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1
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0028064781
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Temporal regulation of non-transmembrane protein tyrosine kinase enzyme activity following T cell antigen receptor engagement
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Burkhardt AL, Stealey B, Rowley RB, Mahajan S, Prendergast M, Fargnoli J, Bolen JB. Temporal regulation of non-transmembrane protein tyrosine kinase enzyme activity following T cell antigen receptor engagement. J Biol Chem. 269:1994;23642-23647.
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(1994)
J Biol Chem.
, vol.269
, pp. 23642-23647
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Burkhardt, A.L.1
Stealey, B.2
Rowley, R.B.3
Mahajan, S.4
Prendergast, M.5
Fargnoli, J.6
Bolen, J.B.7
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2
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0028209548
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Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases
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of outstanding interest. This paper was the first to demonstrate that ZAP-70 SH2 domains bind to the dp- but not the unphosphorylated ITAM. This data suggested that an ordered sequence of events occurs during T-cell activation.
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Iwashima M, Irving BA, Van Oers N, Chan AC, Weiss A. Sequential interactions of the TCR with two distinct cytoplasmic tyrosine kinases. of outstanding interest Science. 263:1994;1136-1139 This paper was the first to demonstrate that ZAP-70 SH2 domains bind to the dp- but not the unphosphorylated ITAM. This data suggested that an ordered sequence of events occurs during T-cell activation.
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(1994)
Science
, vol.263
, pp. 1136-1139
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Iwashima, M.1
Irving, B.A.2
Van Oers, N.3
Chan, A.C.4
Weiss, A.5
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3
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0028942111
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ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: The tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity
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of special interest. Using competitive inhibition, the authors analyze the binding affinity of the ZAP-70 SH2 domains towards a panel of TCR ITAM peptides. They demonstrate that both SH2 domains and phosphorylated tyrosines are required for binding.
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Isakov N, Wange RL, Burgess WH, Watts JD, Aebersold R, Samelson LE. ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity. of special interest J Exp Med. 181:1995;375-380 Using competitive inhibition, the authors analyze the binding affinity of the ZAP-70 SH2 domains towards a panel of TCR ITAM peptides. They demonstrate that both SH2 domains and phosphorylated tyrosines are required for binding.
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(1995)
J Exp Med.
, vol.181
, pp. 375-380
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-
Isakov, N.1
Wange, R.L.2
Burgess, W.H.3
Watts, J.D.4
Aebersold, R.5
Samelson, L.E.6
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4
-
-
0028231891
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Delineation of a T-cell activation motif required for binding of protein tyrosine kinases containing tandem SH2 domains
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Koyasu S, Tse AG, Moingeon P, Hussey RE, Mildonian A, Hannisian J, Clayton LK, Reinherz EL. Delineation of a T-cell activation motif required for binding of protein tyrosine kinases containing tandem SH2 domains. Proc Natl Acad Sci USA. 91:1994;6693-6697.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 6693-6697
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Koyasu, S.1
Tse, A.G.2
Moingeon, P.3
Hussey, R.E.4
Mildonian, A.5
Hannisian, J.6
Clayton, L.K.7
Reinherz, E.L.8
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5
-
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0028176584
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Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: Defining the nature of a signaling motif
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of special interest. The authors analyze the ability of the ITAM to directly bind Src kinases, as well as ZAP-70, p59fyn, but not p56lck, could bind directly to the ITAM but the binding did not require any of the conserved features of the ITAM. In contrast, ZAP-70 binding to the ITAM required prior tyrosine phosphorylation as well as all of the conserved features of the ITAM.
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Gauen LK, Zhu Y, Letourneur F, Hu Q, Bolen JB, Matis LA, Klausner RD, Shaw AS. Interactions of p59fyn and ZAP-70 with T-cell receptor activation motifs: defining the nature of a signaling motif. of special interest Mol Cell Biol. 14:1994;3729-3741 The authors analyze the ability of the ITAM to directly bind Src kinases, as well as ZAP-70, p59fyn, but not p56lck, could bind directly to the ITAM but the binding did not require any of the conserved features of the ITAM. In contrast, ZAP-70 binding to the ITAM required prior tyrosine phosphorylation as well as all of the conserved features of the ITAM.
-
(1994)
Mol Cell Biol.
, vol.14
, pp. 3729-3741
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-
Gauen, L.K.1
Zhu, Y.2
Letourneur, F.3
Hu, Q.4
Bolen, J.B.5
Matis, L.A.6
Klausner, R.D.7
Shaw, A.S.8
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6
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0029063151
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Analysis of the interaction of ZAP-70 and syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance
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of special interest. Using surface plasmon resonance, the authors measured the affinity of the single and tandem SH2 domains of ZAP-70 and Syk towards a panel of phosphorylated and unphosphorylated ITAM peptides. They demonstrate that both phosphorylated tyrosines, as well as both SH2 domains, are required for high-affinity binding.
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Bu JY, Shaw AS, Chan AC. Analysis of the interaction of ZAP-70 and syk protein-tyrosine kinases with the T-cell antigen receptor by plasmon resonance. of special interest Proc Natl Acad Sci USA. 92:1995;5106-5110 Using surface plasmon resonance, the authors measured the affinity of the single and tandem SH2 domains of ZAP-70 and Syk towards a panel of phosphorylated and unphosphorylated ITAM peptides. They demonstrate that both phosphorylated tyrosines, as well as both SH2 domains, are required for high-affinity binding.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 5106-5110
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Bu, J.Y.1
Shaw, A.S.2
Chan, A.C.3
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7
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0029076731
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Reconstitution of Syk function by the ZAP-70 protein tyrosine kinase
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of special interest. The authors demonstrate that ZAP-70 and Syk are functionally homologous. In addition, the authors study lymphocytes to provide functional evidence that both SH2 domains, as well as the catalytic activity of ZAP-70, are required for efficient antigen-receptor function.
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Kong GH, Bu JY, Kurosaki T, Shaw AS, Chan AC. Reconstitution of Syk function by the ZAP-70 protein tyrosine kinase. of special interest Immunity. 2:1995;485-492 The authors demonstrate that ZAP-70 and Syk are functionally homologous. In addition, the authors study lymphocytes to provide functional evidence that both SH2 domains, as well as the catalytic activity of ZAP-70, are required for efficient antigen-receptor function.
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(1995)
Immunity
, vol.2
, pp. 485-492
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Kong, G.H.1
Bu, J.Y.2
Kurosaki, T.3
Shaw, A.S.4
Chan, A.C.5
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8
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0028783396
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Role of Syk autophosphorylation site and SH2 domains in B cell antigen receptor function
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of special interest. The authors provide functional evidence that both SH2 domains of Syk are required for efficient BCR function.
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Kurosaki T, Johnson SA, Pao L, Sada K, Yamamura H, Cambier JC. Role of Syk autophosphorylation site and SH2 domains in B cell antigen receptor function. of special interest J Exp Med. 182:1996;1815-1821 The authors provide functional evidence that both SH2 domains of Syk are required for efficient BCR function.
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(1996)
J Exp Med.
, vol.182
, pp. 1815-1821
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Kurosaki, T.1
Johnson, S.A.2
Pao, L.3
Sada, K.4
Yamamura, H.5
Cambier, J.C.6
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9
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0028985602
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F2(Pmp)2-TAM zeta 3, a novel competitive inhibitor of the binding of ZAP-70 to the T cell antigen receptor, blocks early T cell signaling
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Wange RL, Isakov N, Burke TJ, Otaka A, Roller PP, Watts JD, Aebersold R, Samelson LE. F2(Pmp)2-TAM zeta 3, a novel competitive inhibitor of the binding of ZAP-70 to the T cell antigen receptor, blocks early T cell signaling. J Biol Chem. 270:1995;944-948.
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(1995)
J Biol Chem.
, vol.270
, pp. 944-948
-
-
Wange, R.L.1
Isakov, N.2
Burke, T.J.3
Otaka, A.4
Roller, P.P.5
Watts, J.D.6
Aebersold, R.7
Samelson, L.E.8
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10
-
-
84988043558
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Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor
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of special interest. The authors provide the first characterization of a structure containing dual SH2 domains binding a dp-ITAM.
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Hatada MH, Lu X, Laird ER, Green J, Morgenstern JP, Lou M, Marr CS, Phillips RB, Ram MK, Teriault K, et al. Molecular basis for interaction of the protein tyrosine kinase ZAP-70 with the T-cell receptor. of special interest Nature. 376:1995;32-38 The authors provide the first characterization of a structure containing dual SH2 domains binding a dp-ITAM.
-
(1995)
Nature
, vol.376
, pp. 32-38
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-
Hatada, M.H.1
Lu, X.2
Laird, E.R.3
Green, J.4
Morgenstern, J.P.5
Lou, M.6
Marr, C.S.7
Phillips, R.B.8
Ram, M.K.9
Teriault, K.10
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11
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0028304998
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Association of phosphatidylinositol 3-kinase with a specific sequence of the T cell receptor zeta chain is dependent on T cell activation
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Exley M, Varticovski L, Peter M, Sancho J, Terhorst C. Association of phosphatidylinositol 3-kinase with a specific sequence of the T cell receptor zeta chain is dependent on T cell activation. J Biol Chem. 269:1994;15140-15146.
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(1994)
J Biol Chem.
, vol.269
, pp. 15140-15146
-
-
Exley, M.1
Varticovski, L.2
Peter, M.3
Sancho, J.4
Terhorst, C.5
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12
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0029072239
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A comparison of the interaction of Shc and the tyrosine kinase ZAP-70 with the T cell antigen receptor zeta chain tyrosine-based activation motif
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Osman N, Lucas SC, Turner H, Cantrell D. A comparison of the interaction of Shc and the tyrosine kinase ZAP-70 with the T cell antigen receptor zeta chain tyrosine-based activation motif. J Biol Chem. 270:1995;13981-13986.
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(1995)
J Biol Chem.
, vol.270
, pp. 13981-13986
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-
Osman, N.1
Lucas, S.C.2
Turner, H.3
Cantrell, D.4
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13
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0027998862
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Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor
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Jouvin MH, Adamczewski M, Numerof R, Letourneur O, Valle A, Kinet JP. Differential control of the tyrosine kinases Lyn and Syk by the two signaling chains of the high affinity immunoglobulin E receptor. J Biol Chem. 269:1994;5918-5925.
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(1994)
J Biol Chem.
, vol.269
, pp. 5918-5925
-
-
Jouvin, M.H.1
Adamczewski, M.2
Numerof, R.3
Letourneur, O.4
Valle, A.5
Kinet, J.P.6
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14
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0028793187
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Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate lyn and syk tyrosine kinases
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of special interest. The authors demonstrate the binding of Src kinases to the phosphorylated ITAM activates their kinase activity.
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Johnson SA, Pleiman CM, Pao L, Schneringer J, Hippen K, Cambier JC. Phosphorylated immunoreceptor signaling motifs (ITAMs) exhibit unique abilities to bind and activate lyn and syk tyrosine kinases. of special interest J Immunol. 155:1995;4596-4603 The authors demonstrate the binding of Src kinases to the phosphorylated ITAM activates their kinase activity.
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(1995)
J Immunol.
, vol.155
, pp. 4596-4603
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Johnson, S.A.1
Pleiman, C.M.2
Pao, L.3
Schneringer, J.4
Hippen, K.5
Cambier, J.C.6
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15
-
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0028902765
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Signals through T cell receptor-zeta chain alone are insufficient to prime resting T lymphocytes
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Brocker T, Karjalainen K. Signals through T cell receptor-zeta chain alone are insufficient to prime resting T lymphocytes. J Exp Med. 181:1995;1653-1659.
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(1995)
J Exp Med.
, vol.181
, pp. 1653-1659
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Brocker, T.1
Karjalainen, K.2
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16
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0028051551
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Role of TCR zeta chain in T cell development and selection
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of special interest. This elegant study analyzed whether any of the ζ-chain ITAMs contribute an unique function in thymocyte development and TCR activation in a biologically relevant system.
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Shores EW, Huang K, Tran T, Lee E, Grinberg A, Love PE. Role of TCR zeta chain in T cell development and selection. of special interest Science. 266:1994;1047-1050 This elegant study analyzed whether any of the ζ-chain ITAMs contribute an unique function in thymocyte development and TCR activation in a biologically relevant system.
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(1994)
Science
, vol.266
, pp. 1047-1050
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-
Shores, E.W.1
Huang, K.2
Tran, T.3
Lee, E.4
Grinberg, A.5
Love, P.E.6
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17
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0028986925
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CD3 epsilon and CD3 zeta cytoplasmic domains can independently generate signals for T cell development and function
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Shinkai Y, Ma A, Cheng HL, Alt FW. CD3 epsilon and CD3 zeta cytoplasmic domains can independently generate signals for T cell development and function. Immunity. 2:1995;401-411.
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(1995)
Immunity
, vol.2
, pp. 401-411
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Shinkai, Y.1
Ma, A.2
Cheng, H.L.3
Alt, F.W.4
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18
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0029045870
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Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering
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of outstanding interest. Using recombinant vaccinia viruses that express IgE receptor, lyn and Syk, the authors reconstitute the early events of AgR signaling in fibroblast cells. They demonstrate that expression of lyn is required for phosphorylation of ITAM and binding of Syk.
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Scharenberg AM, Lin S, Cuenod B, Yamamura H, Kinet JP. Reconstitution of interactions between tyrosine kinases and the high affinity IgE receptor which are controlled by receptor clustering. of outstanding interest EMBO J. 14:1995;3385-3394 Using recombinant vaccinia viruses that express IgE receptor, lyn and Syk, the authors reconstitute the early events of AgR signaling in fibroblast cells. They demonstrate that expression of lyn is required for phosphorylation of ITAM and binding of Syk.
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(1995)
EMBO J
, vol.14
, pp. 3385-3394
-
-
Scharenberg, A.M.1
Lin, S.2
Cuenod, B.3
Yamamura, H.4
Kinet, J.P.5
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19
-
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0028176193
-
Distinct p53/56lyn and p59fyn domains associate with nonphosphorylated and phosphorylated Ig-alpha
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Pleiman CM, Abrams C, Gauen LT, Bedzyk W, Jongstra J, Shaw AS, Cambier JC. Distinct p53/56lyn and p59fyn domains associate with nonphosphorylated and phosphorylated Ig-alpha. Proc Natl Acad Sci USA. 91:1994;4268-4272.
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(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 4268-4272
-
-
Pleiman, C.M.1
Abrams, C.2
Gauen, L.T.3
Bedzyk, W.4
Jongstra, J.5
Shaw, A.S.6
Cambier, J.C.7
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20
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0030162958
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Multiple features of the p59fyn SH4 domain define a motif for ITAM binding and for plasma membrane localization
-
in press
-
in press Gauen LT, Linder ME, Shaw AS. Multiple features of the p59fyn SH4 domain define a motif for ITAM binding and for plasma membrane localization. J Cell Biol. 1996.
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(1996)
J Cell Biol.
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Gauen, L.T.1
Linder, M.E.2
Shaw, A.S.3
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21
-
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0028339767
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Amino acid residues that flank core peptide epitopes and the extracellular domains of CD4 modulate differential signaling through the T cell receptor
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Vignali DA, Strominger JL. Amino acid residues that flank core peptide epitopes and the extracellular domains of CD4 modulate differential signaling through the T cell receptor. J Exp Med. 179:1994;1945-1956.
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(1994)
J Exp Med.
, vol.179
, pp. 1945-1956
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Vignali, D.A.1
Strominger, J.L.2
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22
-
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0027967385
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Partial T cell signaling: Altered phospho-zeta and lack of zep70 recruitment in APL-induced T cell energy
-
of outstanding interest. See annotation [23].
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Sloan-Lancaster J, Shaw AS, Rothbard JB, Allen PM. Partial T cell signaling: altered phospho-zeta and lack of zep70 recruitment in APL-induced T cell energy. of outstanding interest Cell. 79:1994;913-922 See annotation [23].
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(1994)
Cell.
, vol.79
, pp. 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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23
-
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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. This paper and [22] analyze AgR signaling by altered-peptide ligands that lead to anergy of T cells. The authors demonstrate the provocative finding that anergic stimuli lead to altered phosphorylation TCR ζ chain. No tyrosine phosphorylation or activation of ZAP-70 is detected even though it is recruited to the TCR.
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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 This paper and [22] analyze AgR signaling by altered-peptide ligands that lead to anergy of T cells. The authors demonstrate the provocative finding that anergic stimuli lead to altered phosphorylation TCR ζ chain. No tyrosine phosphorylation or activation of ZAP-70 is detected even though it is recruited to the TCR.
-
(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
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24
-
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0028535120
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ZAP-70 is constitutively associated with tyrosine-phosphorylated TCR zeta in murine thymocytes and lymph node T cells
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of special interest. This paper demonstrates that in both thymocytes and peripheral T cells the TCR is constitutively phosphorylated and that ZAP-70 is constitutively associated with the TCR, but not tyrosine phosphorylated. Moreover, no additional ZAP-70 is recruited to the receptor following TCR cross-linking in both thymocytes and peripheral T cells.
-
Van Oers N, Killeen N, Weiss A. ZAP-70 is constitutively associated with tyrosine-phosphorylated TCR zeta in murine thymocytes and lymph node T cells. of special interest Immunity. 1:1994;675-685 This paper demonstrates that in both thymocytes and peripheral T cells the TCR is constitutively phosphorylated and that ZAP-70 is constitutively associated with the TCR, but not tyrosine phosphorylated. Moreover, no additional ZAP-70 is recruited to the receptor following TCR cross-linking in both thymocytes and peripheral T cells.
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(1994)
Immunity
, vol.1
, pp. 675-685
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Van Oers, N.1
Killeen, N.2
Weiss, A.3
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25
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0027379699
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+ thymocytes by p56Ick tyrosine kinase: Basis for differential signaling by CD4 and CD8 in immature thymocytes expressing both coreceptor molecules
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+ thymocytes by p56Ick tyrosine kinase: basis for differential signaling by CD4 and CD8 in immature thymocytes expressing both coreceptor molecules. J Exp Med. 178:1993;1701-1712.
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(1993)
J Exp Med.
, vol.178
, pp. 1701-1712
-
-
Wiest, D.L.1
Yuan, L.2
Jefferson, J.3
Benveniste, P.4
Tsokos, M.5
Klausner, R.D.6
Glimcher, L.H.7
Samelson, L.E.8
Singer, A.9
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26
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0028176660
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Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity
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Clark MR, Johnson SA, Cambier JC. Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels of binding specificity and tyrosine phosphorylated Ig-alpha stimulation of Fyn activity. EMBO J. 13:1994;1911-1919.
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(1994)
EMBO J
, vol.13
, pp. 1911-1919
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Clark, M.R.1
Johnson, S.A.2
Cambier, J.C.3
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27
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0028125752
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Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor
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of special interest. The authors demonstrate that phosphorylated ITAMs can activate Src PTKs and that an ordered sequence of phsophorylation of the ITAM may occur.
-
Flaswinkel H, Reth M. Dual role of the tyrosine activation motif of the Ig-alpha protein during signal transduction via the B cell antigen receptor. of special interest EMBO J. 13:1994;83-89 The authors demonstrate that phosphorylated ITAMs can activate Src PTKs and that an ordered sequence of phsophorylation of the ITAM may occur.
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(1994)
EMBO J
, vol.13
, pp. 83-89
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-
Flaswinkel, H.1
Reth, M.2
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28
-
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0028905060
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Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE
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of special interest. See annotation [29].
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Shiue L, Zoller MJ, Brugge JS. Syk is activated by phosphotyrosine-containing peptides representing the tyrosine-based activation motifs of the high affinity receptor for IgE. of special interest J Biol Chem. 270:1995;10498-10502 See annotation [29].
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(1995)
J Biol Chem.
, vol.270
, pp. 10498-10502
-
-
Shiue, L.1
Zoller, M.J.2
Brugge, J.S.3
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29
-
-
0029068171
-
Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Igα/Igβ immunoreceptor tyrosine activation motif binding and autophosphorylation
-
of special interest. This paper and [28] demonstrate that the dp-ITAM can activate catalytic activity of Syk.
-
Rowley RB, Burkardt AL, Chao H-G, Matsueda GR, Bolen JB. Syk protein-tyrosine kinase is regulated by tyrosine-phosphorylated Igα/Igβ immunoreceptor tyrosine activation motif binding and autophosphorylation. of special interest J Biol Chem. 270:1995;11590-11594 This paper and [28] demonstrate that the dp-ITAM can activate catalytic activity of Syk.
-
(1995)
J Biol Chem.
, vol.270
, pp. 11590-11594
-
-
Rowley, R.B.1
Burkardt, A.L.2
Chao, H.-G.3
Matsueda, G.R.4
Bolen, J.B.5
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30
-
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0029031806
-
Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins
-
of special interest. In this study, the authors propose that a major substrate of ZAP-70 is itself, and that its recruitment to the TCR complex functions to facilitate its autophosphorylation on tyrosine residues resulting in the generation of a scaffold for the recruitment of SH2 domains. Peptide mapping demonstrated that autophosphorylation generates a large variety of sites that can bind SH2-containing signaling proteins.
-
Neumeister EN, Zhu Y, Richard S, Terhorst C, Chan AC, Shaw AS. Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. of special interest Mol Cell Biol. 15:1995;3171-3178 In this study, the authors propose that a major substrate of ZAP-70 is itself, and that its recruitment to the TCR complex functions to facilitate its autophosphorylation on tyrosine residues resulting in the generation of a scaffold for the recruitment of SH2 domains. Peptide mapping demonstrated that autophosphorylation generates a large variety of sites that can bind SH2-containing signaling proteins.
-
(1995)
Mol Cell Biol.
, vol.15
, pp. 3171-3178
-
-
Neumeister, E.N.1
Zhu, Y.2
Richard, S.3
Terhorst, C.4
Chan, A.C.5
Shaw, A.S.6
-
31
-
-
0029071585
-
Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function
-
of special interest. See annotations [32], [33].
-
Chan AC, Dalton M, Johnson R, Kong GH, Wang T, Thoma R, Kurosaki T. Activation of ZAP-70 kinase activity by phosphorylation of tyrosine 493 is required for lymphocyte antigen receptor function. of special interest EMBO J. 14:1995;2499-2508 See annotations [32], [33].
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(1995)
EMBO J
, vol.14
, pp. 2499-2508
-
-
Chan, A.C.1
Dalton, M.2
Johnson, R.3
Kong, G.H.4
Wang, T.5
Thoma, R.6
Kurosaki, T.7
-
32
-
-
0029151944
-
Activating and inhibitory mutations in adjacent tyrosines in the kinase domain of ZAP-70
-
of outstanding interest. of outstanding interest. This paper and [31] demonstrate that catalytic activation of ZAP-70 is mediated by the phosphorylation of Tyr493 within the trans-activation loop of ZAP-70's catalytic domain. In addition, [31] provides evidence that phosphorylation of this tyrosine residue is required for AgR function.
-
of outstanding interest Wange RL, Guitian R, Isakov N, Watts JD, Aebersold R, Samelson LE. Activating and inhibitory mutations in adjacent tyrosines in the kinase domain of ZAP-70. of outstanding interest J Biol Chem. 270:1995;18730-18733 This paper and [31] demonstrate that catalytic activation of ZAP-70 is mediated by the phosphorylation of Tyr493 within the trans-activation loop of ZAP-70's catalytic domain. In addition, [31] provides evidence that phosphorylation of this tyrosine residue is required for AgR function.
-
(1995)
J Biol Chem.
, vol.270
, pp. 18730-18733
-
-
Wange, R.L.1
Guitian, R.2
Isakov, N.3
Watts, J.D.4
Aebersold, R.5
Samelson, L.E.6
-
33
-
-
0028062116
-
Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70
-
of special interest. of special interest. Together with [31], the authors identify the sites of tyrosine phosphorylation within ZAP-70.
-
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SH3 domains of the adapter molecule Grb2 complex with two proteins in T cells: The guanine nucleotide exchange protein SOS and a 75-kDa protein that is substrate for T cell antigen receptor-activated tyrosine kinases
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43
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0029587597
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Cloning and characterization of Lnk, a signal transduction protein that links T-cell receptor activation signal to phospholipase Cγ 1, Grb2, and phosphatidylinositol 3-kinase
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of special interest. See annotation [46].
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Huang X, Li Y, Tanaka K, Moore KG, Hayashi JI. Cloning and characterization of Lnk, a signal transduction protein that links T-cell receptor activation signal to phospholipase Cγ 1, Grb2, and phosphatidylinositol 3-kinase. of special interest Proc Natl Acad Sci USA. 92:1995;11618-11622 See annotation [46].
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Huang, X.1
Li, Y.2
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44
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Zhang, R.1
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46
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0028956337
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Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav
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of outstanding interest. of outstanding interest. This paper, along with [43-45] demonstrates the functional requirements of vav in lymphocyte development.
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of outstanding interest Tarakhovsky A, Turner M, Schaal S, Mee PJ, Duddy LP, Rajewsky K, Tybulewicz VLJ. Defective antigen receptor-mediated proliferation of B and T cells in the absence of Vav. of outstanding interest Nature. 374:1995;467-470 This paper, along with [43-45] demonstrates the functional requirements of vav in lymphocyte development.
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Tarakhovsky, A.1
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Tyrosine-phosphorylated T cell receptor ζ chain associate with the actin cytoskeleton upon activation of the mature T lymphocytes
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Finkel, T.H.3
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51
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Interactions between the protein tyrosine kinase ZAP-70, the proto-oncogene Vav, and tubulin in Jurkat T cells
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52
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0029063148
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Kinetic proofreading in T-cell receptor signal transduction
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of outstanding interest. A model is proposed in which the multiple layers of regulation present in AgR signal transduction may permit lymphocytes to discriminate antigens that promote or inhibit 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 A model is proposed in which the multiple layers of regulation present in AgR signal transduction may permit lymphocytes to discriminate antigens that promote or inhibit signaling.
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McKeithan, T.W.1
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53
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0028340167
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ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency
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of outstanding interest. See annotation [55].
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Chan AC, Kadlecek TA, Elder ME, Filipovich AH, Kuo WL, Iwashima M, Parslow TG, Weiss A. ZAP-70 deficiency in an autosomal recessive form of severe combined immunodeficiency. of outstanding interest Science. 264:1994;1599-1601 See annotation [55].
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Science
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Chan, A.C.1
Kadlecek, T.A.2
Elder, M.E.3
Filipovich, A.H.4
Kuo, W.L.5
Iwashima, M.6
Parslow, T.G.7
Weiss, A.8
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54
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0028292001
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Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase
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of outstanding interest. See annotation [55].
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Elder ME, Lin D, Clever J, Chan AC, Hope TJ, Weiss A, Parslow TG. Human severe combined immunodeficiency due to a defect in ZAP-70, a T cell tyrosine kinase. of outstanding interest Science. 264:1994;1596-1599 See annotation [55].
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Science
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Elder, M.E.1
Lin, D.2
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Chan, A.C.4
Hope, T.J.5
Weiss, A.6
Parslow, T.G.7
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55
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0028269436
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+ thymic selection in humans lacking zap-70 kinase
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of outstanding interest. This paper, along with [53,54] represents the first observations of the functional significance of ZAP-70 in human TCR activation and thymocyte development.
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+ thymic selection in humans lacking zap-70 kinase. of outstanding interest Cell. 76:1994;947-958 This paper, along with [53,54] represents the first observations of the functional significance of ZAP-70 in human TCR activation and thymocyte development.
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Cell.
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56
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0029087530
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Absence of ZAP-70 prevents signaling through the antigen receptor on peripheral blood T cells but not on thymocytes
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Gelfand EW, Weinberg K, Mazer BD, Kadlecek TA, Weiss A. Absence of ZAP-70 prevents signaling through the antigen receptor on peripheral blood T cells but not on thymocytes. J Exp Med. 182:1995;1057-1065.
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Weiss, A.5
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57
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0029133646
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Essential role for ZAP-70 in both positive and negative selection of thymocytes
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of outstanding interest. The authors demonstrate the functional requirement of ZAP-70 in both positive and negative selection of thymocytes.
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Negishi I, Motoyama N, Nakayama K, Nakayama K, Senju S, Hatakeyama S, Zhang Q, Chan AC, Loh DY. Essential role for ZAP-70 in both positive and negative selection of thymocytes. of outstanding interest Nature. 376:1995;435-438 The authors demonstrate the functional requirement of ZAP-70 in both positive and negative selection of thymocytes.
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Nature
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Negishi, I.1
Motoyama, N.2
Nakayama, K.3
Nakayama, K.4
Senju, S.5
Hatakeyama, S.6
Zhang, Q.7
Chan, A.C.8
Loh, D.Y.9
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58
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0028216232
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Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling
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Chan AC, Van Oers N, Tran A, Turka L, Law CL, Ryan JC, Clark EA, Weiss A. Differential expression of ZAP-70 and Syk protein tyrosine kinases, and the role of this family of protein tyrosine kinases in TCR signaling. J Immunol. 152:1994;4758-4766.
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Chan, A.C.1
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Law, C.L.5
Ryan, J.C.6
Clark, E.A.7
Weiss, A.8
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59
-
-
0028180858
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2+ mobilization through distinct pathways
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of outstanding interest. The authors provide the first functional evidence that Syk and Lyn are both required for BCR activation.
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2+ mobilization through distinct pathways. of outstanding interest EMBO J. 13:1994;1341-1349 The authors provide the first functional evidence that Syk and Lyn are both required for BCR activation.
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EMBO J
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Takata, M.1
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Homma, Y.5
Nukada, T.6
Yamamura, H.7
Kurosaki, T.8
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60
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0028889302
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Perinatal lethality and blocked B-cell development in mice lacking the tyrosine kinase Syk
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of outstanding interest. See annotation [61].
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Turner M, Mee PJ, Costello PS, Williams O, Price AA, Duddy LP, Furlong MT, Geahlen RL, Tybulewicz VLJ. Perinatal lethality and blocked B-cell development in mice lacking the tyrosine kinase Syk. of outstanding interest Nature. 378:1995;298-302 See annotation [61].
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Nature
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Turner, M.1
Mee, P.J.2
Costello, P.S.3
Williams, O.4
Price, A.A.5
Duddy, L.P.6
Furlong, M.T.7
Geahlen, R.L.8
Tybulewicz, V.L.J.9
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61
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0028783322
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Syk tyrosine kinase required for mouse viability and B-cell development
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of outstanding interest. This paper and [60] demonstrate that Syk is required for B-cell development.
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Cheng AM, Rowley RB, Pao W, Hayday A, Bolen JB, Pawson T. Syk tyrosine kinase required for mouse viability and B-cell development. of outstanding interest Nature. 378:1995;303-306 This paper and [60] demonstrate that Syk is required for B-cell development.
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Nature
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-
Cheng, A.M.1
Rowley, R.B.2
Pao, W.3
Hayday, A.4
Bolen, J.B.5
Pawson, T.6
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