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Volumn 9, Issue 3, 1997, Pages 390-395

Interactions of TCRs with MHC-peptide complexes: A quantitative basis for mechanistic models

Author keywords

[No Author keywords available]

Indexed keywords

MAJOR HISTOCOMPATIBILITY ANTIGEN; T LYMPHOCYTE RECEPTOR;

EID: 0030738184     PISSN: 09527915     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0952-7915(97)80086-6     Document Type: Article
Times cited : (55)

References (56)
  • 1
    • 0027468145 scopus 로고
    • The biochemistry and cell biology of antigen processing and presentation
    • Germain RN, Margulies DH. The biochemistry and cell biology of antigen processing and presentation. Annu Rev Immunol. 11:1993;403-450.
    • (1993) Annu Rev Immunol , vol.11 , pp. 403-450
    • Germain, R.N.1    Margulies, D.H.2
  • 2
    • 0028038426 scopus 로고
    • MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
    • Germain RN. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell. 76:1994;287-299.
    • (1994) Cell , vol.76 , pp. 287-299
    • Germain, R.N.1
  • 3
    • 0028943275 scopus 로고
    • The three-dimensional structure of peptide-MHC complexes
    • Madden DR. The three-dimensional structure of peptide-MHC complexes. Annu Rev Immunol. 13:1995;545-586.
    • (1995) Annu Rev Immunol , vol.13 , pp. 545-586
    • Madden, D.R.1
  • 5
    • 0028956603 scopus 로고
    • Crystal structure of the beta chain of a T cell antigen receptor
    • of outstanding interest. The first high resolution crystallographic structure of a TCR fragment.
    • Bentley GA, Boulot G, Karjalainen K, Mariuzza RA. Crystal structure of the beta chain of a T cell antigen receptor. of outstanding interest Science. 267:1995;1984-1987 The first high resolution crystallographic structure of a TCR fragment.
    • (1995) Science , vol.267 , pp. 1984-1987
    • Bentley, G.A.1    Boulot, G.2    Karjalainen, K.3    Mariuzza, R.A.4
  • 6
    • 0029985104 scopus 로고    scopus 로고
    • Crystal structure of a T-cell receptor beta chain complexed with a superantigen
    • of special interest. The structure of a TCR-superantigen complex reveals how superantigens can have TCR Vβ specificity.
    • Fields BA, Malchiodi EL, Li H, Ysern X, Stauffacher CV, Schlievert PM, Karjalainen K, Mariuzza RA. Crystal structure of a T-cell receptor beta chain complexed with a superantigen. of special interest Nature. 384:1996;188-192 The structure of a TCR-superantigen complex reveals how superantigens can have TCR Vβ specificity.
    • (1996) Nature , vol.384 , pp. 188-192
    • Fields, B.A.1    Malchiodi, E.L.2    Li, H.3    Ysern, X.4    Stauffacher, C.V.5    Schlievert, P.M.6    Karjalainen, K.7    Mariuzza, R.A.8
  • 7
    • 0029662223 scopus 로고    scopus 로고
    • An alpha/beta T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex
    • of outstanding interest. The first X-ray structure of a complete TCR combining site and the first reported structure of a TCR-MHC-peptide complex.
    • Garcia KC, Degano M, Stanfield RL, Brunmark A, Jackson MR, Peterson PA, Teyton L, Wilson IA. An alpha/beta T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex. of outstanding interest Science. 274:1996;209-219 The first X-ray structure of a complete TCR combining site and the first reported structure of a TCR-MHC-peptide complex.
    • (1996) Science , vol.274 , pp. 209-219
    • Garcia, K.C.1    Degano, M.2    Stanfield, R.L.3    Brunmark, A.4    Jackson, M.R.5    Peterson, P.A.6    Teyton, L.7    Wilson, I.A.8
  • 8
    • 0029855347 scopus 로고    scopus 로고
    • Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
    • of outstanding interest. Describes the high resolution X-ray structure of a TCR-MHC-peptide complex with good visualization of the interface between the three components
    • Garboczi DN, Ghosh P, Utz U, Fan QR, Biddison WE, Wiley DC. Structure of the complex between human T-cell receptor, viral peptide and HLA-A2. of outstanding interest Nature. 384:1996;134-141 Describes the high resolution X-ray structure of a TCR-MHC-peptide complex with good visualization of the interface between the three components.
    • (1996) Nature , vol.384 , pp. 134-141
    • Garboczi, D.N.1    Ghosh, P.2    Utz, U.3    Fan, Q.R.4    Biddison, W.E.5    Wiley, D.C.6
  • 9
    • 0031020557 scopus 로고    scopus 로고
    • Immunology: Feeling out the receptor
    • Padlan EA, Margulies DH. Immunology: feeling out the receptor. Curr Biol. 7:1997;R17-R20.
    • (1997) Curr Biol , vol.7
    • Padlan, E.A.1    Margulies, D.H.2
  • 13
    • 0011298312 scopus 로고
    • The kinetics of binding of peptide/MHC complexes to T-cell receptors: Application of surface plasmon resonance to a low-affinity measurement
    • Boniface JJ, Davis MM. The kinetics of binding of peptide/MHC complexes to T-cell receptors: application of surface plasmon resonance to a low-affinity measurement. Methods: A Companion to Methods Enzymol. 6:1994;168-175.
    • (1994) Methods: A Companion to Methods Enzymol , vol.6 , pp. 168-175
    • Boniface, J.J.1    Davis, M.M.2
  • 14
    • 0029013301 scopus 로고
    • Lack of strict correlation of functional sensitization with the apparent affinity of MHC-peptide complexes for the TCR
    • of special interest. A survey of variant peptides for function in T cell activation and binding to the cognate TCR as MHC-peptide complexes. Describes a single anomalous peptide which forms an MHC-peptide complex that stimulates T cells but does not bind detectably to the TCR
    • Al-Ramadi BK, Jelonek MT, Boyd LF, Margulies DH, Bothwell ALM. Lack of strict correlation of functional sensitization with the apparent affinity of MHC-peptide complexes for the TCR. of special interest J Immunol. 155:1995;662-673 A survey of variant peptides for function in T cell activation and binding to the cognate TCR as MHC-peptide complexes. Describes a single anomalous peptide which forms an MHC-peptide complex that stimulates T cells but does not bind detectably to the TCR.
    • (1995) J Immunol , vol.155 , pp. 662-673
    • Al-Ramadi, B.K.1    Jelonek, M.T.2    Boyd, L.F.3    Margulies, D.H.4    Bothwell, A.L.M.5
  • 15
    • 0030022868 scopus 로고    scopus 로고
    • Studying interactions involving the T cell antigen receptor by surface plasmon resonance
    • of special interest. A review of the use of SPR, which allows the sensitive kinetic measurement of binding reactions, as applied to TCR-MHC-peptide interactions.
    • Margulies DH, Plaksin D, Khilko SN, Jelonek MT. Studying interactions involving the T cell antigen receptor by surface plasmon resonance. of special interest Curr Opin Immunol. 8:1996;262-270 A review of the use of SPR, which allows the sensitive kinetic measurement of binding reactions, as applied to TCR-MHC-peptide interactions.
    • (1996) Curr Opin Immunol , vol.8 , pp. 262-270
    • Margulies, D.H.1    Plaksin, D.2    Khilko, S.N.3    Jelonek, M.T.4
  • 16
    • 0031091745 scopus 로고    scopus 로고
    • A three domain TCR is biologically active and specifically stains cell surface MHC-peptide complexes
    • d - P18-110 complex. The paper includes a survey of 26 variant peptides for TCR activation and binding as well as the demonstration of specific staining of cell surface MHC-peptide complexes with the biotinylated TCR
    • d - P18-110 complex. The paper includes a survey of 26 variant peptides for TCR activation and binding as well as the demonstration of specific staining of cell surface MHC-peptide complexes with the biotinylated TCR.
    • (1997) J Immunol , vol.158 , pp. 2218-2227
    • Plaksin, D.1    Polakova, K.2    McPhie, P.3    Margulies, D.H.4
  • 17
    • 0026434554 scopus 로고
    • Separation of IL-4 production from Th cell proliferation by an altered TCR ligand
    • Evavold BD, Allen PM. Separation of IL-4 production from Th cell proliferation by an altered TCR ligand. Science. 252:1991;1308-1310.
    • (1991) Science , vol.252 , pp. 1308-1310
    • Evavold, B.D.1    Allen, P.M.2
  • 19
    • 0025721116 scopus 로고
    • The molecular basis of class II MHC allelic control of T cell responses
    • Racioppi L, Ronchese F, Schwartz RH, Germain RN. The molecular basis of class II MHC allelic control of T cell responses. J Immunol. 147:1991;3718-3727.
    • (1991) J Immunol , vol.147 , pp. 3718-3727
    • Racioppi, L.1    Ronchese, F.2    Schwartz, R.H.3    Germain, R.N.4
  • 20
    • 0028801774 scopus 로고
    • The T-cell receptor as a diverse signal transduction machine
    • Germain RN, Levine EH, Madrenas J. The T-cell receptor as a diverse signal transduction machine. Res Trends. 3:(4):1995;113-121.
    • (1995) Res Trends , vol.3 , Issue.4 , pp. 113-121
    • Germain, R.N.1    Levine, E.H.2    Madrenas, J.3
  • 21
    • 0003104975 scopus 로고    scopus 로고
    • A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists
    • of outstanding interest. An evaluation of antagonist MHC-peptide binding to the TCR using SPR. Describes several examples of peptides that, in complex with MHC molecules, have a low stability in TCR binding which correlates with their antagonist function.
    • Lyons DS, Lieberman SA, Hampl J, Boniface JJ, Chien Y-H, Berg LJ, Davis MM. A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists. of outstanding interest Immunity. 5:1996;53-61 An evaluation of antagonist MHC-peptide binding to the TCR using SPR. Describes several examples of peptides that, in complex with MHC molecules, have a low stability in TCR binding which correlates with their antagonist function.
    • (1996) Immunity , vol.5 , pp. 53-61
    • Lyons, D.S.1    Lieberman, S.A.2    Hampl, J.3    Boniface, J.J.4    Chien, Y.-H.5    Berg, L.J.6    Davis, M.M.7
  • 22
    • 0030014002 scopus 로고    scopus 로고
    • TCR affinity and thymocyte positive selection
    • of outstanding interest. Demonstrates that peptides which form peptide - MHC complexes with a low affinity for the cognate TCR tend to be those peptides that act to positively select T cells.
    • Alam SM, Travers PJ, Wung JL, Nasholds W, Redpath S, Jameson SC, Gascoigne NRJ. TCR affinity and thymocyte positive selection. of outstanding interest Nature. 381:1996;616-620 Demonstrates that peptides which form peptide - MHC complexes with a low affinity for the cognate TCR tend to be those peptides that act to positively select T cells.
    • (1996) Nature , vol.381 , pp. 616-620
    • Alam, S.M.1    Travers, P.J.2    Wung, J.L.3    Nasholds, W.4    Redpath, S.5    Jameson, S.C.6    Gascoigne, N.R.J.7
  • 23
    • 0028797801 scopus 로고
    • CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes
    • of special interest. Evaluation of TCR - MHC - peptide interactions using photoactivatable cross-linking. The experiments show a time-dependent effect of CD8 engagement, indicating the dynamic aspects of avidity during the early steps of T cell activation.
    • Luescher IF, Vivier E, Layer A, Mahiou J, Godeau F, Malissen B, Romero P. CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes. of special interest Nature. 373:1995;353-356 Evaluation of TCR - MHC - peptide interactions using photoactivatable cross-linking. The experiments show a time-dependent effect of CD8 engagement, indicating the dynamic aspects of avidity during the early steps of T cell activation.
    • (1995) Nature , vol.373 , pp. 353-356
    • Luescher, I.F.1    Vivier, E.2    Layer, A.3    Mahiou, J.4    Godeau, F.5    Malissen, B.6    Romero, P.7
  • 24
    • 0029807351 scopus 로고    scopus 로고
    • CD8 enhances formation of stable T-cell receptor/MHC class I molecule complexes
    • of outstanding interest. Direct binding of CD8 to MHC-I and the augmentation of the MHC - TCR interaction in the presence of CD8 are demonstrated
    • Garcia KC, Scott CA, Brunmark A, Carbone FR, Peterson PA, Wilson IA, Teyton L. CD8 enhances formation of stable T-cell receptor/MHC class I molecule complexes. of outstanding interest Nature. 384:1996;577-581 Direct binding of CD8 to MHC-I and the augmentation of the MHC - TCR interaction in the presence of CD8 are demonstrated.
    • (1996) Nature , vol.384 , pp. 577-581
    • Garcia, K.C.1    Scott, C.A.2    Brunmark, A.3    Carbone, F.R.4    Peterson, P.A.5    Wilson, I.A.6    Teyton, L.7
  • 25
    • 0030008145 scopus 로고    scopus 로고
    • Variant TCR ligands: New insights into the molecular basis of antigen-dependent signal transduction and T-cell activation
    • Madrenas J, Germain RN. Variant TCR ligands: new insights into the molecular basis of antigen-dependent signal transduction and T-cell activation. Semin Immunol. 8:1996;83-101.
    • (1996) Semin Immunol , vol.8 , pp. 83-101
    • Madrenas, J.1    Germain, R.N.2
  • 26
    • 0027967385 scopus 로고
    • Partial T cell signaling: Altered phospho-zeta and lack of zap70 recruitment in APL-induced T cell energy
    • Sloan-Lancaster J, Shaw AS, Rothbard JB, Allen PM. Partial T cell signaling: altered phospho-zeta and lack of zap70 recruitment in APL-induced T cell energy. Cell. 79:1994;913-922.
    • (1994) Cell , vol.79 , pp. 913-922
    • Sloan-Lancaster, J.1    Shaw, A.S.2    Rothbard, J.B.3    Allen, P.M.4
  • 27
    • 0028902752 scopus 로고
    • Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists
    • of outstanding interest. Clear demonstration of distinct phosphorylation patterns due to agonist as compared to antagonist or partial agonist MHC - peptide ligands.
    • Madrenas J, Wange RL, Wang JL, Isakov N, Samelson LE, Germain RN. Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists. of outstanding interest Science. 267:1995;515-518 Clear demonstration of distinct phosphorylation patterns due to agonist as compared to antagonist or partial agonist MHC - peptide ligands.
    • (1995) Science , vol.267 , pp. 515-518
    • Madrenas, J.1    Wange, R.L.2    Wang, J.L.3    Isakov, N.4    Samelson, L.E.5    Germain, R.N.6
  • 29
    • 0029037210 scopus 로고
    • Serial triggering of many T-cell receptors by a few peptide-MHC complexes
    • of special interest. Measurement of TCR downregulation as a result of stimulation with a low density of MHC - peptide ligand leads to a serial engagement model in which individual MHC - peptide complexes are suggested to bind, trigger and release numerous TCRs.
    • Valitutti S, Muller S, Cella M, Padovan E, Lanzavecchia A. Serial triggering of many T-cell receptors by a few peptide-MHC complexes. of special interest Nature. 375:1995;148-151 Measurement of TCR downregulation as a result of stimulation with a low density of MHC - peptide ligand leads to a serial engagement model in which individual MHC - peptide complexes are suggested to bind, trigger and release numerous TCRs.
    • (1995) Nature , vol.375 , pp. 148-151
    • Valitutti, S.1    Muller, S.2    Cella, M.3    Padovan, E.4    Lanzavecchia, A.5
  • 30
    • 0029063148 scopus 로고
    • Kinetic proofreading in T-cell receptor signal transduction
    • of outstanding interest. Elaboration of the kinetic proofreading model as applied to TCR signaling.
    • McKeithan TW. Kinetic proofreading in T-cell receptor signal transduction. of outstanding interest Proc Natl Acad Sci USA. 92:1995;5042-5046 Elaboration of the kinetic proofreading model as applied to TCR signaling.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5042-5046
    • McKeithan, T.W.1
  • 31
    • 0029855923 scopus 로고    scopus 로고
    • Tuning of activation thresholds explains flexibility in the selection and development of T cells in the thymus
    • of special interest. Refinement of the tuning of activation threshold model and its application to thymic selection and development.
    • Grossman Z, Singer A. Tuning of activation thresholds explains flexibility in the selection and development of T cells in the thymus. of special interest Proc Natl Acad Sci USA. 93:1996;14747-14752 Refinement of the tuning of activation threshold model and its application to thymic selection and development.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14747-14752
    • Grossman, Z.1    Singer, A.2
  • 32
    • 0029926145 scopus 로고    scopus 로고
    • Kinetic discrimination in T-cell activation
    • of special interest. A refined kinetic proofreading model to account for inhibitory signals.
    • Rabinowitz JD, Beeson C, Lyons DS, Davis MM, McConnell HM. Kinetic discrimination in T-cell activation. of special interest Proc Natl Acad Sci USA. 93:1996;1401-1405 A refined kinetic proofreading model to account for inhibitory signals.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1401-1405
    • Rabinowitz, J.D.1    Beeson, C.2    Lyons, D.S.3    Davis, M.M.4    McConnell, H.M.5
  • 34
    • 0025233576 scopus 로고
    • Genetic and mutational analysis of the T-cell antigen receptor
    • Ashwell JD, Klusner RD. Genetic and mutational analysis of the T-cell antigen receptor. Annu Rev Immunol. 8:1990;139-167.
    • (1990) Annu Rev Immunol , vol.8 , pp. 139-167
    • Ashwell, J.D.1    Klusner, R.D.2
  • 35
    • 0028288927 scopus 로고
    • The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction
    • Chan AC, Desai DM, Weiss A. The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu Rev Immunol. 12:1994;555-592.
    • (1994) Annu Rev Immunol , vol.12 , pp. 555-592
    • Chan, A.C.1    Desai, D.M.2    Weiss, A.3
  • 36
    • 0029565761 scopus 로고
    • Hierarchy of T cell antigen receptor assembly
    • Manolios N. Hierarchy of T cell antigen receptor assembly. Immunol Cell Biol. 73:1995;544-548.
    • (1995) Immunol Cell Biol , vol.73 , pp. 544-548
    • Manolios, N.1
  • 37
    • 0027977974 scopus 로고
    • Transient intercellular adhesion: The importance of weak protein-protein interactions
    • Van der Merwe PA, Barclay AN. Transient intercellular adhesion: the importance of weak protein-protein interactions. Trends Biochem Sci. 19:1994;354-358.
    • (1994) Trends Biochem Sci , vol.19 , pp. 354-358
    • Van Der Merwe, P.A.1    Barclay, A.N.2
  • 38
    • 0030061494 scopus 로고    scopus 로고
    • Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area
    • of outstanding interest. Use of fluorescence microscopy to visualize and quantitate accessory molecule interactions at the cell - cell interface.
    • Dustin ML, Ferguson LM, Chan PY, Springer TA, Golan DE. Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area. of outstanding interest J Cell Biol. 132:1996;465-474 Use of fluorescence microscopy to visualize and quantitate accessory molecule interactions at the cell - cell interface.
    • (1996) J Cell Biol , vol.132 , pp. 465-474
    • Dustin, M.L.1    Ferguson, L.M.2    Chan, P.Y.3    Springer, T.A.4    Golan, D.E.5
  • 39
    • 0030292822 scopus 로고    scopus 로고
    • A motif within the TCR alpha chain constant region connecting peptide domain controls antigen responsiveness
    • of special interest. Identification of a region in the TCR α chain constant domain that is critically involved in signal transduction.
    • Backstrom BT, Milia E, Peter A, Jaureguiberry B, Baldari CT, Palmer E. A motif within the TCR alpha chain constant region connecting peptide domain controls antigen responsiveness. of special interest Immunity. 5:1996;437-447 Identification of a region in the TCR α chain constant domain that is critically involved in signal transduction.
    • (1996) Immunity , vol.5 , pp. 437-447
    • Backstrom, B.T.1    Milia, E.2    Peter, A.3    Jaureguiberry, B.4    Baldari, C.T.5    Palmer, E.6
  • 40
    • 0028027340 scopus 로고
    • The T-cell antigen receptor: A multisubunit signaling complex
    • Weissman AM. The T-cell antigen receptor: a multisubunit signaling complex. Chem Immunol. 59:1994;1-18.
    • (1994) Chem Immunol , vol.59 , pp. 1-18
    • Weissman, A.M.1
  • 41
    • 0029883778 scopus 로고    scopus 로고
    • Biophysical studies of T-cell receptors and their ligands
    • Fremont DH, Rees WA, Kozono H. Biophysical studies of T-cell receptors and their ligands. Curr Opin Immunol. 8:1996;93-100.
    • (1996) Curr Opin Immunol , vol.8 , pp. 93-100
    • Fremont, D.H.1    Rees, W.A.2    Kozono, H.3
  • 42
    • 0028410566 scopus 로고
    • Kinetics and affinity of reactions between an antigen-specific TCR and peptide-MHC complexes
    • Sykulev Y, Brunmark A, Jackson M, Cohen RJ, Peterson PA, Eisen HN. Kinetics and affinity of reactions between an antigen-specific TCR and peptide-MHC complexes. Immunity. 1:1994;15-22.
    • (1994) Immunity , vol.1 , pp. 15-22
    • Sykulev, Y.1    Brunmark, A.2    Jackson, M.3    Cohen, R.J.4    Peterson, P.A.5    Eisen, H.N.6
  • 44
    • 0030070499 scopus 로고    scopus 로고
    • Kinetics of ligand binding to receptor immobilized in a polymer matrix, as detected with an evanescent wave biosensor .1. A computer simulation of the influence of mass transport
    • Schuck P. Kinetics of ligand binding to receptor immobilized in a polymer matrix, as detected with an evanescent wave biosensor .1. A computer simulation of the influence of mass transport. Biophys J. 70:1996;1230-1249.
    • (1996) Biophys J , vol.70 , pp. 1230-1249
    • Schuck, P.1
  • 47
    • 0026675654 scopus 로고
    • Transmembrane signaling: The joy of aggregation
    • Metzger H. Transmembrane signaling: the joy of aggregation. J Immunol. 149:1992;1477-1487.
    • (1992) J Immunol , vol.149 , pp. 1477-1487
    • Metzger, H.1
  • 48
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells JA. Binding in the growth hormone receptor complex. Proc Natl Acad Sci USA. 93:1996;1-6.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 49
    • 0028913816 scopus 로고
    • Ligands for the T-cell receptor: Hard times for avidity models
    • Janeway CA. Ligands for the T-cell receptor: hard times for avidity models. Immunol Today. 16:1995;223-225.
    • (1995) Immunol Today , vol.16 , pp. 223-225
    • Janeway, C.A.1
  • 50
    • 0030176270 scopus 로고    scopus 로고
    • Evidence that a single peptide-MHC complex on a target cell can elicit a cytolytic T cell response
    • Sykulev Y, Joo M, Vturina I, Tsomides TJ, Eisen HN. Evidence that a single peptide-MHC complex on a target cell can elicit a cytolytic T cell response. Immunity. 4:1996;565-571.
    • (1996) Immunity , vol.4 , pp. 565-571
    • Sykulev, Y.1    Joo, M.2    Vturina, I.3    Tsomides, T.J.4    Eisen, H.N.5
  • 51
    • 0025182003 scopus 로고
    • The minimal number of class II MHC-antigen complexes needed for T cell activation
    • Demotz S, Grey H, Sette A. The minimal number of class II MHC-antigen complexes needed for T cell activation. Science. 249:1990;1028-1030.
    • (1990) Science , vol.249 , pp. 1028-1030
    • Demotz, S.1    Grey, H.2    Sette, A.3
  • 52
    • 0025741031 scopus 로고
    • Peptide binding to class I MHC on living cells and quantitation of complexes required for CTL lysis
    • Christinck E, Luscher M, Barber B, Williams D. Peptide binding to class I MHC on living cells and quantitation of complexes required for CTL lysis. Nature. 352:1991;62-70.
    • (1991) Nature , vol.352 , pp. 62-70
    • Christinck, E.1    Luscher, M.2    Barber, B.3    Williams, D.4
  • 54
    • 0028961573 scopus 로고
    • Sustained signaling leading to T cell activation results from prolonged TCR occupancy. Role of T cell actin cytoskeleton
    • Valitutti S, Dessing M, Aktories K, Gallati H, Lanzavecchia A. Sustained signaling leading to T cell activation results from prolonged TCR occupancy. Role of T cell actin cytoskeleton. J Exp Med. 181:1995;577-584.
    • (1995) J Exp Med , vol.181 , pp. 577-584
    • Valitutti, S.1    Dessing, M.2    Aktories, K.3    Gallati, H.4    Lanzavecchia, A.5
  • 55
    • 0026443849 scopus 로고
    • Adaptive cellular interactions in the immune system: The tunable activation threshold and the significance of subthreshold responses
    • Grossman Z, Paul WE. Adaptive cellular interactions in the immune system: the tunable activation threshold and the significance of subthreshold responses. Proc Natl Acad Sci USA. 89:1992;10365-10369.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10365-10369
    • Grossman, Z.1    Paul, W.E.2
  • 56
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • of outstanding interest. An exhaustive review on protein folding and development of convincing arguments in favor of energy landscape models.
    • Dill KA, Chan HS. From Levinthal to pathways to funnels. of outstanding interest Nat Struct Biol. 4:1997;10-19 An exhaustive review on protein folding and development of convincing arguments in favor of energy landscape models.
    • (1997) Nat Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2


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