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Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences
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+ T-cell clones deficient in the expression of the CD45 protein tyrosine phosphatase have impaired responses to T-cell receptor stimuli
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Weaver1
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CD45-negative mutants of a rat natural killer cell line fail to lyse tumor target cells
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Bell1
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CD45 cell surface antigens are linked to stimulation of early human myeloid progenitor cells by interleukin 3 (IL-3), granulocyte/macrophage colony-stimulating factor (GM-CSF), a GM-CSF/IL-3 fusion protein, and mast cell growth factor (a c-kit ligand)
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12
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0028358822
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Leukocyte common antigen (CD45) is required for immunoglobulin E-mediated degradulation of mast cells
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Further characterization of CD45-deficient mice demonstrating that CD45 is also required for FceRI function.
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Berger1
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19
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0027389272
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CD45 specifically modulates binding of Lck to a phosphopeptide encompassing the negative regulatory tyrosine of Lck
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lck in the CD45-deficient jurkat line.
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Sieh1
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fyn couples the T cell antigen receptor to pathways of diacylglycerol production, protein kinase C activation and calcium influx
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Differential effects of expression of the CD45 tyrosine protein phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src tyrosine protein kinases
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Hurley1
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23
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0028339795
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CD45 regulation of tyrosine phosphorylation and enzyme activity of src family kinases
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lck in the CD45-deficient YAC-1 cell line.
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Burns1
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25
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0027997103
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Specific interaction of the CD45 protein-tyrosine phosphatase with tyrosine-phosphorylated CD3 ζ chain
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edn 1, Provides evidence that the tyrosyl-phosphorylated TCR ζ-chain is a substrate for CD45.
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Furukawa1
Itoh2
Krueger3
Streuli4
Saito5
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26
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0027992975
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CD45 tyrosine phosphatase activity and membrane anchoring are required for T-cell antigen receptor signaling
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Demonstrates that catalytic domains of CD45 need to be localized to the membrane for CD45 to regulate signaling through the TCR. With the data presented in [65•], demonstrates that the catalytic activity of the first protein tyrosine phosphatase (PTPase) domain is necessary and sufficient for CD45 function. Thus, if the second domain does have minimal PTPase activity, it is not required for regulation of the TCR.
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Niklinska1
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Ashwell5
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27
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0027266773
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Ligand-mediated negative regulation of a chimeric transmembrane receptor tyrosine phosphatase
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Uses a chimeric molecule consisting of the epidermal growth factor receptor extracellular and transmembrane domain and the CD45 cytoplasmic domain to rescue CD45-deficient HPB.ALL cells. Along with the data presented in [28••,29••], demonstrates that the CD45 extracellular domain is not required for TCR signaling when the TCR is cross-linked with antibodies. Supports the idea that the activity of the phosphatase domains is not increased by interactions of the extracellular domain. Dimerization of the chimeric receptor with epidermal growth factor inhibits TCR-mediated signaling.
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0027254049
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Rescue of signaling by a chimeric protein containing the cytoplasmic domain of CD45
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Expression of a chimeric protein consisting of MHC class I extracellular and transmembrane regions, and CD45 cytoplasmic domain rescues TCR signaling in CD45-deficient Jurkat cells.
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Hovis1
Donovan2
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Koretzky7
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29
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0027289547
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Regulation of TCR signaling by CD45 lacking transmembrane and extracellular domains
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c-src that contains the sequences for myristylation (and thus membrane localization) and CD45-cytoplasmic domain rescues TCR signaling in the CD45-deficient YAC-1 cell line.
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Volarevic1
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0028206504
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Thymic CD45 tyrosine phosphatase regulates apoptosis and MHC-restricted negative selection
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Development of transgenic mice that overexpress the low molecular weight CD45 isoform (CD45RO or CD45θ) in the thymus results in a 40–60% reduction in thymocyte number and implicates CD45 in the regulation of apoptosis.
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Ong1
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31
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0028058008
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Specific CD45 isoforms differentially regulate T cell receptor signaling
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Comparison of signal transduction from thymocyte populations of transgenic animals that either expressed the low molecular weight CD45 isoform (CD45RO or CD45θ) or the high molecular weight CD45 isoform (CD45RABC or CD45α) suggests that there is differential signaling with different CD45 isoforms.
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0028426282
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Isoforms of the transmembrane tyrosine phosphatase CD45 differentially affect T cell recognition
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Transfection of components of the TCR with different CD45 isoforms in a thymoma line resulted in differential ability to respond to antigen when CD4 was also expressed. These data suggest that the signaling capability of the TCR is dependent upon the CD45 isoform expressed.
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Novak1
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The cell and molecular basis of leukocyte common antigen (CD45)-triggered, lymphocyte function-associated antigen-1-/intercellular adhesion molecule-1-dependent, leukocyte adhesion
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40
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CD45 mAb induces cell adhesion in peripheral blood mononuclear cells via lymphocyte function-associated antigen-1 (LFA-1) and intercellular cell adhesion molecule 1 (ICAM-1)
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Regulation of the tyrosine kinase-dependent adhesion pathway in human lymphocytes through CD45
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42
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Administration of anti-CD45 mAb specific for a B cell-restricted epitope abrogates the B cell response to a T-dependent antigen in vivo
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Domiati-Saad1
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43
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Sialylation of the B lymphocyte molecule CD22 by α2,6-sialtransferase is implicated in the regulation of CD22-mediated adhesion
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49
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Mac-1 (CD11b/CD18) and CD45 mediate the adhesion of hematopoietic progenitor cells to stromal cell elements via recognition of stromal heparan sulfate
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Coombe1
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50
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0027499881
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CD45-associated kinase activity requires lck but not T cell receptor expression in the Jurkat T cell line
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Koretzky1
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52
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Evidence for monomeric and dimeric forms of CD45 associated with a 30-kDa phosphorylated protein
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Takeda1
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55
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0028049470
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Molecular cloning of the CD45-associated 30-kDa protein
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Characterization of a mouse cDNA clone that encodes a protein that associates with CD45. The cDNA is the apparent species homologue to the cDNA reported in [54•].
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Takeda1
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58
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0026806918
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Tyrosine phosphatase activity of lymphoma CD45 (GP180) is regulated by a direct interaction with the cytoskeleton
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Lokeshwar1
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61
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0028036692
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Mapping the fodrin binding domain in CD45, a leukocyte membrane-associated tyrosine phosphatase
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Identifies the site within the CD45 cytoplasmic domain that interacts with fodrin.
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Iida1
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62
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Negative regulation of CD45 protein tyrosine phosphatase activity by ionomycin in T cells
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Science
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Ostergaard1
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63
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0028017607
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Protein-tyrosine phosphatase activity of CD45 is activated by sequential phosphorylation by two kinases
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Demonstrates mthat tyrosine phosphorylation of CD45, followed by serine phosphorylation by casein kinase II, results in an increase in CD45 phosphatase activity.
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Stover1
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0027399347
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Demonstration of protein tyrosine phosphatase activity in the second domain of two homologous domains of CD45
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Tan1
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65
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0027981910
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The catalytic activity of the CD45 membrane-proximal phosphatase domain is required for TCR signaling and regulation
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Demonstrates that the catalytic activity of the first protein tyrosine phosphatase domain in CD45 is necessary and sufficient to rescue TCR signal transduction in CD45-deficient HPB.ALL cells.
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EMBO J
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Desai1
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67
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0025277449
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Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR
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Streuli1
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68
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0027531637
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SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases
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Feng1
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71
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Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosphila corkscrew
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Freeman1
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73
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0026630991
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corkscrew encodes a putative protein tyrosine phosphatase that functions to transduce the terminal signal from the receptor tyrosine kinase torso
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Perkins1
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76
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0028342948
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SH-PTP2/Syp SH2 domain binding specificity is defined by direct interactions with platelet-derived growth factor β-receptor, epidermal growth factor receptor, and insulin receptor substrate-1-derived phosphopeptides
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Case1
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84
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0027179869
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The 64-kDa protein that associates with the platelet-derived grwoth factor receptor β subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase
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Kazlauskas1
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Tyrosyl phosphorylation and growth factor receptor association of the human corkscrew homologue, SH-PTP2
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Perrimon1
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88
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0027197067
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Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene
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Together with the results presented in [89••], demonstratres that the molecular defect in the motheaten and motheaten variable mice is a mutation within the SHP gene that renders the mice deficient in SHP protein expression. Implicates SHP in the negative regulation of leukocyte activation.
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Shultz1
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89
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0027195626
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Motheaten and viable motheaten mice have mutations in the haematopoietic cell phosphatase gene
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Characterizes the genetic defect in me and mev mice and demonstrates point mutations within the SHP gene.
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Tsui1
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90
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0027488637
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Hematopoietic cell phosphatase associates with the interleukin-3 (IL-3) receptor β chain and down-regulates IL-3 induced tyrosine phosphorylation and mitogenesis
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Demonstrates that overexpression of anti-sense SHP cDNA results in the increased proliferation of an IL-3-dependent cell line in response to IL-3.
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Yi1
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91
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0027280226
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Association of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand
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Yi1
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92
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0028961264
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Protein tyrosine phosphatase 1C negatively regulates antigen receptor signaling in B lymphocytes and determines thresholds for negative selection
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In bone marrow chimeric animals in which the donor cells are of mev origin, B cells that contain a transgene coding for an antibody to hen egg lysozyme are more sensitive to B-cell receptor signal transduction and have a lower threshold for deletion in response to antigen. Implicates SHP in the negative regulation of the B-cell receptor.
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Cyster1
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94
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0028322113
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Purification and characterization of PTP2C, a widely distributed protein tyrosine phosphatase containing two SH2 domains
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Zhao1
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96
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0027404080
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Overexpression, purification, and characterization of SHPTP1, Src homology 2-containing protein-tyrosine-phosphatase
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Pei1
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100
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0028580116
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Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology domains
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Demonstrates that phopshotyrosyl peptides that interact with the SH2 domains markedly activate the catalytic domain. The data suggest that the catalytic activity of SHP is regulated by an allosteric mechanism.
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Pei1
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101
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0028282967
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Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1
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Sugimoto1
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Neel4
Walsh5
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