메뉴 건너뛰기




Volumn 346, Issue 6209, 2014, Pages

The minimal cadherin-catenin complex binds to actin filaments under force

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; CATENIN; F ACTIN; ACTIN;

EID: 84909592568     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1254211     Document Type: Article
Times cited : (477)

References (52)
  • 1
    • 23144442645 scopus 로고    scopus 로고
    • Regulation of cadherin-mediated adhesion in morphogenesis
    • pmid: 16025097
    • B. M. Gumbiner, Regulation of cadherin-mediated adhesion in morphogenesis. Nat. Rev. Mol. Cell Biol. 6, 622-634 (2005). doi: 10.1038/nrm1699; pmid: 16025097
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 622-634
    • Gumbiner, B.M.1
  • 2
    • 79955642014 scopus 로고    scopus 로고
    • Tissue organization by cadherin adhesion molecules: Dynamic molecular and cellular mechanisms of morphogenetic regulation
    • pmid: 21527735
    • C. M. Niessen, D. Leckband, A. S. Yap, Tissue organization by cadherin adhesion molecules: Dynamic molecular and cellular mechanisms of morphogenetic regulation. Physiol. Rev. 91, 691-731 (2011). doi: 10.1152/physrev. 00004.2010; pmid: 21527735
    • (2011) Physiol. Rev. , vol.91 , pp. 691-731
    • Niessen, C.M.1    Leckband, D.2    Yap, A.S.3
  • 3
    • 84874598008 scopus 로고    scopus 로고
    • Adherens junctions and cancer
    • pmid: 22674080
    • V. Vasioukhin, Adherens junctions and cancer. Subcell. Biochem. 60, 379-414 (2012). doi: 10.1007/978-94-007-4186-7-16; pmid: 22674080
    • (2012) Subcell. Biochem. , vol.60 , pp. 379-414
    • Vasioukhin, V.1
  • 4
    • 84901491471 scopus 로고    scopus 로고
    • Dynamic contacts: Rearranging adherens junctions to drive epithelial remodelling
    • pmid: 24824068
    • M. Takeichi, Dynamic contacts: Rearranging adherens junctions to drive epithelial remodelling. Nat. Rev. Mol. Cell Biol. 15, 397-410 (2014). doi: 10.1038/nrm3802; pmid: 24824068
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 397-410
    • Takeichi, M.1
  • 5
    • 77149179101 scopus 로고    scopus 로고
    • Adherens junction: Molecular architecture and regulation
    • pmid: 20457565
    • W. Meng, M. Takeichi, Adherens junction: Molecular architecture and regulation. Cold Spring Harb. Perspect. Biol. 1, a002899 (2009). doi: 10.1101/cshperspect.a002899; pmid: 20457565
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1 , pp. a002899
    • Meng, W.1    Takeichi, M.2
  • 6
    • 0034741031 scopus 로고    scopus 로고
    • αT-catenin: A novel tissue-specific b-catenin-binding protein mediating strong cell-cell adhesion
    • pmid: 11590244
    • B. Janssens et al., αT-catenin: A novel tissue-specific b-catenin-binding protein mediating strong cell-cell adhesion. J. Cell Sci. 114, 3177-3188 (2001). pmid: 11590244
    • (2001) J. Cell Sci. , vol.114 , pp. 3177-3188
    • Janssens, B.1
  • 7
    • 84900449829 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of cadherin·β-catenin·α-catenin complex formation
    • pmid: 24692547
    • S. Pokutta, H. J. Choi, G. Ahlsen, S. D. Hansen, W. I. Weis, Structural and thermodynamic characterization of cadherin·β-catenin·α-catenin complex formation. J. Biol. Chem. 289, 13589-13601 (2014). doi: 10.1074/jbc. M114.554709; pmid: 24692547
    • (2014) J. Biol. Chem. , vol.289 , pp. 13589-13601
    • Pokutta, S.1    Choi, H.J.2    Ahlsen, G.3    Hansen, S.D.4    Weis, W.I.5
  • 8
    • 28344433073 scopus 로고    scopus 로고
    • Deconstructing the cadherin-catenin-actin complex
    • pmid: 16325582
    • S. Yamada, S. Pokutta, F. Drees, W. I. Weis, W. J. Nelson, Deconstructing the cadherin-catenin-actin complex. Cell 123, 889-901 (2005). doi: 10.1016/j.cell.2005.09.020; pmid: 16325582
    • (2005) Cell , vol.123 , pp. 889-901
    • Yamada, S.1    Pokutta, S.2    Drees, F.3    Weis, W.I.4    Nelson, W.J.5
  • 9
    • 84889020463 scopus 로고    scopus 로고
    • αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors
    • pmid: 24068324
    • S. D. Hansen et al., αE-catenin actin-binding domain alters actin filament conformation and regulates binding of nucleation and disassembly factors. Mol. Biol. Cell 24, 3710-3720 (2013). doi: 10.1091/mbc. E13-07-0388; pmid: 24068324
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3710-3720
    • Hansen, S.D.1
  • 10
    • 84881251103 scopus 로고    scopus 로고
    • Danio rerio αE-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αE-catenin
    • pmid: 23788645
    • P. W. Miller et al., Danio rerio αE-catenin is a monomeric F-actin binding protein with distinct properties from Mus musculus αE-catenin. J. Biol. Chem. 288, 22324-22332 (2013). doi: 10.1074/jbc. M113.458406; pmid: 23788645
    • (2013) J. Biol. Chem. , vol.288 , pp. 22324-22332
    • Miller, P.W.1
  • 11
    • 0028981208 scopus 로고
    • α 1 (E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex
    • pmid: 7568023
    • D. L. Rimm, E. R. Koslov, P. Kebriaei, C. D. Cianci, J. S. Morrow, α 1 (E)-catenin is an actin-binding and -bundling protein mediating the attachment of F-actin to the membrane adhesion complex. Proc. Natl. Acad. Sci. U. S. A. 92, 8813-8817 (1995). doi: 10.1073/pnas.92.19.8813; pmid: 7568023
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 8813-8817
    • Rimm, D.L.1    Koslov, E.R.2    Kebriaei, P.3    Cianci, C.D.4    Morrow, J.S.5
  • 12
    • 84864506988 scopus 로고    scopus 로고
    • E-cadherin is under constitutive actomyosingenerated tension that is increased at cell-cell contacts upon externally applied stretch
    • pmid: 22802638
    • N. Borghi et al., E-cadherin is under constitutive actomyosingenerated tension that is increased at cell-cell contacts upon externally applied stretch. Proc. Natl. Acad. Sci. U. S. A. 109, 12568-12573 (2012). doi: 10.1073/pnas.1204390109; pmid: 22802638
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 12568-12573
    • Borghi, N.1
  • 13
    • 28344439885 scopus 로고    scopus 로고
    • α-catenin is a molecular switch that binds E-cadherin-β-catenin and regulates actin-filament assembly
    • pmid: 16325583
    • F. Drees, S. Pokutta, S. Yamada, W. J. Nelson, W. I. Weis, α-catenin is a molecular switch that binds E-cadherin-β-catenin and regulates actin-filament assembly. Cell 123, 903-915 (2005). doi: 10.1016/j.cell.2005.09.021; pmid: 16325583
    • (2005) Cell , vol.123 , pp. 903-915
    • Drees, F.1    Pokutta, S.2    Yamada, S.3    Nelson, W.J.4    Weis, W.I.5
  • 14
    • 84861856697 scopus 로고    scopus 로고
    • αE-catenin is an autoinhibited molecule that coactivates vinculin
    • pmid: 22586082
    • H. J. Choi et al., αE-catenin is an autoinhibited molecule that coactivates vinculin. Proc. Natl. Acad. Sci. U. S. A. 109, 8576-8581 (2012). doi: 10.1073/pnas.1203906109; pmid: 22586082
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 8576-8581
    • Choi, H.J.1
  • 15
    • 77953123743 scopus 로고    scopus 로고
    • α-Catenin as a tension transducer that induces adherens junction development
    • pmid: 20453849
    • S. Yonemura, Y. Wada, T. Watanabe, A. Nagafuchi, M. Shibata, α-Catenin as a tension transducer that induces adherens junction development. Nat. Cell Biol. 12, 533-542 (2010). doi: 10.1038/ncb2055; pmid: 20453849
    • (2010) Nat. Cell Biol. , vol.12 , pp. 533-542
    • Yonemura, S.1    Wada, Y.2    Watanabe, T.3    Nagafuchi, A.4    Shibata, M.5
  • 16
    • 84905482347 scopus 로고    scopus 로고
    • Force-dependent conformational switch of a-catenin controls vinculin binding
    • pmid: 25077739
    • M. Yao et al., Force-dependent conformational switch of a-catenin controls vinculin binding. Nat. Commun. 5, 4525 (2014). doi: 10.1038/n omms5525; pmid: 25077739
    • (2014) Nat. Commun. , vol.5 , pp. 4525
    • Yao, M.1
  • 17
    • 0031436412 scopus 로고    scopus 로고
    • Vinculin is associated th the E-cadherin adhesion complex
    • pm 9405455
    • R. B. Hazan, L. Kang, Roe, P. I. Borgen, D. L. Rimm, Vinculin is associated th the E-cadherin adhesion complex. J. Biol. Chem. 272, 32 48-32453 (1997). doi: 10.1074/jbc.272.51.32448; pm 9405455
    • (1997) J. Biol. Chem. , vol.272 , pp. 3248-32453
    • Hazan, R.B.1    Kang, L.2    Roe3    Borgen, P.I.4    Rimm, D.L.5
  • 18
    • 0032482254 scopus 로고    scopus 로고
    • Vinculin is art of the cadherin-catenin junctional complex: Complex for ation between a-catenin and vinculin
    • pmid: 9566974
    • E. E. Weiss, M. Kroemr, A. H. Rüdiger, B. M. Jockusch, M. Rüdiger, Vinculin is art of the cadherin-catenin junctional complex: Complex for ation between a-catenin and vinculin. J. Cell Biol. 141, 755-7 4 (1998). doi: 10.1083/jcb.141.3.755; pmid: 9566974
    • (1998) J. Cell Biol. , vol.141 , pp. 755-774
    • Weiss, E.E.1    Kroemr, M.2    Rüdiger, A.H.3    Jockusch, B.M.4    Rüdiger, M.5
  • 19
    • 38349138921 scopus 로고    scopus 로고
    • E IN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt
    • pmid: 18093941
    • K. Abe, M. Takeichi, E IN mediates linkage of the cadherin catenin complex to F-actin and stabilizes the circumferential actin belt. Proc. Natl. Acad. Sci. U. S. A. 105, 13-19 (2008). doi: 10.1073/pnas.0710504105; pmid: 18093941
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13-19
    • Abe, K.1    Takeichi, M.2
  • 20
    • 0028979956 scopus 로고
    • Interaction of α-actinin with the cadherin/catenin cell-cell adhesion complex via a-catenin
    • pmid: 7790378
    • K. A. Knudsen, A. P. Soler, K. R. Johnson, M. J. Wheelock, Interaction of α-actinin with the cadherin/catenin cell-cell adhesion complex via a-catenin. J. Cell Biol. 130, 67-77 (1995). doi: 10.1083/jcb.130.1.67; pmid: 7790378
    • (1995) J. Cell Biol. , vol.130 , pp. 67-77
    • Knudsen, K.A.1    Soler, A.P.2    Johnson, K.R.3    Wheelock, M.J.4
  • 21
    • 0037166245 scopus 로고    scopus 로고
    • Biochemical and structural definition of the l-afadin- and actinbinding sites of α-catenin
    • pmid: 11907041
    • S. Pokutta, F. Drees, Y. Takai, W. J. Nelson, W. I. Weis, Biochemical and structural definition of the l-afadin- and actinbinding sites of α-catenin. J. Biol. Chem. 277, 18868-18874 (2002). doi: 10.1074/jbc. M201463200; pmid: 11907041
    • (2002) J. Biol. Chem. , vol.277 , pp. 18868-18874
    • Pokutta, S.1    Drees, F.2    Takai, Y.3    Nelson, W.J.4    Weis, W.I.5
  • 22
    • 0034605062 scopus 로고    scopus 로고
    • Two cell adhesion molecules, nectin and cadherin, interact through their cytoplasmic domainassociated proteins
    • pmid: 10974003
    • K. Tachibana et al., Two cell adhesion molecules, nectin and cadherin, interact through their cytoplasmic domainassociated proteins. J. Cell Biol. 150, 1161-1176 (2000). doi: 10.1083/jcb.150.5.1161; pmid: 10974003
    • (2000) J. Cell Biol. , vol.150 , pp. 1161-1176
    • Tachibana, K.1
  • 23
    • 84964963599 scopus 로고    scopus 로고
    • Vinculin-dependent cadherin mechanosensing regulates efficient epithelial barrier formation
    • pmid: 23213393
    • F. Twiss et al., Vinculin-dependent cadherin mechanosensing regulates efficient epithelial barrier formation. Biol. Open 1, 1128-1140 (2012). doi: 10.1242/bio.20122428; pmid: 23213393
    • (2012) Biol. Open , vol.1 , pp. 1128-1140
    • Twiss, F.1
  • 24
    • 84859992640 scopus 로고    scopus 로고
    • Vinculin associates with endothelial VE-cadherin junctions to control force-dependent remodeling
    • pmid: 22391038
    • S. Huveneers et al., Vinculin associates with endothelial VE-cadherin junctions to control force-dependent remodeling. J. Cell Biol. 196, 641-652 (2012). doi: 10.1083/jcb.201108120; pmid: 22391038
    • (2012) J. Cell Biol. , vol.196 , pp. 641-652
    • Huveneers, S.1
  • 25
    • 77954410997 scopus 로고    scopus 로고
    • Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner
    • pmid: 20584916
    • Q. le Duc et al., Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner. J. Cell Biol. 189, 1107-1115 (2010). doi: 10.1083/jcb.201001149; pmid: 20584916
    • (2010) J. Cell Biol. , vol.189 , pp. 1107-1115
    • Le Duc, Q.1
  • 26
    • 84898925056 scopus 로고    scopus 로고
    • α-catenin cytomechanics: Role in cadherindependent adhesion and mechanotransduction
    • pmid: 24522187
    • A. K. Barry et al., α-catenin cytomechanics: Role in cadherindependent adhesion and mechanotransduction. J. Cell Sci. 127, 1779-1791 (2014). doi: 10.1242/jcs.139014; pmid: 24522187
    • (2014) J. Cell Sci. , vol.127 , pp. 1779-1791
    • Barry, A.K.1
  • 27
    • 84861562162 scopus 로고    scopus 로고
    • The cytoskeletal protein α-catenin unfurls upon binding to vinculin
    • pmid: 22493458
    • E. S. Rangarajan, T. Izard, The cytoskeletal protein α-catenin unfurls upon binding to vinculin. J. Biol. Chem. 287, 18492-18499 (2012). doi: 10.1074/jbc. M112.351023; pmid: 22493458
    • (2012) J. Biol. Chem. , vol.287 , pp. 18492-18499
    • Rangarajan, E.S.1    Izard, T.2
  • 28
    • 0037653696 scopus 로고    scopus 로고
    • Direct observation of catch bonds involving cell-adhesion molecules
    • pmid: 12736689
    • B. T. Marshall et al., Direct observation of catch bonds involving cell-adhesion molecules. Nature 423, 190-193 (2003). doi: 10.1038/nature01605; pmid: 12736689
    • (2003) Nature , vol.423 , pp. 190-193
    • Marshall, B.T.1
  • 29
    • 40149093643 scopus 로고    scopus 로고
    • Biophysics of catch bonds
    • pmid: 18573088
    • W. E. Thomas, V. Vogel, E. Sokurenko, Biophysics of catch bonds. Annu Rev Biophys 37, 399-416 (2008). doi: 10.1146/annurev. biophys.37.032807.125804; pmid: 18573088
    • (2008) Annu Rev Biophys , vol.37 , pp. 399-416
    • Thomas, W.E.1    Vogel, V.2    Sokurenko, E.3
  • 30
    • 33646088314 scopus 로고    scopus 로고
    • Catch-bond model derived from allostery explains force-activated bacterial adhesion
    • pmid: 16272438
    • W. Thomas et al., Catch-bond model derived from allostery explains force-activated bacterial adhesion. Biophys. J. 90, 753-764 (2006). doi: 10.1529/biophysj.105.066548; pmid: 16272438
    • (2006) Biophys. J. , vol.90 , pp. 753-764
    • Thomas, W.1
  • 31
    • 34547571737 scopus 로고    scopus 로고
    • Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion
    • pmid: 17646397
    • S. Yamada, W. J. Nelson, Localized zones of Rho and Rac activities drive initiation and expansion of epithelial cell-cell adhesion. J. Cell Biol. 178, 517-527 (2007). doi: 10.1083/jcb.200701058; pmid: 17646397
    • (2007) J. Cell Biol. , vol.178 , pp. 517-527
    • Yamada, S.1    Nelson, W.J.2
  • 32
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • pmid: 347575
    • G. I. Bell, Models for the specific adhesion of cells to cells. Science 200, 618-627 (1978). doi: 10.1126/science.347575; pmid: 347575
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 33
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force-lifetime- and chemistry in single molecular bonds
    • pmid: 11340054
    • E. Evans, Probing the relation between force-lifetime- and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30, 105-128 (2001). doi: 10.1146/annurev. biophys.30.1.105; pmid: 11340054
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 105-128
    • Evans, E.1
  • 34
    • 34547275473 scopus 로고
    • Brownian motion in a field of force and the diffusion model of chemical reactions
    • H. A. Kramers, Brownian motion in a field of force and the diffusion model of chemical reactions. Physica 7, 284-304 (1940). doi: 10.1016/S0031-8914 (40) 90098-2
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 35
    • 41349113512 scopus 로고    scopus 로고
    • Dynamic response of adhesion complexes: Beyond the single-path picture
    • pmid: 12059596
    • D. Bartolo, I. Derényi, A. Ajdari, Dynamic response of adhesion complexes: Beyond the single-path picture. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 65, 051910 (2002). doi: 10.1103/PhysRevE.65.051910; pmid: 12059596
    • (2002) Phys. Rev. E Stat. Nonlin. Soft Matter Phys. , vol.65 , pp. 051910
    • Bartolo, D.1    Derényi, I.2    Ajdari, A.3
  • 36
    • 3843151375 scopus 로고    scopus 로고
    • Mechanical switching and coupling between two dissociation pathways in a P-selectin adhesion bond
    • pmid: 15277675
    • E. Evans, A. Leung, V. Heinrich, C. Zhu, Mechanical switching and coupling between two dissociation pathways in a P-selectin adhesion bond. Proc. Natl. Acad. Sci. U. S. A. 101, 11281-11286 (2004). doi: 10.1073/pnas.0401870101; pmid: 15277675
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11281-11286
    • Evans, E.1    Leung, A.2    Heinrich, V.3    Zhu, C.4
  • 37
    • 13844309581 scopus 로고    scopus 로고
    • Dynamics of unbinding of cell adhesion molecules: Transition from catch to slip bonds
    • pmid: 15701706
    • V. Barsegov, D. Thirumalai, Dynamics of unbinding of cell adhesion molecules: Transition from catch to slip bonds. Proc. Natl. Acad. Sci. U. S. A. 102, 1835-1839 (2005). doi: 10.1073/pnas.0406938102; pmid: 15701706
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 1835-1839
    • Barsegov, V.1    Thirumalai, D.2
  • 38
    • 21244479320 scopus 로고    scopus 로고
    • Force history dependence of receptor-ligand dissociation
    • pmid: 15556978
    • B. T. Marshall, K. K. Sarangapani, J. Lou, R. P. McEver, C. Zhu, Force history dependence of receptor-ligand dissociation. Biophys. J. 88, 1458-1466 (2005). doi: 10.1529/biophysj. 104.050567; pmid: 15556978
    • (2005) Biophys. J. , vol.88 , pp. 1458-1466
    • Marshall, B.T.1    Sarangapani, K.K.2    Lou, J.3    McEver, R.P.4    Zhu, C.5
  • 39
    • 0035898657 scopus 로고    scopus 로고
    • Crystal structure of the M-fragment of α-catenin: Implications for modulation of cell adhesion
    • pmid: 11447106
    • J. Yang, P. Dokurno, N. K. Tonks, D. Barford, Crystal structure of the M-fragment of α-catenin: Implications for modulation of cell adhesion. EMBO J. 20, 3645-3656 (2001). doi: 10.1093/emboj/20.14.3645; pmid: 11447106
    • (2001) EMBO J. , vol.20 , pp. 3645-3656
    • Yang, J.1    Dokurno, P.2    Tonks, N.K.3    Barford, D.4
  • 40
    • 84873569278 scopus 로고    scopus 로고
    • Dimer asymmetry defines α-catenin interactions
    • pmid: 23292143
    • E. S. Rangarajan, T. Izard, Dimer asymmetry defines α-catenin interactions. Nat. Struct. Mol. Biol. 20, 188-193 (2013). doi: 10.1038/nsmb.2479; pmid: 23292143
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 188-193
    • Rangarajan, E.S.1    Izard, T.2
  • 41
    • 0033695362 scopus 로고    scopus 로고
    • Structure of the dimerization and b-catenin-binding region of a-catenin
    • pmid: 10882138
    • S. Pokutta, W. I. Weis, Structure of the dimerization and b-catenin-binding region of a-catenin. Mol. Cell 5, 533-543 (2000). doi: 10.1016/S1097-2765 (00) 80447-5; pmid: 10882138
    • (2000) Mol. Cell , vol.5 , pp. 533-543
    • Pokutta, S.1    Weis, W.I.2
  • 42
    • 84878387476 scopus 로고    scopus 로고
    • An autoinhibited structure of α-catenin and its implications for vinculin recruitment to adherens junctions
    • pmid: 23589308
    • N. Ishiyama et al., An autoinhibited structure of α-catenin and its implications for vinculin recruitment to adherens junctions. J. Biol. Chem. 288, 15913-15925 (2013). doi: 10.1074/jbc. M113.453928; pmid: 23589308
    • (2013) J. Biol. Chem. , vol.288 , pp. 15913-15925
    • Ishiyama, N.1
  • 43
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • pmid: 19564406
    • F. Kong, A. J. García, A. P. Mould, M. J. Humphries, C. Zhu, Demonstration of catch bonds between an integrin and its ligand. J. Cell Biol. 185, 1275-1284 (2009). doi: 10.1083/jcb.200810002; pmid: 19564406
    • (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
  • 44
    • 0346457092 scopus 로고    scopus 로고
    • Low force decelerates L-selectin dissociation from P-selectin glycoprotein ligand-1 and endoglycan
    • pmid: 14573602
    • K. K. Sarangapani et al., Low force decelerates L-selectin dissociation from P-selectin glycoprotein ligand-1 and endoglycan. J. Biol. Chem. 279, 2291-2298 (2004). doi: 10.1074/jbc. M310396200; pmid: 14573602
    • (2004) J. Biol. Chem. , vol.279 , pp. 2291-2298
    • Sarangapani, K.K.1
  • 45
    • 33745617696 scopus 로고    scopus 로고
    • Mechanics of actomyosin bonds in different nucleotide states are tuned to muscle contraction
    • pmid: 16785439
    • B. Guo, W. H. Guilford, Mechanics of actomyosin bonds in different nucleotide states are tuned to muscle contraction. Proc. Natl. Acad. Sci. U. S. A. 103, 9844-9849 (2006). doi: 10.1073/pnas.0601255103; pmid: 16785439
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 9844-9849
    • Guo, B.1    Guilford, W.H.2
  • 46
    • 84904245804 scopus 로고    scopus 로고
    • Loop 2 of myosin is a force-dependent inhibitor of the rigor bond
    • pmid: 24500136
    • A. M. Clobes, W. H. Guilford, Loop 2 of myosin is a force-dependent inhibitor of the rigor bond. J. Muscle Res. Cell Motil. 35, 143-152 (2014). doi: 10.1007/s10974-014-9375-z; pmid: 24500136
    • (2014) J. Muscle Res. Cell Motil. , vol.35 , pp. 143-152
    • Clobes, A.M.1    Guilford, W.H.2
  • 48
    • 84901929348 scopus 로고    scopus 로고
    • Resolving the molecular mechanism of cadherin catch bond formation
    • pmid: 24887573
    • K. Manibog, H. Li, S. Rakshit, S. Sivasankar, Resolving the molecular mechanism of cadherin catch bond formation. Nat. Commun. 5, 3941 (2014). doi: 10.1038/ncomms4941; pmid: 24887573
    • (2014) Nat. Commun. , vol.5 , pp. 3941
    • Manibog, K.1    Li, H.2    Rakshit, S.3    Sivasankar, S.4
  • 49
    • 33847780609 scopus 로고    scopus 로고
    • A structure-based sliding-rebinding mechanism for catch bonds
    • pmid: 17142266
    • J. Lou, C. Zhu, A structure-based sliding-rebinding mechanism for catch bonds. Biophys. J. 92, 1471-1485 (2007). doi: 10.1529/biophysj.106.097048; pmid: 17142266
    • (2007) Biophys. J. , vol.92 , pp. 1471-1485
    • Lou, J.1    Zhu, C.2
  • 50
    • 58549108194 scopus 로고    scopus 로고
    • Structural basis for selectin mechanochemistry
    • pmid: 19118197
    • T. A. Springer, Structural basis for selectin mechanochemistry. Proc. Natl. Acad. Sci. U. S. A. 106, 91-96 (2009). doi: 10.1073/pnas.0810784105; pmid: 19118197
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 91-96
    • Springer, T.A.1
  • 51
    • 84903463890 scopus 로고    scopus 로고
    • Plasticity of hydrogen bond networks regulates mechanochemistry of cell adhesion complexes
    • pmid: 24927549
    • S. Chakrabarti, M. Hinczewski, D. Thirumalai, Plasticity of hydrogen bond networks regulates mechanochemistry of cell adhesion complexes. Proc. Natl. Acad. Sci. U. S. A. 111, 9048-9053 (2014). doi: 10.1073/pnas. 1405384111; pmid: 24927549
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 9048-9053
    • Chakrabarti, S.1    Hinczewski, M.2    Thirumalai, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.