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Volumn 133, Issue 3, 2011, Pages 271-277

Inside the microcluster: Antigen receptor signalling viewed with molecular imaging tools

Author keywords

Antigen; Imaging; Lymphocyte activation

Indexed keywords

ANTIGEN;

EID: 79957833444     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/j.1365-2567.2011.03452.x     Document Type: Review
Times cited : (3)

References (70)
  • 1
    • 0026750092 scopus 로고
    • Antigen receptors on B lymphocytes
    • Reth M. Antigen receptors on B lymphocytes. Annu Rev Immunol 1992; 10:97-121.
    • (1992) Annu Rev Immunol , vol.10 , pp. 97-121
    • Reth, M.1
  • 2
    • 17644395663 scopus 로고    scopus 로고
    • The T cell receptor: critical role of the membrane environment in receptor assembly and function
    • Call ME, Wucherpfennig KW. The T cell receptor: critical role of the membrane environment in receptor assembly and function. Annu Rev Immunol 2005; 23:101-25.
    • (2005) Annu Rev Immunol , vol.23 , pp. 101-125
    • Call, M.E.1    Wucherpfennig, K.W.2
  • 3
    • 78650599246 scopus 로고    scopus 로고
    • Mechanisms for T cell receptor triggering
    • van der Merwe PA, Dushek O. Mechanisms for T cell receptor triggering. Nat Rev Immunol 2011; 11:47-55.
    • (2011) Nat Rev Immunol , vol.11 , pp. 47-55
    • van der Merwe, P.A.1    Dushek, O.2
  • 4
    • 78049287668 scopus 로고    scopus 로고
    • The tipping points in the initiation of B cell signalling: how small changes make big differences
    • Pierce SK, Liu W. The tipping points in the initiation of B cell signalling: how small changes make big differences. Nat Rev Immunol 2010; 10:767-77.
    • (2010) Nat Rev Immunol , vol.10 , pp. 767-777
    • Pierce, S.K.1    Liu, W.2
  • 5
    • 78649863361 scopus 로고    scopus 로고
    • The dissociation activation model of B cell antigen receptor triggering
    • Yang J, Reth M. The dissociation activation model of B cell antigen receptor triggering. FEBS Lett 2010; 584:4872-7.
    • (2010) FEBS Lett , vol.584 , pp. 4872-4877
    • Yang, J.1    Reth, M.2
  • 6
    • 77956076669 scopus 로고    scopus 로고
    • Structural biology of the T-cell receptor: insights into receptor assembly, ligand recognition, and initiation of signaling
    • Wucherpfennig KW, Gagnon E, Call MJ, Huseby ES, Call ME. Structural biology of the T-cell receptor: insights into receptor assembly, ligand recognition, and initiation of signaling. Cold Spring Harb Perspect Biol 2010; 2:a005140.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Wucherpfennig, K.W.1    Gagnon, E.2    Call, M.J.3    Huseby, E.S.4    Call, M.E.5
  • 7
    • 78649812470 scopus 로고    scopus 로고
    • Signaling microdomains in T cells
    • Choudhuri K, Dustin ML. Signaling microdomains in T cells. FEBS Lett 2010; 584:4823-31.
    • (2010) FEBS Lett , vol.584 , pp. 4823-4831
    • Choudhuri, K.1    Dustin, M.L.2
  • 8
    • 0032480279 scopus 로고    scopus 로고
    • Three-dimensional segregation of supramolecular activation clusters in T cells
    • Monks C, Freiberg B, Kupfer H, Sciaky N, Kupfer A. Three-dimensional segregation of supramolecular activation clusters in T cells. Nature 1998; 395:82-6.
    • (1998) Nature , vol.395 , pp. 82-86
    • Monks, C.1    Freiberg, B.2    Kupfer, H.3    Sciaky, N.4    Kupfer, A.5
  • 10
    • 0035942781 scopus 로고    scopus 로고
    • B cells acquire antigen from target cells after synapse formation
    • Batista FD, Iber D, Neuberger MS. B cells acquire antigen from target cells after synapse formation. Nature 2001; 411:489-94.
    • (2001) Nature , vol.411 , pp. 489-494
    • Batista, F.D.1    Iber, D.2    Neuberger, M.S.3
  • 11
    • 0035655587 scopus 로고    scopus 로고
    • The immunological synapse of CTL contains a secretory domain and membrane bridges
    • Stinchcombe JC, Bossi G, Booth S, Griffiths GM. The immunological synapse of CTL contains a secretory domain and membrane bridges. Immunity 2001; 15:751-61.
    • (2001) Immunity , vol.15 , pp. 751-761
    • Stinchcombe, J.C.1    Bossi, G.2    Booth, S.3    Griffiths, G.M.4
  • 12
    • 64049108784 scopus 로고    scopus 로고
    • The cellular context of T cell signaling
    • Dustin ML. The cellular context of T cell signaling. Immunity 2009; 30:482-92.
    • (2009) Immunity , vol.30 , pp. 482-492
    • Dustin, M.L.1
  • 13
    • 77952310268 scopus 로고    scopus 로고
    • Functional anatomy of T cell activation and synapse formation
    • Fooksman DR, Vardhana S, Vasiliver-Shamis G et al. Functional anatomy of T cell activation and synapse formation. Annu Rev Immunol 2010; 28:79-105.
    • (2010) Annu Rev Immunol , vol.28 , pp. 79-105
    • Fooksman, D.R.1    Vardhana, S.2    Vasiliver-Shamis, G.3
  • 14
    • 33746011209 scopus 로고    scopus 로고
    • T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster
    • Varma R, Campi G, Yokosuka T, Saito T, Dustin ML. T cell receptor-proximal signals are sustained in peripheral microclusters and terminated in the central supramolecular activation cluster. Immunity 2006; 25:117-27.
    • (2006) Immunity , vol.25 , pp. 117-127
    • Varma, R.1    Campi, G.2    Yokosuka, T.3    Saito, T.4    Dustin, M.L.5
  • 17
    • 43049165459 scopus 로고    scopus 로고
    • New insights into the early molecular events underlying B cell activation
    • Harwood NE, Batista FD. New insights into the early molecular events underlying B cell activation. Immunity 2008; 28:609-19.
    • (2008) Immunity , vol.28 , pp. 609-619
    • Harwood, N.E.1    Batista, F.D.2
  • 18
    • 58149236663 scopus 로고    scopus 로고
    • Microscopy and its focal switch
    • Hell SW. Microscopy and its focal switch. Nat Methods 2009; 6:24-32.
    • (2009) Nat Methods , vol.6 , pp. 24-32
    • Hell, S.W.1
  • 20
    • 78650512639 scopus 로고    scopus 로고
    • Breaking the diffraction barrier: super-resolution imaging of cells
    • Huang B, Babcock H, Zhuang X. Breaking the diffraction barrier: super-resolution imaging of cells. Cell 2010; 143:1047-58.
    • (2010) Cell , vol.143 , pp. 1047-1058
    • Huang, B.1    Babcock, H.2    Zhuang, X.3
  • 21
    • 33747179417 scopus 로고    scopus 로고
    • Imaging intracellular fluorescent proteins at nanometer resolution
    • Betzig E, Patterson GH, Sougrat R et al. Imaging intracellular fluorescent proteins at nanometer resolution. Science 2006; 313:1642-5.
    • (2006) Science , vol.313 , pp. 1642-1645
    • Betzig, E.1    Patterson, G.H.2    Sougrat, R.3
  • 22
    • 33749026335 scopus 로고    scopus 로고
    • Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM)
    • Rust MJ, Bates M, Zhuang X. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat Methods 2006; 3:793-5.
    • (2006) Nat Methods , vol.3 , pp. 793-795
    • Rust, M.J.1    Bates, M.2    Zhuang, X.3
  • 23
    • 34547878369 scopus 로고    scopus 로고
    • New directions in single-molecule imaging and analysis
    • Moerner W. New directions in single-molecule imaging and analysis. Proc Natl Acad Sci USA 2007; 104:12596-602.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12596-12602
    • Moerner, W.1
  • 24
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo C, Balci H, Ishitsuka Y, Buranachai C, Ha T. Advances in single-molecule fluorescence methods for molecular biology. Annu Rev Biochem 2008; 77:51-76.
    • (2008) Annu Rev Biochem , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 25
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • Thompson RE, Larson DR, Webb WW. Precise nanometer localization analysis for individual fluorescent probes. Biophys J 2002; 82:2775-83.
    • (2002) Biophys J , vol.82 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 26
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • Douglass A, Vale RD. Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells. Cell 2005; 121:937-50.
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.1    Vale, R.D.2
  • 27
    • 38049136514 scopus 로고    scopus 로고
    • Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells
    • Kaizuka Y, Douglass AD, Varma R, Dustin ML, Vale RD. Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells. Proc Natl Acad Sci USA 2007; 104:20296-301.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 20296-20301
    • Kaizuka, Y.1    Douglass, A.D.2    Varma, R.3    Dustin, M.L.4    Vale, R.D.5
  • 29
    • 58149247765 scopus 로고    scopus 로고
    • The constant region of the membrane immunoglobulin mediates B cell-receptor clustering and signaling in response to membrane antigens
    • Tolar P, Hanna J, Krueger PD, Pierce SK. The constant region of the membrane immunoglobulin mediates B cell-receptor clustering and signaling in response to membrane antigens. Immunity 2009; 30:44-55.
    • (2009) Immunity , vol.30 , pp. 44-55
    • Tolar, P.1    Hanna, J.2    Krueger, P.D.3    Pierce, S.K.4
  • 30
    • 48249124978 scopus 로고    scopus 로고
    • Membrane heterogeneities in the formation of B cell receptor-Lyn kinase microclusters and the immune synapse
    • Sohn HW, Tolar P, Pierce SK. Membrane heterogeneities in the formation of B cell receptor-Lyn kinase microclusters and the immune synapse. J Cell Biol 2008; 182:367-79.
    • (2008) J Cell Biol , vol.182 , pp. 367-379
    • Sohn, H.W.1    Tolar, P.2    Pierce, S.K.3
  • 31
    • 77950426522 scopus 로고    scopus 로고
    • Evidence for a functional sidedness to the αβTCR
    • Kuhns MS, Girvin AT, Klein LO et al. Evidence for a functional sidedness to the αβTCR. Proc Natl Acad Sci USA 2010; 107:5094-9.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5094-5099
    • Kuhns, M.S.1    Girvin, A.T.2    Klein, L.O.3
  • 32
    • 77950910326 scopus 로고    scopus 로고
    • A conformation-induced oligomerization model for B cell receptor microclustering and signaling
    • Tolar P, Pierce SK. A conformation-induced oligomerization model for B cell receptor microclustering and signaling. Curr Top Microbiol Immunol 2010; 340:155-69.
    • (2010) Curr Top Microbiol Immunol , vol.340 , pp. 155-169
    • Tolar, P.1    Pierce, S.K.2
  • 35
    • 0035817631 scopus 로고    scopus 로고
    • High resolution mapping of mast cell membranes reveals primary and secondary domains of FcεRI and LAT
    • Wilson BS, Pfeiffer JR, Surviladze Z, Gaudet EA, Oliver JM. High resolution mapping of mast cell membranes reveals primary and secondary domains of FcεRI and LAT. J Cell Biol 2001; 154:645.
    • (2001) J Cell Biol , vol.154 , pp. 645
    • Wilson, B.S.1    Pfeiffer, J.R.2    Surviladze, Z.3    Gaudet, E.A.4    Oliver, J.M.5
  • 36
    • 0033697266 scopus 로고    scopus 로고
    • Monomeric and oligomeric complexes of the B cell antigen receptor
    • Schamel WWA, Reth M. Monomeric and oligomeric complexes of the B cell antigen receptor. Immunity 2000; 13:5-14.
    • (2000) Immunity , vol.13 , pp. 5-14
    • Schamel, W.W.A.1    Reth, M.2
  • 37
    • 77957125242 scopus 로고    scopus 로고
    • Oligomeric organization of the B-cell antigen receptor on resting cells
    • Yang J, Reth M. Oligomeric organization of the B-cell antigen receptor on resting cells. Nature 2010; 467:465-9.
    • (2010) Nature , vol.467 , pp. 465-469
    • Yang, J.1    Reth, M.2
  • 38
    • 0037188899 scopus 로고    scopus 로고
    • Recruitment of Nck by CD3ε reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation
    • Gil D, Schamel WWA, Montoya M, Sanchez-Madrid F, Alarcon B. Recruitment of Nck by CD3ε reveals a ligand-induced conformational change essential for T cell receptor signaling and synapse formation. Cell 2002; 109:901-12.
    • (2002) Cell , vol.109 , pp. 901-912
    • Gil, D.1    Schamel, W.W.A.2    Montoya, M.3    Sanchez-Madrid, F.4    Alarcon, B.5
  • 39
    • 55449138409 scopus 로고    scopus 로고
    • Regulation of T cell receptor activation by dynamic membrane binding of the CD3ε cytoplasmic tyrosine-based motif
    • Xu C, Gagnon E, Call M, Schnell J, Schwieters C, Carman C, Chou J, Wucherpfennig KW. Regulation of T cell receptor activation by dynamic membrane binding of the CD3ε cytoplasmic tyrosine-based motif. Cell 2008; 135:702-13.
    • (2008) Cell , vol.135 , pp. 702-713
    • Xu, C.1    Gagnon, E.2    Call, M.3    Schnell, J.4    Schwieters, C.5    Carman, C.6    Chou, J.7    Wucherpfennig, K.W.8
  • 40
    • 0033762433 scopus 로고    scopus 로고
    • Phosphorylation of T cell receptor ζ is regulated by a lipid dependent folding transition
    • Aivazian D, Stern LJ. Phosphorylation of T cell receptor ζ is regulated by a lipid dependent folding transition. Nat Struct Biol 2000; 7:1023-6.
    • (2000) Nat Struct Biol , vol.7 , pp. 1023-1026
    • Aivazian, D.1    Stern, L.J.2
  • 41
    • 27544446258 scopus 로고    scopus 로고
    • The initiation of antigen-induced B cell antigen receptor signaling viewed in living cells by fluorescence resonance energy transfer
    • Tolar P, Sohn HW, Pierce SK. The initiation of antigen-induced B cell antigen receptor signaling viewed in living cells by fluorescence resonance energy transfer. Nat Immunol 2005; 6:1168-76.
    • (2005) Nat Immunol , vol.6 , pp. 1168-1176
    • Tolar, P.1    Sohn, H.W.2    Pierce, S.K.3
  • 42
    • 67349283033 scopus 로고    scopus 로고
    • Antigen ligation triggers a conformational change within the constant domain of the αβ T cell receptor
    • Beddoe T, Chen Z, Clements C et al. Antigen ligation triggers a conformational change within the constant domain of the αβ T cell receptor. Immunity 2009; 30:777-88.
    • (2009) Immunity , vol.30 , pp. 777-788
    • Beddoe, T.1    Chen, Z.2    Clements, C.3
  • 43
    • 33947173844 scopus 로고    scopus 로고
    • Disruption of extracellular interactions impairs T cell receptor-CD3 complex stability and signaling
    • Kuhns MS, Davis MM. Disruption of extracellular interactions impairs T cell receptor-CD3 complex stability and signaling. Immunity 2007; 26:357-69.
    • (2007) Immunity , vol.26 , pp. 357-369
    • Kuhns, M.S.1    Davis, M.M.2
  • 45
    • 72949124550 scopus 로고    scopus 로고
    • A conserved CXXC motif in CD3ε is critical for T cell development and TCR signaling
    • Wang Y, Becker D, Vass T, White J, Marrack P, Kappler JW. A conserved CXXC motif in CD3ε is critical for T cell development and TCR signaling. PLoS Biol 2009; 7:e1000253.
    • (2009) PLoS Biol , vol.7
    • Wang, Y.1    Becker, D.2    Vass, T.3    White, J.4    Marrack, P.5    Kappler, J.W.6
  • 47
    • 33746545207 scopus 로고    scopus 로고
    • B cell recognition of membrane-bound antigen: an exquisite way of sensing ligands
    • Carrasco Y, Batista FD. B cell recognition of membrane-bound antigen: an exquisite way of sensing ligands. Curr Opin Immunol 2006; 18:286-91.
    • (2006) Curr Opin Immunol , vol.18 , pp. 286-291
    • Carrasco, Y.1    Batista, F.D.2
  • 49
    • 0033711639 scopus 로고    scopus 로고
    • Conversion of a T cell antagonist into an agonist by repairing a defect in the TCR/peptide/MHC interface: implications for TCR signaling
    • Baker BM, Gagnon SJ, Biddison WE, Wiley DC. Conversion of a T cell antagonist into an agonist by repairing a defect in the TCR/peptide/MHC interface: implications for TCR signaling. Immunity 2000; 13:475-84.
    • (2000) Immunity , vol.13 , pp. 475-484
    • Baker, B.M.1    Gagnon, S.J.2    Biddison, W.E.3    Wiley, D.C.4
  • 52
    • 0032438551 scopus 로고    scopus 로고
    • High- and low-potency ligands with similar affinities for the TCR: the importance of kinetics in TCR signaling
    • Kersh GJ, Kersh EN, Fremont DH, Allen PM. High- and low-potency ligands with similar affinities for the TCR: the importance of kinetics in TCR signaling. Immunity 1998; 9:817-26.
    • (1998) Immunity , vol.9 , pp. 817-826
    • Kersh, G.J.1    Kersh, E.N.2    Fremont, D.H.3    Allen, P.M.4
  • 53
    • 33645239805 scopus 로고    scopus 로고
    • Molecular flexibility can influence the stimulatory ability of receptor-ligand interactions at cell-cell junctions
    • Qi S, Krogsgaard M, Davis MM, Chakraborty AK. Molecular flexibility can influence the stimulatory ability of receptor-ligand interactions at cell-cell junctions. Proc Natl Acad Sci USA 2006; 103:4416-21.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4416-4421
    • Qi, S.1    Krogsgaard, M.2    Davis, M.M.3    Chakraborty, A.K.4
  • 54
    • 0034651890 scopus 로고    scopus 로고
    • B cells extract and present immobilized antigen: implications for affinity discrimination
    • Batista FD, Neuberger MS. B cells extract and present immobilized antigen: implications for affinity discrimination. EMBO J 2000; 19:513-20.
    • (2000) EMBO J , vol.19 , pp. 513-520
    • Batista, F.D.1    Neuberger, M.S.2
  • 55
    • 0032100706 scopus 로고    scopus 로고
    • Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate
    • Batista FD, Neuberger MS. Affinity dependence of the B cell response to antigen: a threshold, a ceiling, and the importance of off-rate. Immunity 1998; 8:751-9.
    • (1998) Immunity , vol.8 , pp. 751-759
    • Batista, F.D.1    Neuberger, M.S.2
  • 56
    • 77950809538 scopus 로고    scopus 로고
    • The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness
    • Huang J, Zarnitsyna VI, Liu B, Edwards LJ, Jiang N, Evavold BD, Zhu C. The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness. Nature 2010; 464:932-6.
    • (2010) Nature , vol.464 , pp. 932-936
    • Huang, J.1    Zarnitsyna, V.I.2    Liu, B.3    Edwards, L.J.4    Jiang, N.5    Evavold, B.D.6    Zhu, C.7
  • 57
    • 77249114784 scopus 로고    scopus 로고
    • TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity
    • Huppa JB, Axmann M, Mörtelmaier MA et al. TCR-peptide-MHC interactions in situ show accelerated kinetics and increased affinity. Nature 2010; 463:963-7.
    • (2010) Nature , vol.463 , pp. 963-967
    • Huppa, J.B.1    Axmann, M.2    Mörtelmaier, M.A.3
  • 58
    • 77952314719 scopus 로고    scopus 로고
    • Antigen affinity discrimination is an intrinsic function of the B cell receptor
    • Liu W, Meckel T, Tolar P, Sohn HW, Pierce SK. Antigen affinity discrimination is an intrinsic function of the B cell receptor. J Exp Med 2010; 207:1095-111.
    • (2010) J Exp Med , vol.207 , pp. 1095-1111
    • Liu, W.1    Meckel, T.2    Tolar, P.3    Sohn, H.W.4    Pierce, S.K.5
  • 60
    • 67349114397 scopus 로고    scopus 로고
    • T cell antigen receptor signaling and immunological synapse stability require myosin IIA
    • Ilani T, Vasiliver-Shamis G, Vardhana S, Bretscher A, Dustin ML. T cell antigen receptor signaling and immunological synapse stability require myosin IIA. Nat Immunol 2009; 10:531-9.
    • (2009) Nat Immunol , vol.10 , pp. 531-539
    • Ilani, T.1    Vasiliver-Shamis, G.2    Vardhana, S.3    Bretscher, A.4    Dustin, M.L.5
  • 61
    • 38949216802 scopus 로고    scopus 로고
    • Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy
    • Huang B, Wang W, Bates M, Zhuang X. Three-dimensional super-resolution imaging by stochastic optical reconstruction microscopy. Science 2008; 319:810-3.
    • (2008) Science , vol.319 , pp. 810-813
    • Huang, B.1    Wang, W.2    Bates, M.3    Zhuang, X.4
  • 62
    • 34648826792 scopus 로고    scopus 로고
    • Multicolor super-resolution imaging with photo-switchable fluorescent probes
    • Bates M, Huang B, Dempsey GT, Zhuang X. Multicolor super-resolution imaging with photo-switchable fluorescent probes. Science 2007; 317:1749-53.
    • (2007) Science , vol.317 , pp. 1749-1753
    • Bates, M.1    Huang, B.2    Dempsey, G.T.3    Zhuang, X.4
  • 63
    • 62549155396 scopus 로고    scopus 로고
    • Interferometric fluorescent super-resolution microscopy resolves 3D cellular ultrastructure
    • Shtengel G, Galbraith JA, Galbraith CG et al. Interferometric fluorescent super-resolution microscopy resolves 3D cellular ultrastructure. Proc Natl Acad Sci USA 2009; 106:3125-30.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3125-3130
    • Shtengel, G.1    Galbraith, J.A.2    Galbraith, C.G.3
  • 65
    • 77955175217 scopus 로고    scopus 로고
    • Subnanometre single-molecule localization, registration and distance measurements
    • Pertsinidis A, Zhang Y, Chu S. Subnanometre single-molecule localization, registration and distance measurements. Nature 2010; 466:647-51.
    • (2010) Nature , vol.466 , pp. 647-651
    • Pertsinidis, A.1    Zhang, Y.2    Chu, S.3
  • 66
    • 27644514163 scopus 로고    scopus 로고
    • Repetitive shuttling of a motor protein on DNA
    • Myong S, Rasnik I, Joo C, Lohman TM, Ha T. Repetitive shuttling of a motor protein on DNA. Nature 2005; 437:1321-5.
    • (2005) Nature , vol.437 , pp. 1321-1325
    • Myong, S.1    Rasnik, I.2    Joo, C.3    Lohman, T.M.4    Ha, T.5
  • 67
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization
    • Yildiz A, Forkey JN, McKinney SA, Ha T, Goldman YE, Selvin PR. Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 2003; 300:2061-5.
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6
  • 70
    • 48749103296 scopus 로고    scopus 로고
    • Integrating diverse data for structure determination of macromolecular assemblies
    • Alber F, Förster F, Korkin D, Topf M, Sali A. Integrating diverse data for structure determination of macromolecular assemblies. Annu Rev Biochem 2008; 77:443-77.
    • (2008) Annu Rev Biochem , vol.77 , pp. 443-477
    • Alber, F.1    Förster, F.2    Korkin, D.3    Topf, M.4    Sali, A.5


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