메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Dynamic catch of a Thy-1-α5 β1 +syndecan-4 trimolecular complex

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOHEXIMIDE; GLYCOPROTEIN IB ALPHA; INTEGRIN RECEPTOR; MYOSIN II; SELECTIN; SHORT HAIRPIN RNA; SMALL INTERFERING RNA; SYNDECAN 4; T LYMPHOCYTE RECEPTOR; THY 1 ANTIGEN; UVOMORULIN; VERY LATE ACTIVATION ANTIGEN 5; BETA1 INTEGRIN; PROTEIN BINDING; RECOMBINANT PROTEIN;

EID: 84923372800     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5886     Document Type: Article
Times cited : (83)

References (70)
  • 1
    • 50849132538 scopus 로고    scopus 로고
    • Cells on the run: Shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells
    • Alon, R., & Ley, K. Cells on the run: shear-regulated integrin activation in leukocyte rolling and arrest on endothelial cells. Curr. Opin. Cell Biol. 20, 525-532 (2008).
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 525-532
    • Alon, R.1    Ley, K.2
  • 2
    • 0019554463 scopus 로고
    • Rat brain thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic region
    • Campbell, D. G., Gagnon, J., Reid, K. B., & Williams, A. F. Rat brain Thy-1 glycoprotein. The amino acid sequence, disulphide bonds and an unusual hydrophobic region. Biochem. J. 195, 15-30 (1981).
    • (1981) Biochem. J. , vol.195 , pp. 15-30
    • Campbell, D.G.1    Gagnon, J.2    Reid, K.B.3    Williams, A.4
  • 3
    • 1542619244 scopus 로고    scopus 로고
    • Human thy-1 (cd90) on activated endothelial cells is a counterreceptor for the leukocyte integrin mac-1 (cd11b/cd18
    • Wetzel, A. et al. Human Thy-1 (CD90) on activated endothelial cells is a counterreceptor for the leukocyte integrin Mac-1 (CD11b/CD18). J. Immunol. 172, 3850-3859 (2004).
    • (2004) J. Immunol. , vol.172 , pp. 3850-3859
    • Wetzel, A.1
  • 4
    • 33644653390 scopus 로고    scopus 로고
    • Increased neutrophil adherence in psoriasis: Role of the human endothelial cell receptor thy-1 (cd90
    • Wetzel, A. et al. Increased neutrophil adherence in psoriasis: role of the human endothelial cell receptor Thy-1 (CD90). J. Invest. Dermatol. 126, 441-452 (2006).
    • (2006) J. Invest. Dermatol. , vol.126 , pp. 441-452
    • Wetzel, A.1
  • 5
    • 22744438812 scopus 로고    scopus 로고
    • Interaction of human thy-1 (cd 90) with the integrin alphavbeta3 (cd51/cd61): An important mechanism mediating melanoma cell adhesion to activated endothelium
    • Saalbach, A. et al. Interaction of human Thy-1 (CD 90) with the integrin alphavbeta3 (CD51/CD61): an important mechanism mediating melanoma cell adhesion to activated endothelium. Oncogene 24, 4710-4720 (2005).
    • (2005) Oncogene , vol.24 , pp. 4710-4720
    • Saalbach, A.1
  • 6
    • 43749088702 scopus 로고    scopus 로고
    • Direct thy-1/alphavbeta3 integrin interaction mediates neuron to astrocyte communication
    • Hermosilla, T. et al. Direct Thy-1/alphaVbeta3 integrin interaction mediates neuron to astrocyte communication. Biochim. Biophys. Acta 1783, 1111-1120 (2008).
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1111-1120
    • Hermosilla, T.1
  • 7
    • 70350371490 scopus 로고    scopus 로고
    • Neuronal thy-1 induces astrocyte adhesion by engaging syndecan-4 in a cooperative interaction with alphavbeta3 integrin that activates pkcalpha and rhoa
    • Avalos, A. M. et al. Neuronal Thy-1 induces astrocyte adhesion by engaging syndecan-4 in a cooperative interaction with alphavbeta3 integrin that activates PKCalpha and RhoA. J. Cell Sci. 122, 3462-3471 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 3462-3471
    • Avalos, A.M.1
  • 8
    • 77954568888 scopus 로고    scopus 로고
    • Thy-1-integrin alphav beta5 interactions inhibit lung fibroblast contraction-induced latent transforming growth factor-beta1 activation and myofibroblast differentiation
    • Zhou, Y., Hagood, J. S., Lu, B., Merryman, W. D., & Murphy-Ullrich, J. E. Thy-1-integrin alphav beta5 interactions inhibit lung fibroblast contraction-induced latent transforming growth factor-beta1 activation and myofibroblast differentiation. J. Biol. Chem. 285, 22382-22393 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 22382-22393
    • Zhou, Y.1    Hagood, J.S.2    Lu, B.3    Merryman, W.D.4    Murphy-Ullrich, J.E.5
  • 9
    • 67349184767 scopus 로고    scopus 로고
    • Getting a grip on thy-1 signaling
    • Barker, T. H., & Hagood, J. S. Getting a grip on Thy-1 signaling. Biochim. Biophys. Acta 1793, 921-923 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 921-923
    • Barker, T.H.1    Hagood, J.S.2
  • 10
    • 0020318329 scopus 로고
    • Neuronal cell thy-1 glycoprotein: Homology with immunoglobulin
    • Williams, A. F., & Gagnon, J. Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin. Science 216, 696-703 (1982).
    • (1982) Science , vol.216 , pp. 696-703
    • Williams, A.F.1    Gagnon, J.2
  • 11
    • 0036018623 scopus 로고    scopus 로고
    • The thy-1/thy-1 ligand interaction is involved in binding of melanoma cells to activated thy-1-positive microvascular endothelial cells
    • Saalbach, A., Hildebrandt, G., Haustein, U.-F., & Anderegg, U. The Thy-1/Thy-1 ligand interaction is involved in binding of melanoma cells to activated Thy-1-positive microvascular endothelial cells. Microvasc. Res. 64, 86-93 (2002).
    • (2002) Microvasc. Res. , vol.64 , pp. 86-93
    • Saalbach, A.1    Hildebrandt, G.2    Haustein, U.-F.3    Anderegg, U.4
  • 12
    • 84871279341 scopus 로고    scopus 로고
    • Melanoma cells use thy-1 (cd90) on endothelial cells for metastasis formation
    • Schubert, K., Gutknecht, D., Köberle, M., Anderegg, U., & Saalbach, A. Melanoma cells use Thy-1 (CD90) on endothelial cells for metastasis formation. Am. J. Pathol. 182, 266-276 (2013).
    • (2013) Am. J. Pathol. , vol.182 , pp. 266-276
    • Schubert, K.1    Gutknecht, D.2    Köberle, M.3    Anderegg, U.4    Saalbach, A.5
  • 13
    • 0034682892 scopus 로고    scopus 로고
    • Genes expressed in human tumor endothelium
    • StCroix, B. et al. Genes expressed in human tumor endothelium. Science 289, 1197-1202 (2000).
    • (2000) Science , vol.289 , pp. 1197-1202
    • Stcroix, B.1
  • 14
    • 0037113167 scopus 로고    scopus 로고
    • Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signalling
    • Bass, M., & Humphries, M. Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signalling. Biochem. J. 368, 1 (2002).
    • (2002) Biochem. J. , vol.368 , pp. 1
    • Bass, M.1    Humphries, M.2
  • 15
    • 34248159909 scopus 로고    scopus 로고
    • Syndecan-4-dependent rac1 regulation determines directional migration in response to the extracellular matrix
    • Bass, M. D. et al. Syndecan-4-dependent Rac1 regulation determines directional migration in response to the extracellular matrix. J. Cell Biol. 177, 527-538 (2007).
    • (2007) J. Cell Biol. , vol.177 , pp. 527-538
    • Bass, M.D.1
  • 16
    • 0033017955 scopus 로고    scopus 로고
    • Syndecan-4 signals cooperatively with integrins in a rho-dependent manner in the assembly of focal adhesions and actin stress fibers
    • Saoncella, S. et al. Syndecan-4 signals cooperatively with integrins in a Rho-dependent manner in the assembly of focal adhesions and actin stress fibers. Proc. Natl Acad. Sci. USA 96, 2805-2810 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 2805-2810
    • Saoncella, S.1
  • 17
    • 33746918654 scopus 로고    scopus 로고
    • Pkcbeta-dependent activation of rhoa by syndecan-4 during focal adhesion formation
    • Dovas, A., Yoneda, A., & Couchman, J. R. PKCbeta-dependent activation of RhoA by syndecan-4 during focal adhesion formation. J. Cell Sci. 119, 2837-2846 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 2837-2846
    • Dovas, A.1    Yoneda, A.2    Couchman, J.R.3
  • 18
    • 45349086241 scopus 로고    scopus 로고
    • P190rhogap is the convergence point of adhesion signals from alpha beta 1 integrin and syndecan-4
    • Bass, M. D. et al. p190RhoGAP is the convergence point of adhesion signals from alpha beta 1 integrin and syndecan-4. J. Cell Biol. 181, 1013-1026 (2008).
    • (2008) J. Cell Biol. , vol.181 , pp. 1013-1026
    • Bass, M.D.1
  • 19
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: Integrating cytoskeletal dynamics and cellular tension
    • Parsons, J. T., Horwitz, A. R., & Schwartz, M. A. Cell adhesion: integrating cytoskeletal dynamics and cellular tension. Nat. Rev. Mol. Cell. Biol. 11, 633-643 (2010).
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 20
    • 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. Nat. Cell. Biol. 3, 466-472 (2001).
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 466-472
    • Balaban, N.Q.1
  • 21
    • 79960325552 scopus 로고    scopus 로고
    • Spatiotemporal constraints on the force-dependent growth of focal adhesions
    • Stricker, J., Aratyn-Schaus, Y., Oakes, P. W., & Gardel, M. L. Spatiotemporal constraints on the force-dependent growth of focal adhesions. Biophys. J. 100, 2883-2893 (2011).
    • (2011) Biophys. J. , vol.100 , pp. 2883-2893
    • Stricker, J.1    Aratyn-Schaus, Y.2    Oakes, P.W.3    Gardel, M.L.4
  • 22
    • 84869111112 scopus 로고    scopus 로고
    • United we stand: Integrating the actin cytoskeleton and cell-matrix adhesions in cellular mechanotransduction
    • Schwarz, U. S., & Gardel, M. L. United we stand: integrating the actin cytoskeleton and cell-matrix adhesions in cellular mechanotransduction. J. Cell Sci. 125, 3051-3060 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 3051-3060
    • Schwarz, U.S.1    Gardel, M.L.2
  • 23
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • Zaidel-Bar, R., Ballestrem, C., Kam, Z., & Geiger, B. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J. Cell Sci. 116, 4605-4613 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 24
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha5beta1 function
    • Friedland, J. C., Lee, M. H., & Boettiger, D. Mechanically activated integrin switch controls alpha5beta1 function. Science 323, 642-644 (2009).
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 25
    • 79957889032 scopus 로고    scopus 로고
    • The rho gefs larg and gef-h1 regulate the mechanical response to force on integrins
    • Guilluy, C. et al. The Rho GEFs LARG and GEF-H1 regulate the mechanical response to force on integrins. Nat. Cell Biol. 13, 722-727 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 722-727
    • Guilluy, C.1
  • 26
    • 79955441991 scopus 로고    scopus 로고
    • Balancing forces: Architectural control of mechanotransduction
    • DuFort, C. C., Paszek, M. J., & Weaver, V. M. Balancing forces: architectural control of mechanotransduction. Nat. Rev. Mol. Cell. Biol. 12, 308-319 (2011).
    • (2011) Nat. Rev. Mol. Cell. Biol. , vol.12 , pp. 308-319
    • Dufort, C.C.1    Paszek, M.J.2    Weaver, V.M.3
  • 27
    • 84869102195 scopus 로고    scopus 로고
    • Finding the weakest link: Exploring integrin-mediated mechanical molecular pathways
    • Roca-Cusachs, P., Iskratsch, T., & Sheetz, M. P. Finding the weakest link: exploring integrin-mediated mechanical molecular pathways. J. Cell Sci. 125, 3025-3038 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 3025-3038
    • Roca-Cusachs, P.1    Iskratsch, T.2    Sheetz, M.P.3
  • 28
    • 78149245953 scopus 로고    scopus 로고
    • Forcing switch from short-to intermediate-And long-lived states of the a 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 A domain generates LFA-1/ICAM-1 catch bonds. J. Biol. Chem. 285, 35967-35978 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 35967-35978
    • Chen, W.1    Lou, J.2    Zhu, C.3
  • 29
    • 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
  • 30
    • 84887430287 scopus 로고    scopus 로고
    • The n-terminal flanking region of the a1 domain regulates the force-dependent binding of von willebrand factor to platelet glycoprotein iba
    • Ju, L., Dong, J.-F., Cruz, M. A., & Zhu, C. The N-terminal flanking region of the A1 domain regulates the force-dependent binding of von Willebrand factor to platelet glycoprotein Iba. J. Biol. Chem. 288, 32289-32301 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 32289-32301
    • Ju, L.1    Dong, J.-F.2    Cruz, M.A.3    Zhu, C.4
  • 31
    • 84898644308 scopus 로고    scopus 로고
    • Accumulation of dynamic catch bonds between tcr and agonist peptide-mhc triggers t cell signaling
    • Liu, B., Chen, W., Evavold, B. D., & Zhu, C. Accumulation of dynamic catch bonds between tcr and agonist peptide-MHC triggers T cell signaling. Cell 157, 357-368 (2014).
    • (2014) Cell , vol.157 , pp. 357-368
    • Liu, B.1    Chen, W.2    Evavold, B.D.3    Zhu, C.4
  • 32
    • 84882747419 scopus 로고    scopus 로고
    • Single-molecule approaches embrace molecular cohorts
    • Ha, T. Single-molecule approaches embrace molecular cohorts. Cell 154, 723-726 (2013).
    • (2013) Cell , vol.154 , pp. 723-726
    • Ha, T.1
  • 33
    • 84867345947 scopus 로고    scopus 로고
    • Catch bonds
    • Hertig, S., & Vogel, V. Catch bonds. Curr. Biol. 22, R823-R825 (2012).
    • (2012) Curr. Biol. , vol.22 , pp. R823-R825
    • Hertig, S.1    Vogel, V.2
  • 34
    • 84899010469 scopus 로고    scopus 로고
    • Mechanochemistry: A molecular biomechanics view of mechanosensing-springer
    • Zhu, C. Mechanochemistry: a molecular biomechanics view of mechanosensing-springer. Ann. Biomed. Eng. 42, 388-404 (2013).
    • (2013) Ann. Biomed. Eng. , vol.42 , pp. 388-404
    • Zhu, C.1
  • 35
    • 50249122663 scopus 로고    scopus 로고
    • Catch bonds in adhesion
    • Thomas, W. Catch bonds in adhesion. Annu. Rev. Biomed. Eng. 10, 39-57 (2008).
    • (2008) Annu. Rev. Biomed. Eng. , vol.10 , pp. 39-57
    • Thomas, W.1
  • 37
    • 84875610297 scopus 로고    scopus 로고
    • Neutrophil rolling at high shear: Flattening, catch bond behavior, tethers and slings
    • Sundd, P., Pospieszalska, M. K., & Ley, K. Neutrophil rolling at high shear: flattening, catch bond behavior, tethers and slings. Mol. Immunol. 55, 59-69 (2013).
    • (2013) Mol. Immunol. , vol.55 , pp. 59-69
    • Sundd, P.1    Pospieszalska, M.K.2    Ley, K.3
  • 38
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong, F., Garcia, A. J., Mould, A. P., Humphries, M. J., & Zhu, C. Demonstration of catch bonds between an integrin and its ligand. J. Cell Biol. 185, 1275-1284 (2009).
    • (2009) J. Cell Biol. , vol.185 , pp. 1275-1284
    • Kong, F.1    Garcia, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 39
    • 84891952179 scopus 로고    scopus 로고
    • Dynamic control of b1 integrin adhesion by the plexind1-sema3e axis
    • Choi, Y. I. et al. Dynamic control of b1 integrin adhesion by the plexinD1-sema3E axis. Proc. Natl Acad. Sci. USA 111, 379-384 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.111 , pp. 379-384
    • Choi, Y.I.1
  • 40
    • 0037653696 scopus 로고    scopus 로고
    • Direct observation of catch bonds involving cell-Adhesion molecules
    • Marshall, B. T. et al. Direct observation of catch bonds involving cell-Adhesion molecules. Nature 423, 190-193 (2003).
    • (2003) Nature , vol.423 , pp. 190-193
    • Marshall, B.T.1
  • 41
    • 0346457092 scopus 로고    scopus 로고
    • Low force decelerates l-selectin dissociation from p-selectin glycoprotein ligand-1 and endoglycan
    • Sarangapani, K. K. et al. Low force decelerates L-selectin dissociation from P-selectin glycoprotein ligand-1 and endoglycan. J. Biol. Chem. 279, 2291-2298 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 2291-2298
    • Sarangapani, K.K.1
  • 42
    • 51349154185 scopus 로고    scopus 로고
    • Platelet glycoprotein ibalpha forms catch bonds with human wt vwf but not with type 2b von willebrand disease vwf
    • Yago, T. et al. Platelet glycoprotein Ibalpha forms catch bonds with human WT vWF but not with type 2B von Willebrand disease vWF. J. Clin. Invest. 118, 3195-3207 (2008).
    • (2008) J. Clin. Invest. , vol.118 , pp. 3195-3207
    • Yago, T.1
  • 44
    • 77952513211 scopus 로고    scopus 로고
    • Structural basis for mechanical force regulation of the adhesin fimh via finger trap-like b sheet twisting
    • Le Trong, I. et al. Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like b sheet twisting. Cell 141, 645-655 (2010).
    • (2010) Cell , vol.141 , pp. 645-655
    • Le Trong, I.1
  • 45
    • 78649476255 scopus 로고    scopus 로고
    • Tension directly stabilizes reconstituted kinetochoremicrotubule attachments
    • Akiyoshi, B. et al. Tension directly stabilizes reconstituted kinetochoremicrotubule attachments. Nature 468, 576-579 (2010).
    • (2010) Nature , vol.468 , pp. 576-579
    • Akiyoshi, B.1
  • 46
    • 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
  • 47
    • 84878598076 scopus 로고    scopus 로고
    • B1-And av-class integrins cooperate to regulate myosin ii during rigidity sensing of fibronectin-based microenvironments
    • Schiller, H. B. et al. b1-And av-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. Nat. Cell. Biol. 15, 625-636 (2013).
    • (2013) Nat. Cell. Biol. , vol.15 , pp. 625-636
    • Schiller, H.B.1
  • 48
    • 0035838390 scopus 로고    scopus 로고
    • Thy-1 binds to integrin beta(3) on astrocytes and triggers formation of focal contact sites
    • Leyton, L. et al. Thy-1 binds to integrin beta(3) on astrocytes and triggers formation of focal contact sites. Curr. Biol. 11, 1028-1038 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1028-1038
    • Leyton, L.1
  • 49
    • 0023198059 scopus 로고
    • Characterization of the cell surface heterodimer vla-4 and related peptides
    • Hemler, M. E. et al. Characterization of the cell surface heterodimer VLA-4 and related peptides. J. Biol. Chem. 262, 11478-11485 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 11478-11485
    • Hemler, M.E.1
  • 50
    • 0029878968 scopus 로고    scopus 로고
    • Stimulation of fibroblast growth factor receptor-1 occupancy and signaling by cell surface-Associated syndecans and glypican
    • Steinfeld, R., Van Den Berghe, H., & David, G. Stimulation of fibroblast growth factor receptor-1 occupancy and signaling by cell surface-Associated syndecans and glypican. J. Cell Biol. 133, 405-416 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 405-416
    • Steinfeld, R.1    Van Den Berghe, H.2    David, G.3
  • 51
    • 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
  • 52
    • 84880795356 scopus 로고    scopus 로고
    • Thy-1-interacting molecules and cellular signaling in cis and trans
    • Herrera-Molina, R. et al. Thy-1-interacting molecules and cellular signaling in cis and trans. Int. Rev. Cell. Mol. Biol. 305, 163-216 (2013).
    • (2013) Int. Rev. Cell. Mol. Biol. , vol.305 , pp. 163-216
    • Herrera-Molina, R.1
  • 53
    • 78751696945 scopus 로고    scopus 로고
    • Two-stage cooperative t cell receptor-peptide major histocompatibility complex-cd8 trimolecular interactions amplify antigen discrimination
    • Jiang, N. et al. Two-stage cooperative T cell receptor-peptide major histocompatibility complex-CD8 trimolecular interactions amplify antigen discrimination. Immunity 34, 13-23 (2011).
    • (2011) Immunity , vol.34 , pp. 13-23
    • Jiang, N.1
  • 54
    • 0033808405 scopus 로고    scopus 로고
    • Modeling concurrent binding of multiple molecular species in cell adhesion
    • Zhu, C., & Williams, T. E. Modeling concurrent binding of multiple molecular species in cell adhesion. Biophys. J. 79, 1850-1857 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 1850-1857
    • Zhu, C.1    Williams, T.E.2
  • 56
    • 80054759061 scopus 로고    scopus 로고
    • A syndecan-4 hair trigger initiates wound healing through caveolin-And rhog-regulated integrin endocytosis
    • Bass, M. D. et al. A syndecan-4 hair trigger initiates wound healing through caveolin-And RhoG-regulated integrin endocytosis. Dev. Cell 21, 681-693 (2011).
    • (2011) Dev. Cell , vol.21 , pp. 681-693
    • Bass, M.D.1
  • 57
    • 84875259429 scopus 로고    scopus 로고
    • Syndecan-4 phosphorylation is a control point for integrin recycling
    • Morgan, M. R. et al. Syndecan-4 phosphorylation is a control point for integrin recycling. Dev. Cell 24, 472-485 (2013).
    • (2013) Dev. Cell , vol.24 , pp. 472-485
    • Morgan, M.R.1
  • 58
    • 84899010469 scopus 로고    scopus 로고
    • Mechanochemistry: A molecular biomechanics view of mechanosensing
    • Zhu, C. Mechanochemistry: a molecular biomechanics view of mechanosensing. Ann. Biomed. Eng. 42, 388-404 (2013).
    • (2013) Ann. Biomed. Eng. , vol.42 , pp. 388-404
    • Zhu, C.1
  • 59
    • 79959636906 scopus 로고    scopus 로고
    • The physics of cancer: The role of physical interactions and mechanical forces in metastasis
    • Wirtz, D., Konstantopoulos, K., & Searson, P. C. The physics of cancer: the role of physical interactions and mechanical forces in metastasis. Nat. Rev. Cancer 11, 512-522 (2011).
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 512-522
    • Wirtz, D.1    Konstantopoulos, K.2    Searson, P.C.3
  • 60
    • 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
  • 61
    • 33751335857 scopus 로고    scopus 로고
    • Force sensing by mechanical extension of the src family kinase substrate p130cas
    • Sawada, Y. et al. Force sensing by mechanical extension of the Src family kinase substrate p130Cas. Cell 127, 1015-1026 (2006).
    • (2006) Cell , vol.127 , pp. 1015-1026
    • Sawada, Y.1
  • 62
    • 79251534982 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans mediate interstitial flow mechanotransduction regulating mmp-13 expression and cell motility via fak-erk in 3d collagen
    • Shi, Z. D., Wang, H., & Tarbell, J. M. Heparan sulfate proteoglycans mediate interstitial flow mechanotransduction regulating MMP-13 expression and cell motility via FAK-ERK in 3D collagen. PLoS ONE 6, e15956 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e15956
    • Shi, Z.D.1    Wang, H.2    Tarbell, J.M.3
  • 63
    • 77955774525 scopus 로고    scopus 로고
    • Use of molecular beacons to image effects of titanium surface microstructure on beta1 integrin expression in live osteoblast-like cells
    • Lennon, F. E. et al. Use of molecular beacons to image effects of titanium surface microstructure on beta1 integrin expression in live osteoblast-like cells. Biomaterials 31, 7640-7647 (2010).
    • (2010) Biomaterials , vol.31 , pp. 7640-7647
    • Lennon, F.E.1
  • 64
    • 0035929622 scopus 로고    scopus 로고
    • Ogeneration of a minimal alpha5beta1 integrin-fc fragment
    • Coe, A. P. et al. Generation of a minimal alpha5beta1 integrin-Fc fragment. J. Biol. Chem. 276, 35854-35866 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35854-35866
    • Coe, A.P.1
  • 65
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-ii-responsive focal adhesion proteome reveals a role for b-pix in negative regulation of focal adhesion maturation
    • Kuo, J.-C., Han, X., Hsiao, C.-T., Yates, J. R., & Waterman, C. M. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for b-Pix in negative regulation of focal adhesion maturation. Nat. Cell. Biol. 13, 383-393 (2011).
    • (2011) Nat. Cell. Biol. , vol.13 , pp. 383-393
    • Kuo, J.-C.1    Han, X.2    Hsiao, C.-T.3    Yates, J.R.4    Waterman, C.M.5
  • 66
    • 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
  • 67
    • 84859387007 scopus 로고    scopus 로고
    • Tension is required but not sufficient for focal adhesion maturation without a stress fiber template
    • Oakes, P. W., Beckham, Y., Stricker, J., & Gardel, M. L. Tension is required but not sufficient for focal adhesion maturation without a stress fiber template. J. Cell Biol. 196, 363-374 (2012).
    • (2012) J. Cell Biol. , vol.196 , pp. 363-374
    • Oakes, P.W.1    Beckham, Y.2    Stricker, J.3    Gardel, M.L.4
  • 68
    • 0037135977 scopus 로고    scopus 로고
    • Distinct molecular and cellular contributions to stabilizing selectin-mediated rolling under flow
    • Yago, T. et al. Distinct molecular and cellular contributions to stabilizing selectin-mediated rolling under flow. J. Cell Biol. 158, 787-799 (2002).
    • (2002) J. Cell Biol. , vol.158 , pp. 787-799
    • Yago, T.1
  • 69
    • 0031682733 scopus 로고    scopus 로고
    • Measuring two-dimensional receptor-ligand binding kinetics by micropipette
    • Chesla, S., Selvaraj, P., & Zhu, C. Measuring two-dimensional receptor-ligand binding kinetics by micropipette. Biophys. J. 75, 1553-1572 (1998).
    • (1998) Biophys. J. , vol.75 , pp. 1553-1572
    • Chesla, S.1    Selvaraj, P.2    Zhu, C.3
  • 70
    • 33644970620 scopus 로고    scopus 로고
    • Measuring molecular elasticity by atomic force microscope cantilever fluctuations
    • Marshall, B. T. et al. Measuring molecular elasticity by atomic force microscope cantilever fluctuations. Biophys. J. 90, 681-692 (2006).
    • (2006) Biophys. J. , vol.90 , pp. 681-692
    • Marshall, B.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.