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Germain RN, Margulies DH. The biochemistry and cell biology of antigen processing and presentation. Annu Rev Immunol. 11:1993;403-450.
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Germain, R.N.1
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MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
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Germain RN. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell. 76:1994;287-299.
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Germain, R.N.1
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0028943275
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The three-dimensional structure of peptide-MHC complexes
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Madden, D.R.1
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4
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0029417003
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Crystal structure of the V alpha domain of a T cell antigen receptor
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Fields BA, Ober B, Malchiodi EL, Lebedeva MI, Braden BC, Ysem X, Kim JK, Shao X, Ward ES, Mariuzza RA. Crystal structure of the V alpha domain of a T cell antigen receptor. Science. 270:1995;1821-1824.
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Fields, B.A.1
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Ysem, X.6
Kim, J.K.7
Shao, X.8
Ward, E.S.9
Mariuzza, R.A.10
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5
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0028956603
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Crystal structure of the beta chain of a T cell antigen receptor
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of outstanding interest. The first high resolution crystallographic structure of a TCR fragment.
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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.
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Science
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Bentley, G.A.1
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Karjalainen, K.3
Mariuzza, R.A.4
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6
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0029985104
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Crystal structure of a T-cell receptor beta chain complexed with a superantigen
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of special interest. The structure of a TCR-superantigen complex reveals how superantigens can have TCR Vβ specificity.
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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.
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Nature
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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
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7
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0029662223
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An alpha/beta T cell receptor structure at 2.5 Å and its orientation in the TCR-MHC complex
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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.
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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.
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Science
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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
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8
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0029855347
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Structure of the complex between human T-cell receptor, viral peptide and HLA-A2
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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
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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.
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Nature
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Garboczi, D.N.1
Ghosh, P.2
Utz, U.3
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9
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0031020557
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Immunology: Feeling out the receptor
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Padlan EA, Margulies DH. Immunology: feeling out the receptor. Curr Biol. 7:1997;R17-R20.
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Padlan, E.A.1
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10
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0026345967
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Low affinity interaction of peptide-MHC complexes with TCRs
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Matsui K, Boniface JJ, Reay PA, Schild H, Fazekas de St Groth B, Davis MM. Low affinity interaction of peptide-MHC complexes with TCRs. Science. 254:1991;1788-1791.
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Science
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Matsui, K.1
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Fazekas De St Groth, B.5
Davis, M.M.6
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11
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0028120414
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TCR-MHC class I peptide interactions: Affinity, kinetics, and specificity
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Corr M, Slanetz AE, Boyd LF, Jelonek MT, Khilko S, Al-Ramadi BK, Kim YS, Maher SE, Bothwell AL, Margulies DH. TCR-MHC class I peptide interactions: affinity, kinetics, and specificity. Science. 265:1994;946-949.
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Corr, M.1
Slanetz, A.E.2
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Al-Ramadi, B.K.6
Kim, Y.S.7
Maher, S.E.8
Bothwell, A.L.9
Margulies, D.H.10
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13
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0011298312
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The kinetics of binding of peptide/MHC complexes to T-cell receptors: Application of surface plasmon resonance to a low-affinity measurement
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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.
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Boniface, J.J.1
Davis, M.M.2
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14
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0029013301
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Lack of strict correlation of functional sensitization with the apparent affinity of MHC-peptide complexes for the TCR
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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
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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.
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J Immunol
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Al-Ramadi, B.K.1
Jelonek, M.T.2
Boyd, L.F.3
Margulies, D.H.4
Bothwell, A.L.M.5
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15
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0030022868
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Studying interactions involving the T cell antigen receptor by surface plasmon resonance
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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.
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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.
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Curr Opin Immunol
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Margulies, D.H.1
Plaksin, D.2
Khilko, S.N.3
Jelonek, M.T.4
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16
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0031091745
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A three domain TCR is biologically active and specifically stains cell surface MHC-peptide complexes
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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
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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.
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Plaksin, D.1
Polakova, K.2
McPhie, P.3
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17
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0026434554
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Separation of IL-4 production from Th cell proliferation by an altered TCR ligand
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Evavold BD, Allen PM. Separation of IL-4 production from Th cell proliferation by an altered TCR ligand. Science. 252:1991;1308-1310.
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Evavold, B.D.1
Allen, P.M.2
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18
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0026503161
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Antigen analog-major histocompatibility complexes act as antagonists of the TCR
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De Magistris MT, Alexander J, Coggeshall M, Altman A, Gaeta FC, Grey HM, Sette A. Antigen analog-major histocompatibility complexes act as antagonists of the TCR. Cell. 68:1992;625-634.
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De Magistris, M.T.1
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Sette, A.7
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19
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0025721116
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The molecular basis of class II MHC allelic control of T cell responses
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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.
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Racioppi, L.1
Ronchese, F.2
Schwartz, R.H.3
Germain, R.N.4
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20
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0028801774
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The T-cell receptor as a diverse signal transduction machine
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Germain RN, Levine EH, Madrenas J. The T-cell receptor as a diverse signal transduction machine. Res Trends. 3:(4):1995;113-121.
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Germain, R.N.1
Levine, E.H.2
Madrenas, J.3
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21
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0003104975
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A TCR binds to antagonist ligands with lower affinities and faster dissociation rates than to agonists
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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.
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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.
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Immunity
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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
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22
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0030014002
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TCR affinity and thymocyte positive selection
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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.
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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.
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Nature
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Alam, S.M.1
Travers, P.J.2
Wung, J.L.3
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Jameson, S.C.6
Gascoigne, N.R.J.7
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23
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0028797801
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CD8 modulation of T-cell antigen receptor-ligand interactions on living cytotoxic T lymphocytes
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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.
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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.
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(1995)
Nature
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Luescher, I.F.1
Vivier, E.2
Layer, A.3
Mahiou, J.4
Godeau, F.5
Malissen, B.6
Romero, P.7
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24
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0029807351
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CD8 enhances formation of stable T-cell receptor/MHC class I molecule complexes
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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
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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.
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Nature
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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
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25
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0030008145
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Variant TCR ligands: New insights into the molecular basis of antigen-dependent signal transduction and T-cell activation
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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.
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Semin Immunol
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Madrenas, J.1
Germain, R.N.2
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26
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0027967385
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Partial T cell signaling: Altered phospho-zeta and lack of zap70 recruitment in APL-induced T cell energy
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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.
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Sloan-Lancaster, J.1
Shaw, A.S.2
Rothbard, J.B.3
Allen, P.M.4
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27
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0028902752
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Zeta phosphorylation without ZAP-70 activation induced by TCR antagonists or partial agonists
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of outstanding interest. Clear demonstration of distinct phosphorylation patterns due to agonist as compared to antagonist or partial agonist MHC - peptide ligands.
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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.
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Science
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Madrenas, J.1
Wange, R.L.2
Wang, J.L.3
Isakov, N.4
Samelson, L.E.5
Germain, R.N.6
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28
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0029810397
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Early biochemical signals arise from low affinity TCR-ligand reactions at the cell-cell interface
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Beeson C, Rabinowitz J, Tate K, Gutgemann I, Chien YH, Jones PP, Davis MM, McConnell HM. Early biochemical signals arise from low affinity TCR-ligand reactions at the cell-cell interface. J Exp Med. 184:1996;777-782.
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Beeson, C.1
Rabinowitz, J.2
Tate, K.3
Gutgemann, I.4
Chien, Y.H.5
Jones, P.P.6
Davis, M.M.7
McConnell, H.M.8
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29
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0029037210
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Serial triggering of many T-cell receptors by a few peptide-MHC complexes
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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.
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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.
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Nature
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Valitutti, S.1
Muller, S.2
Cella, M.3
Padovan, E.4
Lanzavecchia, A.5
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30
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0029063148
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Kinetic proofreading in T-cell receptor signal transduction
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of outstanding interest. Elaboration of the kinetic proofreading model as applied to TCR signaling.
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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.
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McKeithan, T.W.1
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31
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0029855923
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Tuning of activation thresholds explains flexibility in the selection and development of T cells in the thymus
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of special interest. Refinement of the tuning of activation threshold model and its application to thymic selection and development.
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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.
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Grossman, Z.1
Singer, A.2
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Kinetic discrimination in T-cell activation
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of special interest. A refined kinetic proofreading model to account for inhibitory signals.
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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.
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Rabinowitz, J.D.1
Beeson, C.2
Lyons, D.S.3
Davis, M.M.4
McConnell, H.M.5
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Signal transduction mediated by the T-cell antigen receptor
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Isakov, N.3
Ota, Y.4
Wange, R.L.5
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The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction
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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.
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Annu Rev Immunol
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Chan, A.C.1
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0027977974
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Transient intercellular adhesion: The importance of weak protein-protein interactions
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0030061494
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Visualization of CD2 interaction with LFA-3 and determination of the two-dimensional dissociation constant for adhesion receptors in a contact area
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of outstanding interest. Use of fluorescence microscopy to visualize and quantitate accessory molecule interactions at the cell - cell interface.
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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.
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Dustin, M.L.1
Ferguson, L.M.2
Chan, P.Y.3
Springer, T.A.4
Golan, D.E.5
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39
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0030292822
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A motif within the TCR alpha chain constant region connecting peptide domain controls antigen responsiveness
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of special interest. Identification of a region in the TCR α chain constant domain that is critically involved in signal transduction.
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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.
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Immunity
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Backstrom, B.T.1
Milia, E.2
Peter, A.3
Jaureguiberry, B.4
Baldari, C.T.5
Palmer, E.6
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Weissman AM. The T-cell antigen receptor: a multisubunit signaling complex. Chem Immunol. 59:1994;1-18.
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Fremont DH, Rees WA, Kozono H. Biophysical studies of T-cell receptors and their ligands. Curr Opin Immunol. 8:1996;93-100.
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Kinetics and affinity of reactions between an antigen-specific TCR and peptide-MHC complexes
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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.
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44
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0030070499
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