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Volumn 49, Issue 6, 2013, Pages 1060-1068

Cyclic mechanical reinforcement of integrin-ligand interactions

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; INTEGRIN; LIGAND;

EID: 84875803668     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2013.01.015     Document Type: Article
Times cited : (133)

References (31)
  • 2
    • 0035858878 scopus 로고    scopus 로고
    • Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts
    • Beningo K.A., Dembo M., Kaverina I., Small J.V., Wang Y.L. Nascent focal adhesions are responsible for the generation of strong propulsive forces in migrating fibroblasts. J. Cell Biol. 2001, 153:881-888.
    • (2001) J. Cell Biol. , vol.153 , pp. 881-888
    • Beningo, K.A.1    Dembo, M.2    Kaverina, I.3    Small, J.V.4    Wang, Y.L.5
  • 3
    • 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 2008, 322:1687-1691.
    • (2008) Science , vol.322 , pp. 1687-1691
    • Chan, C.E.1    Odde, D.J.2
  • 4
    • 56349169536 scopus 로고    scopus 로고
    • Mechanotransduction-a field pulling together?
    • Chen C.S. Mechanotransduction-a field pulling together?. J. Cell Sci. 2008, 121:3285-3292.
    • (2008) J. Cell Sci. , vol.121 , pp. 3285-3292
    • Chen, C.S.1
  • 5
    • 38349065134 scopus 로고    scopus 로고
    • Monitoring receptor-ligand interactions between surfaces by thermal fluctuations
    • Chen W., Evans E.A., McEver R.P., Zhu C. Monitoring receptor-ligand interactions between surfaces by thermal fluctuations. Biophys. J. 2008, 94:694-701.
    • (2008) Biophys. J. , vol.94 , pp. 694-701
    • Chen, W.1    Evans, E.A.2    McEver, R.P.3    Zhu, C.4
  • 6
    • 78149245953 scopus 로고    scopus 로고
    • Forcing switch from short- to intermediate- and long-lived states of the alphaA domain generates LFA-1/ICAM-1 catch bonds
    • Chen W., Lou J., Zhu C. Forcing switch from short- to intermediate- and long-lived states of the alphaA domain generates LFA-1/ICAM-1 catch bonds. J. Biol. Chem. 2010, 285:35967-35978.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35967-35978
    • Chen, W.1    Lou, J.2    Zhu, C.3
  • 7
    • 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. 2012, 199:497-512.
    • (2012) J. Cell Biol. , vol.199 , pp. 497-512
    • Chen, W.1    Lou, J.2    Evans, E.A.3    Zhu, C.4
  • 8
    • 51049104617 scopus 로고    scopus 로고
    • Actin and α-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi C.K., Vicente-Manzanares M., Zareno J., Whitmore L.A., Mogilner A., Horwitz A.R. Actin and α-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 2008, 10:1039-1050.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 9
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • Choquet D., Felsenfeld D.P., Sheetz M.P. Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 1997, 88:39-48.
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 12
  • 14
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith C.G., Yamada K.M., Sheetz M.P. The relationship between force and focal complex development. J. Cell Biol. 2002, 159:695-705.
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 15
    • 33847159264 scopus 로고    scopus 로고
    • Polymerizing actin fibers position integrins primed to probe for adhesion sites
    • Galbraith C.G., Yamada K.M., Galbraith J.A. Polymerizing actin fibers position integrins primed to probe for adhesion sites. Science 2007, 315:992-995.
    • (2007) Science , vol.315 , pp. 992-995
    • Galbraith, C.G.1    Yamada, K.M.2    Galbraith, J.A.3
  • 16
    • 58249086114 scopus 로고    scopus 로고
    • Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed
    • Gardel M.L., Sabass B., Ji L., Danuser G., Schwarz U.S., Waterman C.M. Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed. J. Cell Biol. 2008, 183:999-1005.
    • (2008) J. Cell Biol. , vol.183 , pp. 999-1005
    • Gardel, M.L.1    Sabass, B.2    Ji, L.3    Danuser, G.4    Schwarz, U.S.5    Waterman, C.M.6
  • 18
    • 57049151271 scopus 로고    scopus 로고
    • Fluctuations of intracellular forces during cell protrusion
    • Ji L., Lim J., Danuser G. Fluctuations of intracellular forces during cell protrusion. Nat. Cell Biol. 2008, 10:1393-1400.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1393-1400
    • Ji, L.1    Lim, J.2    Danuser, G.3
  • 19
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong F., García A.J., Mould A.P., Humphries M.J., Zhu C. Demonstration of catch bonds between an integrin and its ligand. J. Cell Biol. 2009, 185:1275-1284.
    • (2009) J. Cell Biol. , vol.185 , pp. 1275-1284
    • Kong, F.1    García, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 20
    • 0033557842 scopus 로고    scopus 로고
    • A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study
    • Lahiri J., Isaacs L., Tien J., Whitesides G.M. A strategy for the generation of surfaces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study. Anal. Chem. 1999, 71:777-790.
    • (1999) Anal. Chem. , vol.71 , pp. 777-790
    • Lahiri, J.1    Isaacs, L.2    Tien, J.3    Whitesides, G.M.4
  • 21
    • 3042602113 scopus 로고    scopus 로고
    • 1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain
    • 1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain. J. Biol. Chem. 2004, 279:27466-27471.
    • (2004) J. Biol. Chem. , vol.279 , pp. 27466-27471
    • Luo, B.H.1    Strokovich, K.2    Walz, T.3    Springer, T.A.4    Takagi, J.5
  • 22
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo B.H., Carman C.V., Springer T.A. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 2007, 25:619-647.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 23
    • 0026730043 scopus 로고
    • Requirement for VLA-4 and VLA-5 integrins in lymphoma cells binding to and migration beneath stromal cells in culture
    • Miyake K., Hasunuma Y., Yagita H., Kimoto M. Requirement for VLA-4 and VLA-5 integrins in lymphoma cells binding to and migration beneath stromal cells in culture. J. Cell Biol. 1992, 119:653-662.
    • (1992) J. Cell Biol. , vol.119 , pp. 653-662
    • Miyake, K.1    Hasunuma, Y.2    Yagita, H.3    Kimoto, M.4
  • 24
    • 0030798854 scopus 로고    scopus 로고
    • Defining the topology of integrin α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies. Evidence that the synergy sequence of fibronectin is recognized by the amino-terminal repeats of the α5 subunit
    • Mould A.P., Askari J.A., Aota Si., Yamada K.M., Irie A., Takada Y., Mardon H.J., Humphries M.J. Defining the topology of integrin α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies. Evidence that the synergy sequence of fibronectin is recognized by the amino-terminal repeats of the α5 subunit. J. Biol. Chem. 1997, 272:17283-17292.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17283-17292
    • Mould, A.P.1    Askari, J.A.2    Aota, S.3    Yamada, K.M.4    Irie, A.5    Takada, Y.6    Mardon, H.J.7    Humphries, M.J.8
  • 25
    • 0013307787 scopus 로고    scopus 로고
    • Conformational changes in the integrin β A domain provide a mechanism for signal transduction via hybrid domain movement
    • Mould A.P., Barton S.J., Askari J.A., McEwan P.A., Buckley P.A., Craig S.E., Humphries M.J. Conformational changes in the integrin β A domain provide a mechanism for signal transduction via hybrid domain movement. J. Biol. Chem. 2003, 278:17028-17035.
    • (2003) J. Biol. Chem. , vol.278 , pp. 17028-17035
    • Mould, A.P.1    Barton, S.J.2    Askari, J.A.3    McEwan, P.A.4    Buckley, P.A.5    Craig, S.E.6    Humphries, M.J.7
  • 27
    • 33746255971 scopus 로고    scopus 로고
    • Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment compared to RGD supports
    • Petrie T.A., Capadona J.R., Reyes C.D., García A.J. Integrin specificity and enhanced cellular activities associated with surfaces presenting a recombinant fibronectin fragment compared to RGD supports. Biomaterials 2006, 27:5459-5470.
    • (2006) Biomaterials , vol.27 , pp. 5459-5470
    • Petrie, T.A.1    Capadona, J.R.2    Reyes, C.D.3    García, A.J.4
  • 31
    • 33645758327 scopus 로고    scopus 로고
    • Force generation in single conventional actomyosin complexes under high dynamic load
    • Takagi Y., Homsher E.E., Goldman Y.E., Shuman H. Force generation in single conventional actomyosin complexes under high dynamic load. Biophys. J. 2006, 90:1295-1307.
    • (2006) Biophys. J. , vol.90 , pp. 1295-1307
    • Takagi, Y.1    Homsher, E.E.2    Goldman, Y.E.3    Shuman, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.