotes chondrogenesis in vitro
    • Mackie E. J., Thesleff I. & Chiquet-Ehrismann R. Tenascin is associated with chondrogenic and osteogenic differentiation in vivo and promotes chondrogenesis in vitro. J. Cell Biol. 105, 2569-2579 (1987
    • (1987) J. Cell Biol , vol.105 , pp. 2569-2579
    • MacKie, E.J.1    Thesleff, I.2    Chiquet-Ehrismann, R.3
  • 82
    • 0038236713 scopus 로고    scopus 로고
    • Tenascins: Regulation and putative functions during pathological stress
    • Chiquet-Ehrismann R. & Chiquet M. Tenascins: regulation and putative functions during pathological stress. J. Pathol. 200, 488-499 (2003
    • (2003) J. Pathol , vol.200 , pp. 488-499
    • Chiquet-Ehrismann, R.1    Chiquet, M.2
  • 83
  • 84
    • 33846224310 scopus 로고    scopus 로고
    • Deficiency of tenascin C attenuates liver fibrosis in immune-mediated chronic hepatitis in mice
    • El Karef A., et al. Deficiency of tenascin C attenuates liver fibrosis in immune-mediated chronic hepatitis in mice. J. Pathol. 211, 86-94 (2007
    • (2007) J. Pathol , vol.211 , pp. 86-94
    • El Karef, A.1
  • 85
    • 77749242706 scopus 로고    scopus 로고
    • Tenascin C may aggravate left ventricular remodeling and function after myocardial infarction in mice
    • Nishioka T., et al. Tenascin C may aggravate left ventricular remodeling and function after myocardial infarction in mice. Am. J. Physiol. Heart Circ. Physiol. 298, H1072-H1078 (2010
    • (2010) Am. J. Physiol. Heart Circ. Physiol , vol.298 , pp. H1072-H1078
    • Nishioka, T.1
  • 86
    • 33846625096 scopus 로고    scopus 로고
    • Nonequilibrium mechanics of active cytoskeletal networks
    • Mizuno D., Tardin C., Schmidt C. F. & Mackintosh F. C. Nonequilibrium mechanics of active cytoskeletal networks. Science 315, 370-373 (2007
    • (2007) Science , vol.315 , pp. 370-373
    • Mizuno, D.1    Tardin, C.2    Schmidt, C.F.3    MacKintosh, F.C.4
  • 87
    • 0028265522 scopus 로고
    • Cross-linker dynamics determine the mechanical properties of actin gels
    • Wachsstock D. H., Schwarz W. H. & Pollard T. D. 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
  • 88
    • 6344240540 scopus 로고    scopus 로고
    • Viscoelasticity of human alveolar epithelial cells subjected to stretch
    • Trepat X., et al. Viscoelasticity of human alveolar epithelial cells subjected to stretch. Am. J. Physiol. Lung Cell. Mol. Physiol. 287, L1025-L1034 (2004
    • (2004) Am. J. Physiol. Lung Cell. Mol. Physiol , vol.287 , pp. L1025-L1034
    • Trepat, X.1
  • 89
    • 84903948040 scopus 로고    scopus 로고
    • Tensional homeostasis in single fibroblasts
    • Webster K. D., Ng W. P. & Fletcher D. A. Tensional homeostasis in single fibroblasts. Biophys. J. 107, 146-155 (2014
    • (2014) Biophys. J. , vol.107 , pp. 146-155
    • Webster, K.D.1    Ng, W.P.2    Fletcher, D.A.3
  • 90
    • 55949135876 scopus 로고    scopus 로고
    • Two characteristic regimes in frequency-dependent dynamic reorientation of fibroblasts on cyclically stretched substrates
    • Jungbauer S., Gao H. J., Spatz J. P. & Kemkemer R. Two characteristic regimes in frequency-dependent dynamic reorientation of fibroblasts on cyclically stretched substrates. Biophys. J. 95, 3470-3478 (2008
    • (2008) Biophys. J. , vol.95 , pp. 3470-3478
    • Jungbauer, S.1    Gao, H.J.2    Spatz, J.P.3    Kemkemer, R.4
  • 91
    • 83455246926 scopus 로고    scopus 로고
    • Cyclic stress at mHz frequencies aligns fibroblasts in direction of zero strain
    • Faust U., et al. Cyclic stress at mHz frequencies aligns fibroblasts in direction of zero strain. PLoS ONE 6, 16 (2011
    • (2011) Plos One , vol.6 , pp. 16
    • Faust, U.1
  • 92
    • 84903691947 scopus 로고    scopus 로고
    • Paxillin mediates stretch-induced rho signaling and endothelial permeability via assembly of paxillin p42/44mapk gef h1 complex
    • Gawlak G., et al. Paxillin mediates stretch-induced Rho signaling and endothelial permeability via assembly of paxillin p42/44MAPK GEF H1 complex. FASEB J. 28, 3249-3260 (2014
    • (2014) Faseb J. , vol.28 , pp. 3249-3260
    • Gawlak, G.1
  • 93
    • 79952832477 scopus 로고    scopus 로고
    • Rac1 and RhoA differentially regulate angiotensinogen gene expression in stretched cardiac fibroblasts
    • Verma S. K., et al. Rac1 and RhoA differentially regulate angiotensinogen gene expression in stretched cardiac fibroblasts. Cardiovasc. Res. 90, 88-96 (2011
    • (2011) Cardiovasc. Res , vol.90 , pp. 88-96
    • Verma, S.K.1
  • 94
    • 34548432555 scopus 로고    scopus 로고
    • Dynamics of cell orientation
    • De R., Zemel A. & Safran S. A. Dynamics of cell orientation. Nature Phys. 3, 655-659 (2007
    • (2007) Nature Phys , vol.3 , pp. 655-659
    • De, R.1    Zemel, A.2    Safran, S.A.3
  • 95
  • 96
    • 84901762853 scopus 로고    scopus 로고
    • Cell orientation under cyclic stretching
    • Livne A., Bouchbinder E. & Geiger B. Cell orientation under cyclic stretching. Nature Comm. 5, 3938 (2014
    • (2014) Nature Comm , vol.5 , Issue.3938
    • Livne, A.1    Bouchbinder, E.2    Geiger, B.3
  • 97
    • 0037262361 scopus 로고    scopus 로고
    • A critical role for elastin signaling in vascular morphogenesis and disease
    • Karnik S. K., et al. A critical role for elastin signaling in vascular morphogenesis and disease. Development 130, 411-423 (2003
    • (2003) Development , vol.130 , pp. 411-423
    • Karnik, S.K.1
  • 99
    • 0030582716 scopus 로고    scopus 로고
    • Fibrillar collagen inhibits arterial smooth muscle proliferation through regulation of Cdk2 inhibitors
    • Koyama H., Raines E. W., Bornfeldt K. E., Roberts J. M. & Ross R. Fibrillar collagen inhibits arterial smooth muscle proliferation through regulation of Cdk2 inhibitors. Cell 87, 1069-1078 (1996
    • (1996) Cell , vol.87 , pp. 1069-1078
    • Koyama, H.1    Raines, E.W.2    Bornfeldt, K.E.3    Roberts, J.M.4    Ross, R.5
  • 101
    • 0026554217 scopus 로고
    • Affinity of integrins for damaged extracellular matrix: α v β 3 binds to denatured collagen type i through rgd sites
    • Davis G. E. Affinity of integrins for damaged extracellular matrix: α v β 3 binds to denatured collagen type I through RGD sites. Biochem. Biophys. Res. Commun. 182, 1025-1031 (1992
    • (1992) Biochem. Biophys. Res. Commun , vol.182 , pp. 1025-1031
    • Davis, G.E.1
  • 102
    • 84856566806 scopus 로고    scopus 로고
    • The significance of integrin ligand nanopatterning on lipid raft clustering in hematopoietic stem cells
    • Altrock E., Muth C. A., Klein G., Spatz J. P. & Lee-Thedieck C. The significance of integrin ligand nanopatterning on lipid raft clustering in hematopoietic stem cells. Biomaterials 33, 3107-3118 (2012
    • (2012) Biomaterials , vol.33 , pp. 3107-3118
    • Altrock, E.1    Muth, C.A.2    Klein, G.3    Spatz, J.P.4    Lee-Thedieck, C.5
  • 103
    • 72449173039 scopus 로고    scopus 로고
    • Cell adhesion and response to synthetic nanopatterned environments by steering receptor clustering and spatial location
    • Cavalcanti-Adam E. A., Aydin D., Hirschfeld- Warneken V. C. & Spatz J. P. Cell adhesion and response to synthetic nanopatterned environments by steering receptor clustering and spatial location. HFSP J. 2, 276-285 (2008
    • (2008) Hfsp J. , vol.2 , pp. 276-285
    • Cavalcanti-Adam, E.A.1    Aydin, D.2    Hirschfeld-Warneken, V.C.3    Spatz, J.P.4
  • 104
    • 84862646170 scopus 로고    scopus 로고
    • Extracellular-matrix tethering regulates stem-cell fate
    • Trappmann B., et al. Extracellular-matrix tethering regulates stem-cell fate. Nature Mater. 11, 642-649 (2012
    • (2012) Nature Mater , vol.11 , pp. 642-649
    • Trappmann, B.1
  • 106
    • 0037054552 scopus 로고    scopus 로고
    • Slow local movements of collagen fibers by fibroblasts drive the rapid global self-organization of collagen gels
    • Sawhney R. K. & Howard J. Slow local movements of collagen fibers by fibroblasts drive the rapid global self-organization of collagen gels. J. Cell Biol. 157, 1083-1091 (2002
    • (2002) J. Cell Biol , vol.157 , pp. 1083-1091
    • Sawhney, R.K.1    Howard, J.2
  • 107
    • 67749140074 scopus 로고    scopus 로고
    • Non-linear elasticity of extracellular matrices enables contractile cells to communicate local position and orientation
    • Winer J. P., Oake S. & Janmey P. A. Non-linear elasticity of extracellular matrices enables contractile cells to communicate local position and orientation. PLoS ONE 4, e6382 (2009
    • (2009) Plos One , vol.4 , pp. e6382
    • Winer, J.P.1    Oake, S.2    Janmey, P.A.3
  • 109
    • 77955580383 scopus 로고    scopus 로고
    • Stretchy proteins on stretchy substrates: The important elements of integrin-mediated rigidity sensing
    • Moore S. W., Roca-Cusachs P. & Sheetz M. P. Stretchy proteins on stretchy substrates: the important elements of integrin-mediated rigidity sensing. Dev. Cell 19, 194-206 (2010
    • (2010) Dev. Cell , vol.19 , pp. 194-206
    • Moore, S.W.1    Roca-Cusachs, P.2    Sheetz, M.P.3
  • 110
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C., et al. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141, 539-551 (1998
    • (1998) J. Cell Biol , vol.141 , pp. 539-551
    • Zhong, C.1
  • 111
    • 59149094538 scopus 로고    scopus 로고
    • Stretching single talin rod molecules activates vinculin binding
    • del Rio A., et al. Stretching single talin rod molecules activates vinculin binding. Science 323, 638-641 (2009
    • (2009) Science , vol.323 , pp. 638-641
    • Del Rio, A.1
  • 112
    • 33646338633 scopus 로고    scopus 로고
    • The activity of the vinculin binding sites in talin is influenced by the stability of the helical bundles that make up the talin rod
    • Patel B., et al. The activity of the vinculin binding sites in talin is influenced by the stability of the helical bundles that make up the talin rod. J. Biol. Chem. 281, 7458-7467 (2006
    • (2006) J. Biol. Chem , vol.281 , pp. 7458-7467
    • Patel, B.1
  • 113
    • 77954486800 scopus 로고    scopus 로고
    • Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
    • Grashoff C., et al. Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics. Nature 466, 263-266 (2010
    • (2010) Nature , vol.466 , pp. 263-266
    • Grashoff, C.1
  • 114
    • 77951246518 scopus 로고    scopus 로고
    • Contractility modulates cell adhesion strengthening through focal adhesion kinase and assembly of vinculin-containing focal adhesions
    • Dumbauld D. W., et al. Contractility modulates cell adhesion strengthening through focal adhesion kinase and assembly of vinculin-containing focal adhesions. J. Cell. Physiol. 223, 746-756 (2010
    • (2010) J. Cell. Physiol , vol.223 , pp. 746-756
    • Dumbauld, D.W.1
  • 115
    • 80054043810 scopus 로고    scopus 로고
    • Mechanical strain in actin networks regulates filgap and integrin binding to filamin A
    • Ehrlicher A. J., Nakamura F., Hartwig J. H., Weitz D. A. & Stossel T. P. Mechanical Strain in Actin Networks Regulates FilGAP and Integrin Binding to Filamin A. Nature 478, 260-263 (2011
    • (2011) Nature , vol.478 , pp. 260-263
    • Ehrlicher, A.J.1    Nakamura, F.2    Hartwig, J.H.3    Weitz, D.A.4    Stossel, T.P.5
  • 116
    • 0037043341 scopus 로고    scopus 로고
    • Effects of cell tension on the small GTPase Rac
    • Katsumi A., et al. Effects of cell tension on the small GTPase Rac. J. Cell Biol. 158, 153-164 (2002
    • (2002) J. Cell Biol , vol.158 , pp. 153-164
    • Katsumi, A.1
  • 117
    • 84870381713 scopus 로고    scopus 로고
    • Dynamic force sensing of filamin revealed in single-molecule experiments
    • Rognoni L., Stigler J., Pelz B., Ylanne J. & Rief M. Dynamic force sensing of filamin revealed in single-molecule experiments. Proc. Natl Acad. Sci. USA 109, 19679-19684 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 19679-19684
    • Rognoni, L.1    Stigler, J.2    Pelz, B.3    Ylanne, J.4    Rief, M.5
  • 118
    • 85027919980 scopus 로고    scopus 로고
    • Based detection of mechanical stress in cytoskeletal and extracellular matrix proteins
    • Real Time F.R.E.T
    • Meng F., Suchyna T. M., Lazakovitch E., Gronostajski R. M. & Sachs F. Real Time F. R.E. T. Based detection of mechanical stress in cytoskeletal and extracellular matrix proteins. Cell. Mol. Bioeng. 4, 148-159 (2011
    • (2011) Cell. Mol. Bioeng , vol.4 , pp. 148-159
    • Meng, F.1    Suchyna, T.M.2    Lazakovitch, E.3    Gronostajski, R.M.4    Sachs, F.5
  • 119
    • 84869127061 scopus 로고    scopus 로고
    • Observing force-regulated conformational changes and ligand dissociation from a single integrin on cells
    • Chen W., Lou J., Evans E. A. & Zhu C. Observing force-regulated conformational changes and ligand dissociation from a single integrin on cells. J. Cell Biol. 199, 497-512 (2012
    • (2012) J. Cell Biol , vol.199 , pp. 497-512
    • Chen, W.1    Lou, J.2    Evans, E.A.3    Zhu, C.4
  • 120
    • 84875803668 scopus 로고    scopus 로고
    • Cyclic mechanical reinforcement of integrin-ligand interactions
    • Kong F., et al. Cyclic mechanical reinforcement of integrin-ligand interactions. Mol. Cell 49, 1060-1068 (2013
    • (2013) Mol. Cell , vol.49 , pp. 1060-1068
    • Kong, F.1
  • 121
    • 77949754056 scopus 로고    scopus 로고
    • Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation
    • Pasapera A. M., Schneider I. C., Rericha E., Schlaepfer D. D. & Waterman C. M. Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation. J. Cell Biol. 188, 877-890 (2010
    • (2010) J. Cell Biol , vol.188 , pp. 877-890
    • Pasapera, A.M.1    Schneider, I.C.2    Rericha, E.3    Schlaepfer, D.D.4    Waterman, C.M.5
  • 122
    • 84875515145 scopus 로고    scopus 로고
    • Actin depolymerization under force is governed by lysine 113:glutamic acid 195 mediated catch-slip bonds
    • Lee C. Y., et al. Actin depolymerization under force is governed by lysine 113:glutamic acid 195 mediated catch-slip bonds. Proc. Natl Acad. Sci. USA 110, 5022-5027 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 5022-5027
    • Lee, C.Y.1
  • 123
    • 80054079832 scopus 로고    scopus 로고
    • Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament
    • Hayakawa K., Tatsumi H. & Sokabe M. Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament. J. Cell Biol. 195, 721-727 (2011
    • (2011) J. Cell Biol , vol.195 , pp. 721-727
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 124
    • 70350351208 scopus 로고    scopus 로고
    • Coronin 2A regulates a subset of focal-adhesion-turnover events through the cofilin pathway
    • Marshall T. W., Aloor H. L. & Bear J. E. Coronin 2A regulates a subset of focal-adhesion-turnover events through the cofilin pathway. J. Cell Sci. 122, 3061-3069 (2009
    • (2009) J. Cell Sci , vol.122 , pp. 3061-3069
    • Marshall, T.W.1    Aloor, H.L.2    Bear, J.E.3
  • 125
    • 58249086114 scopus 로고    scopus 로고
    • Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed
    • Gardel M. L., et al. Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed. J. Cell Biol. 183, 999-1005 (2008
    • (2008) J. Cell Biol , vol.183 , pp. 999-1005
    • Gardel, M.L.1
  • 126
    • 33846697554 scopus 로고    scopus 로고
    • Differential transmission of actin motion within focal adhesions
    • Hu K., Ji L., Applegate K. T., Danuser G. & Waterman-Storer C. M. Differential transmission of actin motion within focal adhesions. Science 315, 111-115 (2007
    • (2007) Science , vol.315 , pp. 111-115
    • Hu, K.1    Ji, L.2    Applegate, K.T.3    Danuser, G.4    Waterman-Storer, C.M.5
  • 127
    • 33846176546 scopus 로고    scopus 로고
    • Probing the integrin-actin linkage using high-resolution protein velocity mapping
    • Brown C. M., et al. Probing the integrin-actin linkage using high-resolution protein velocity mapping. J. Cell Sci. 119, 5204-5214 (2006
    • (2006) J. Cell Sci , vol.119 , pp. 5204-5214
    • Brown, C.M.1
  • 128
  • 129
    • 58149230940 scopus 로고    scopus 로고
    • Traction dynamics of filopodia on compliant substrates
    • Chan C. E. & Odde D. J. Traction dynamics of filopodia on compliant substrates. Science 322, 1687-1691 (2008
    • (2008) Science , vol.322 , pp. 1687-1691
    • Chan, C.E.1    Odde, D.J.2
  • 130
    • 80052693572 scopus 로고    scopus 로고
    • Force localization in contracting cell layers
    • Edwards C. M. & Schwarz U. S. Force localization in contracting cell layers. Phys. Rev. Lett. 107, 5 (2011
    • (2011) Phys. Rev. Lett , vol.107 , pp. 5
    • Edwards, C.M.1    Schwarz, U.S.2
  • 131
    • 84860706299 scopus 로고    scopus 로고
    • Scaling of traction forces with the size of cohesive cell colonies
    • Mertz A. F., et al. Scaling of traction forces with the size of cohesive cell colonies. Phys. Rev. Lett. 108, 5 (2012
    • (2012) Phys. Rev. Lett , vol.108 , pp. 5
    • Mertz, A.F.1
  • 132
    • 80053103556 scopus 로고    scopus 로고
    • Rigidity sensing explained by active matter theory
    • Marcq P., Yoshinaga N. & Prost J. Rigidity sensing explained by active matter theory. Biophys. J. 101, L33-L35 (2011
    • (2011) Biophys. J. , vol.101 , pp. L33-L35
    • Marcq, P.1    Yoshinaga, N.2    Prost, J.3
  • 133
  • 134
    • 84860807182 scopus 로고    scopus 로고
    • Evidence of a large-scale mechanosensing mechanism for cellular adaptation to substrate stiffness
    • Trichet L., et al. Evidence of a large-scale mechanosensing mechanism for cellular adaptation to substrate stiffness. Proc. Natl Acad. Sci. USA 109, 6933-6938 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 6933-6938
    • Trichet, L.1
  • 135
    • 0037437150 scopus 로고    scopus 로고
    • Rptp-α acts as a transducer of mechanical force on αv/β3 integrin-cytoskeleton linkages
    • von Wichert G., et al. RPTP-α acts as a transducer of mechanical force on αv/β3 integrin-cytoskeleton linkages. J. Cell Biol. 161, 143-153 (2003
    • (2003) J. Cell Biol , vol.161 , pp. 143-153
    • Von Wichert, G.1
  • 136
    • 33646155963 scopus 로고    scopus 로고
    • Rigidity sensing at the leading edge through αvβ3 integrins and rptpα
    • Jiang G., Huang A. H., Cai Y., Tanase M. & Sheetz M. P. Rigidity sensing at the leading edge through αvβ3 integrins and RPTPα. Biophys. J. 90, 1804-1809 (2006
    • (2006) Biophys. J. , vol.90 , pp. 1804-1809
    • Jiang, G.1    Huang, A.H.2    Cai, Y.3    Tanase, M.4    Sheetz, M.P.5
  • 137
    • 70349496205 scopus 로고    scopus 로고
    • Clustering of α5β1 integrins determines adhesion strength whereas αvβ3 and talin enable mechanotransduction
    • Roca-Cusachs P., Gauthier N. C., Del Rio A. & Sheetz M. P. Clustering of α5β1 integrins determines adhesion strength whereas αvβ3 and talin enable mechanotransduction. Proc. Natl Acad. Sci. USA 106, 16245-16250 (2009
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16245-16250
    • Roca-Cusachs, P.1    Gauthier, N.C.2    Del Rio, A.3    Sheetz, M.P.4
  • 138
    • 84878598076 scopus 로고    scopus 로고
    • Β 1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments
    • Schiller H. B., et al. β1- and αv-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. Nature Cell Biol. 15, 625-636 (2013
    • (2013) Nature Cell Biol , vol.15 , pp. 625-636
    • Schiller, H.B.1
  • 139
    • 0035949694 scopus 로고    scopus 로고
    • Focal adhesion kinase is involved in mechanosensing during fibroblast migration
    • Wang H. B., Dembo M., Hanks S. K. & Wang Y. Focal adhesion kinase is involved in mechanosensing during fibroblast migration. Proc. Natl Acad. Sci. USA 98, 11295-11300 (2001
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11295-11300
    • Wang, H.B.1    Dembo, M.2    Hanks, S.K.3    Wang, Y.4
  • 141
    • 77953806617 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptors gamma reverses hepatic nutritional fibrosis in mice and suppresses activation of hepatic stellate cells in vitro
    • Yu J., et al. Peroxisome proliferator-activated receptors gamma reverses hepatic nutritional fibrosis in mice and suppresses activation of hepatic stellate cells in vitro. Int. J. Biochem. Cell Biol. 42, 948-957 (2010
    • (2010) Int. J. Biochem. Cell Biol , vol.42 , pp. 948-957
    • Yu, J.1
  • 142
    • 84891556733 scopus 로고    scopus 로고
    • Destiffening effect of valsartan and atenolol: Influence of heart rate and blood pressure
    • & EXPLOR trialists
    • Boutouyrie P., Beaussier H., Achouba A., Laurent S. & EXPLOR trialists. Destiffening effect of valsartan and atenolol: influence of heart rate and blood pressure. J. Hypertens. 32, 108-114 (2014
    • (2014) J. Hypertens , vol.32 , pp. 108-114
    • Boutouyrie, P.1    Beaussier, H.2    Achouba, A.3    Laurent, S.4
  • 143
    • 34250760899 scopus 로고    scopus 로고
    • Mechanical factors in arterial aging: A clinical perspective
    • O'Rourke M. F. & Hashimoto J. Mechanical factors in arterial aging: a clinical perspective. J. Am. Coll. Cardiol 50, 1-13 (2007
    • (2007) J. Am. Coll. Cardiol , vol.50 , pp. 1-13
    • O'Rourke, M.F.1    Hashimoto, J.2
  • 144
    • 84873424343 scopus 로고    scopus 로고
    • Apolipoprotein e mediated cell cycle arrest linked to p27 and the Cox2 dependent repression of miR221/222
    • Kothapalli D., et al. Apolipoprotein E mediated cell cycle arrest linked to p27 and the Cox2 dependent repression of miR221/222. Atherosclerosis 227, 65-71 (2013
    • (2013) Atherosclerosis , vol.227 , pp. 65-71
    • Kothapalli, D.1
  • 145
    • 77955914547 scopus 로고    scopus 로고
    • Feedback amplification of fibrosis through matrix stiffening and COX 2 suppression
    • Liu F., et al. Feedback amplification of fibrosis through matrix stiffening and COX 2 suppression. J. Cell Biol. 190, 693-706 (2010
    • (2010) J. Cell Biol , vol.190 , pp. 693-706
    • Liu, F.1
  • 146
    • 0038738331 scopus 로고    scopus 로고
    • Fibroblast biology in three-dimensional collagen matrices
    • Grinnell F. Fibroblast biology in three-dimensional collagen matrices. Trends Cell Biol. 13, 264-269 (2003
    • (2003) Trends Cell Biol , vol.13 , pp. 264-269
    • Grinnell, F.1
  • 147
    • 0034141745 scopus 로고    scopus 로고
    • Racemization and isomerization of type i collagen C telopeptides in human bone and soft tissues: Assessment of tissue turnover
    • Gineyts E., et al. Racemization and isomerization of type I collagen C telopeptides in human bone and soft tissues: assessment of tissue turnover. Biochem. J. 345, 481-485 (2000
    • (2000) Biochem. J. , vol.345 , pp. 481-485
    • Gineyts, E.1
  • 148
    • 58149468382 scopus 로고    scopus 로고
    • Fundamental role of axial stress in compensatory adaptations by arteries
    • Humphrey J. D., Eberth J. F., Dye W. W. & Gleason R. L. Fundamental role of axial stress in compensatory adaptations by arteries. J. Biomech. 42, 1-8 (2009
    • (2009) J. Biomech , vol.42 , pp. 1-8
    • Humphrey, J.D.1    Eberth, J.F.2    Dye, W.W.3    Gleason, R.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.