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Volumn 104, Issue 8, 2013, Pages 1670-1675

Improved ligand discrimination by force-induced unbinding of the T cell receptor from peptide-MHC

Author keywords

[No Author keywords available]

Indexed keywords

HISTOCOMPATIBILITY ANTIGEN; LIGAND; LYMPHOCYTE ANTIGEN RECEPTOR; PEPTIDE;

EID: 84876376859     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2013.03.023     Document Type: Article
Times cited : (36)

References (25)
  • 1
    • 79958213129 scopus 로고    scopus 로고
    • Antigen potency and maximal efficacy reveal a mechanism of efficient T cell activation
    • O. Dushek, and M. Aleksic P.A. van der Merwe Antigen potency and maximal efficacy reveal a mechanism of efficient T cell activation Sci. Signal. 4 2011 ra39
    • (2011) Sci. Signal. , vol.4 , pp. 39
    • Dushek, O.1    Aleksic, M.2    Van Der Merwe, P.A.3
  • 2
    • 0032438551 scopus 로고    scopus 로고
    • High- and low-potency ligands with similar affinities for the TCR: The importance of kinetics in TCR signaling
    • G.J. Kersh, and E.N. Kersh P.M. Allen High- and low-potency ligands with similar affinities for the TCR: the importance of kinetics in TCR signaling Immunity 9 1998 817 826
    • (1998) Immunity , vol.9 , pp. 817-826
    • Kersh, G.J.1    Kersh, E.N.2    Allen, P.M.3
  • 3
    • 0029063148 scopus 로고
    • Kinetic proofreading in T-cell receptor signal transduction
    • T.W. McKeithan Kinetic proofreading in T-cell receptor signal transduction Proc. Natl. Acad. Sci. USA 92 1995 5042 5046
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5042-5046
    • McKeithan, T.W.1
  • 4
    • 23344444616 scopus 로고    scopus 로고
    • T cell activation: Kinetic proofreading, serial engagement and cell adhesion
    • D. Coombs, and B. Goldstein T cell activation: kinetic proofreading, serial engagement and cell adhesion J. Comput. Appl. Math. 184 2005 121 139
    • (2005) J. Comput. Appl. Math. , vol.184 , pp. 121-139
    • Coombs, D.1    Goldstein, B.2
  • 6
    • 77249114784 scopus 로고    scopus 로고
    • TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity
    • J.B. Huppa, and M. Axmann M.M. Davis TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity Nature 463 2010 963 967
    • (2010) Nature , vol.463 , pp. 963-967
    • Huppa, J.B.1    Axmann, M.2    Davis, M.M.3
  • 7
    • 84864775640 scopus 로고    scopus 로고
    • Determination of interaction kinetics between the T cell receptor and peptide-loaded MHC class II via single-molecule diffusion measurements
    • M. Axmann, and J.B. Huppa G.J. Schütz Determination of interaction kinetics between the T cell receptor and peptide-loaded MHC class II via single-molecule diffusion measurements Biophys. J. 103 2012 L17 L19
    • (2012) Biophys. J. , vol.103
    • Axmann, M.1    Huppa, J.B.2    Schütz, G.J.3
  • 8
    • 77950809538 scopus 로고    scopus 로고
    • The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness
    • J. Huang, and V.I. Zarnitsyna C. Zhu The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness Nature 464 2010 932 936
    • (2010) Nature , vol.464 , pp. 932-936
    • Huang, J.1    Zarnitsyna, V.I.2    Zhu, C.3
  • 9
    • 84856020544 scopus 로고    scopus 로고
    • Kinetics and mechanics of two-dimensional interactions between T cell receptors and different activating ligands
    • P. Robert, and M. Aleksic P.A. van der Merwe Kinetics and mechanics of two-dimensional interactions between T cell receptors and different activating ligands Biophys. J. 102 2012 248 257
    • (2012) Biophys. J. , vol.102 , pp. 248-257
    • Robert, P.1    Aleksic, M.2    Van Der Merwe, P.A.3
  • 10
    • 79955904928 scopus 로고    scopus 로고
    • Force generation upon T cell receptor engagement
    • J. Husson, and K. Chemin N. Henry Force generation upon T cell receptor engagement PLoS ONE 6 2011 e19680
    • (2011) PLoS ONE , vol.6 , pp. 19680
    • Husson, J.1    Chemin, K.2    Henry, N.3
  • 11
    • 43849096279 scopus 로고    scopus 로고
    • How cells tiptoe on adhesive surfaces before sticking
    • A. Pierres, and A.M. Benoliel P. Bongrand How cells tiptoe on adhesive surfaces before sticking Biophys. J. 94 2008 4114 4122
    • (2008) Biophys. J. , vol.94 , pp. 4114-4122
    • Pierres, A.1    Benoliel, A.M.2    Bongrand, P.3
  • 12
    • 10044247245 scopus 로고    scopus 로고
    • Pattern formation during T-cell adhesion
    • T.R. Weikl, and R. Lipowsky Pattern formation during T-cell adhesion Biophys. J. 87 2004 3665 3678
    • (2004) Biophys. J. , vol.87 , pp. 3665-3678
    • Weikl, T.R.1    Lipowsky, R.2
  • 13
    • 84863482471 scopus 로고    scopus 로고
    • Biophysical mechanism of T-cell receptor triggering in a reconstituted system
    • J.R. James, and R.D. Vale Biophysical mechanism of T-cell receptor triggering in a reconstituted system Nature 487 2012 64 69
    • (2012) Nature , vol.487 , pp. 64-69
    • James, J.R.1    Vale, R.D.2
  • 14
    • 84858759719 scopus 로고    scopus 로고
    • Mechanical modulation of receptor-ligand interactions at cell-cell interfaces
    • J.F. Allard, and O. Dushek P.A. van der Merwe Mechanical modulation of receptor-ligand interactions at cell-cell interfaces Biophys. J. 102 2012 1265 1273
    • (2012) Biophys. J. , vol.102 , pp. 1265-1273
    • Allard, J.F.1    Dushek, O.2    Van Der Merwe, P.A.3
  • 15
    • 33646021951 scopus 로고    scopus 로고
    • Detection and localization of single molecular recognition events using atomic force microscopy
    • P. Hinterdorfer, and Y.F. Dufrêne Detection and localization of single molecular recognition events using atomic force microscopy Nat. Methods 3 2006 347 355
    • (2006) Nat. Methods , vol.3 , pp. 347-355
    • Hinterdorfer, P.1    Dufrêne, Y.F.2
  • 16
    • 0029883621 scopus 로고    scopus 로고
    • Detection and localization of individual antibody-antigen recognition events by atomic force microscopy
    • P. Hinterdorfer, and W. Baumgartner H. Schindler Detection and localization of individual antibody-antigen recognition events by atomic force microscopy Proc. Natl. Acad. Sci. USA 93 1996 3477 3481
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3477-3481
    • Hinterdorfer, P.1    Baumgartner, W.2    Schindler, H.3
  • 17
    • 33645004171 scopus 로고    scopus 로고
    • Intrinsic rates and activation free energies from single-molecule pulling experiments
    • O.K. Dudko, G. Hummer, and A. Szabo Intrinsic rates and activation free energies from single-molecule pulling experiments Phys. Rev. Lett. 96 2006 108101
    • (2006) Phys. Rev. Lett. , vol.96 , pp. 108101
    • Dudko, O.K.1    Hummer, G.2    Szabo, A.3
  • 18
    • 0348047600 scopus 로고    scopus 로고
    • Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation
    • M. Krogsgaard, and N. Prado M.M. Davis Evidence that structural rearrangements and/or flexibility during TCR binding can contribute to T cell activation Mol. Cell 12 2003 1367 1378
    • (2003) Mol. Cell , vol.12 , pp. 1367-1378
    • Krogsgaard, M.1    Prado, N.2    Davis, M.M.3
  • 19
    • 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 1940 284 304
    • (1940) Physica , vol.7 , pp. 284-304
    • Kramers, H.A.1
  • 20
    • 56649103827 scopus 로고    scopus 로고
    • Multiple receptors involved in human rhinovirus attachment to live cells
    • C. Rankl, and F. Kienberger P. Hinterdorfer Multiple receptors involved in human rhinovirus attachment to live cells Proc. Natl. Acad. Sci. USA 105 2008 17778 17783
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 17778-17783
    • Rankl, C.1    Kienberger, F.2    Hinterdorfer, P.3
  • 21
    • 0037743522 scopus 로고    scopus 로고
    • A molecular switch between alternative conformational states in the complex of Ran and importin β1
    • R. Nevo, and C. Stroh P. Hinterdorfer A molecular switch between alternative conformational states in the complex of Ran and importin β1 Nat. Struct. Biol. 10 2003 553 557
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 553-557
    • Nevo, R.1    Stroh, C.2    Hinterdorfer, P.3
  • 22
    • 79952781332 scopus 로고    scopus 로고
    • Molecular mechanistic insights into the endothelial receptor mediated cytoadherence of Plasmodium falciparum-infected erythrocytes
    • A. Li, and T.S. Lim C.T. Lim Molecular mechanistic insights into the endothelial receptor mediated cytoadherence of Plasmodium falciparum-infected erythrocytes PLoS ONE 6 2011 e16929
    • (2011) PLoS ONE , vol.6 , pp. 16929
    • Li, A.1    Lim, T.S.2    Lim, C.T.3
  • 23
    • 81955164077 scopus 로고    scopus 로고
    • T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex
    • J.J. Adams, and S. Narayanan K.C. Garcia T cell receptor signaling is limited by docking geometry to peptide-major histocompatibility complex Immunity 35 2011 681 693
    • (2011) Immunity , vol.35 , pp. 681-693
    • Adams, J.J.1    Narayanan, S.2    Garcia, K.C.3
  • 24
    • 77953473256 scopus 로고    scopus 로고
    • Cutting edge: Mechanical forces acting on T cells immobilized via the TCR complex can trigger TCR signaling
    • Y.C. Li, and B.M. Chen S.R. Roffler Cutting edge: mechanical forces acting on T cells immobilized via the TCR complex can trigger TCR signaling J. Immunol. 184 2010 5959 5963
    • (2010) J. Immunol. , vol.184 , pp. 5959-5963
    • Li, Y.C.1    Chen, B.M.2    Roffler, S.R.3
  • 25
    • 71449090489 scopus 로고    scopus 로고
    • The αβ T cell receptor is an anisotropic mechanosensor
    • S.T. Kim, and K. Takeuchi E.L. Reinherz The αβ T cell receptor is an anisotropic mechanosensor J. Biol. Chem. 284 2009 31028 31037
    • (2009) J. Biol. Chem. , vol.284 , pp. 31028-31037
    • Kim, S.T.1    Takeuchi, K.2    Reinherz, E.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.